@article{2-s2.0-85184913863,

title = {Decomposition of non-steroidal anti-inflammatory drugs by activated sludge supported by biopreparation in sequencing batch reactor},

author = { A. Dzionek and A. Nowak and D. Wojcieszyńska and I.W. Potocka and W. Smułek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85184913863&doi=10.1016%2fj.biortech.2024.130328&partnerID=40&md5=39d790eda0f9fbd9643a4146cbc5c18d},

doi = {10.1016/j.biortech.2024.130328},

issn = {09608524},

year  = {2024},

date = {2024-01-01},

journal = {Bioresource Technology},

volume = {395},

publisher = {Elsevier Ltd},

abstract = {The presence of non-steroidal anti-inflammatory drugs in wastewater from sewage treatment plants indicates that they are not completely biodegradable. The designed biopreparation based on immobilized bacteria enables the degradation of paracetamol, ibuprofen, naproxen and diclofenac at a rate of 0.50 mg/L*day, 0.14 mg/L*day, 0.16 mg/L*day and 0.04 mg/L*day, respectively. Lower degradation of drugs in the mixture than in monosubstrate systems indicates their additive, antagonistic effect, limiting the degradative capacity of microorganisms. The biopreparation is stable for at least 6 weeks in bioreactor conditions. Biochemical parameters of activated sludge functioning showed increased oxygen demand, which was related to increased ammonia concentration caused by long-term exposure of activated sludge to drugs. Reduced metabolic activity was also observed. The preparation enables decomposing drugs and their metabolites, restoring the activated sludge's functionality. The tested biopreparation can support activated sludge in sewage treatment plants in degrading non-steroidal anti-inflammatory drugs and phenolic compounds. © 2024 Elsevier Ltd},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85181777064,

title = {Naproxen as environmental pollution, its effect on bacteria metabolism and degradation mechanism in immobilized Planococcus sp. S5},

author = { A. Dzionek and D. Wojcieszyńska and A. Marchlewicz and W. Smułek and I.W. Potocka and Ł. Jałowiecki and J. Borgulat and G.A. Płaza and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85181777064&doi=10.1016%2fj.cej.2023.148174&partnerID=40&md5=899216654a60c6867293bebad6864093},

doi = {10.1016/j.cej.2023.148174},

issn = {13858947},

year  = {2024},

date = {2024-01-01},

journal = {Chemical Engineering Journal},

volume = {481},

publisher = {Elsevier B.V.},

abstract = {Planococcus sp. S5 belongs to strains that degrade naproxen, one of the most popular non-steroidal anti-inflammatory drugs. In the presented work, the immobilization of the S5 strain was carried out on the Loofah plant sponge, which improved the degradation efficiency, and kinetic studies indicated the abolition of the inhibition by the substrate observed in the free cell system. At the same time, after immobilization, evident changes were observed in the metabolic profile of the strain, which was related to the specific microenvironment of the carrier. The study also presents the naproxen degradation pathway in a system with the immobilized S5 strain for the first time. The analysis of intermediates formed during the decomposition of naproxen indicated that this decomposition occurs through naphthalene and salicylic acid. Furthermore, the degradation of naproxen via 3-hydroxybenzoic acid to gentisic acid is also possible. The high efficiency of naproxen degradation by the immobilised S5 strain enables its use in bioremediation. © 2023 Elsevier B.V.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85165181270,

title = {Application of Immobilized Biocatalysts in the Biotransformation of Non-Steroidal Anti-Inflammatory Drugs},

author = { A. Nowak and A. Dzionek and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85165181270&doi=10.3390%2fapp13137789&partnerID=40&md5=d7c404aacc43dd4a75ef48ee72f2f9f7},

doi = {10.3390/app13137789},

issn = {20763417},

year  = {2023},

date = {2023-01-01},

journal = {Applied Sciences (Switzerland)},

volume = {13},

number = {13},

publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},

abstract = {Featured Application: Given the new EU Water Directive, wastewater treatment plants are interested in increasing the efficiency of wastewater treatment in terms of pharmaceuticals. Diclofenac is one of the most common pollutants indicated in the above directive. In connection with the above, the developed preparation, after passing tests on a semi-technical scale, can be used as a factor supporting the work of the sewage treatment plant to remove non-steroidal anti-inflammatory drugs. Among the micropollutants identified in the environment, non-steroidal anti-inflammatory drugs (NSAIDs) dominate more and more often. This is due to both the high consumption and low efficiency of biological wastewater treatment plants, where the initial transformation of NSAIDs most often takes place. The solution to the problem may be using preparations supporting activated sludge in sewage treatment plants in the biodegradation of NSAIDs. Therefore, the research aimed to develop a biopreparation stimulating the activated sludge of the sewage treatment plant to decompose paracetamol and selected NSAIDs. This biopreparation is based on strains of Stenotrophomonas maltophilia KB2, Planococcus sp. S5, Bacillus thuringiensis B1(2015b), and Pseudomonas moorei KB4 immobilized on a plant sponge. As a result of the tests, it was shown that the optimal species composition of the proposed preparation includes all tested strains immobilized on a carrier with a mass of 1.2 g/L. The system optimization showed that the optimal amount of strains on the carrier was 17 mg/g of the carrier, 15 mg/g of the carrier, 18 mg/g of the carrier, and 20 mg/g of the carrier for KB4, B1(2015b), KB2, and S5, respectively. The presence of phenol stimulated the degradation of the tested drugs, and this effect deepened with increasing phenol concentration. At the same time, the degradation rate of the mixture of NSAIDs in the presence of phenol did not depend on the amount of biomass. The lack of inhibition in the presence of an additional co-contaminant, i.e., phenol, indicates that the preparation constructed in this way has a chance of being used in sewage treatment plant systems, where introduced strains are exposed to various aromatic compounds. © 2023 by the authors.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85149843765,

title = {Evaluation of the Defined Bacterial Consortium Efficacy in the Biodegradation of NSAIDs},

author = { A. Marchlewicz and U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85149843765&doi=10.3390%2fmolecules28052185&partnerID=40&md5=4092d66ed33e1bc7f11ea9018ced134c},

doi = {10.3390/molecules28052185},

issn = {14203049},

year  = {2023},

date = {2023-01-01},

journal = {Molecules},

volume = {28},

number = {5},

publisher = {MDPI},

abstract = {Due to the increasing pollution of wastewater with non-steroidal anti-inflammatory drugs, preparations need to be developed to decompose these drugs. This work aimed to develop a bacterial consortium with a defined composition and boundary conditions for the degradation of paracetamol and selected non-steroidal anti-inflammatory drugs (NSAIDs), including ibuprofen, naproxen, and diclofenac. The defined bacterial consortium consisted of Bacillus thuringiensis B1(2015b) and Pseudomonas moorei KB4 strains in a ratio of 1:2. During the tests, it was shown that the bacterial consortium worked in the pH range from 5.5 to 9 and temperatures of 15–35 °C, and its great advantage was its resistance to toxic compounds present in sewage, such as organic solvents, phenols, and metal ions. The degradation tests showed that, in the presence of the defined bacterial consortium in the sequencing batch reactor (SBR), drug degradation occurred at rates of 4.88, 10, 0.1, and 0.05 mg/day for ibuprofen, paracetamol, naproxen, and diclofenac, respectively. In addition, the presence of the tested strains was demonstrated during the experiment as well as after its completion. Therefore, the advantage of the described bacterial consortium is its resistance to the antagonistic effects of the activated sludge microbiome, which will enable it to be tested in real activated sludge conditions. © 2023 by the authors.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85148939250,

title = {Diclofenac Biodegradation by Microorganisms and with Immobilised Systems—A Review},

author = { D. Wojcieszyńska and K. Łagoda and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85148939250&doi=10.3390%2fcatal13020412&partnerID=40&md5=c7e843df34dde899f449987f807da374},

doi = {10.3390/catal13020412},

issn = {20734344},

year  = {2023},

date = {2023-01-01},

journal = {Catalysts},

volume = {13},

number = {2},

publisher = {MDPI},

abstract = {Diclofenac is one of the most popular non-steroidal anti-inflammatory drugs. Due to its over-the-counter availability and high consumption along with municipal and hospital wastewater, it enters the sewage treatment plant, where it is not completely degraded. This results in the appearance of diclofenac in the effluents from the treatment plant, and with them, it enters the surface waters. Due to its structure, it is characterised by its high resistance to degradation in the environment. At the same time, it shows documented acute and chronic toxicity to non-target organisms. For this reason, it is necessary to look for cheap solutions that enhance the degradation of diclofenac. The paper discusses both the pathways of microbiological degradation of this drug described so far, as well as modern systems of biocatalyst immobilisation, with a particular emphasis on laccases involved in the biotransformation of diclofenac. © 2023 by the authors.},

note = {10},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85138690790,

title = {Immobilized Stenotrophomonas maltophilia KB2 in Naproxen Degradation},

author = { D. Wojcieszyńska and J. Klamka and A. Marchlewicz and I.W. Potocka and J. Żur and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85138690790&doi=10.3390%2fmolecules27185795&partnerID=40&md5=2dda4f9763acf86cf0ed785d52ea3576},

doi = {10.3390/molecules27185795},

issn = {14203049},

year  = {2022},

date = {2022-01-01},

journal = {Molecules},

volume = {27},

number = {18},

publisher = {MDPI},

abstract = {Immobilization is a commonly used method in response to the need to increase the resistance of microorganisms to the toxic effects of xenobiotics. In this study, a plant sponge from Luffa cylindrica was used as a carrier for the immobilization of the Stenotrophomonas maltophilia KB2 strain since such a carrier meets the criteria for high-quality carriers, i.e., low price and biodegradability. The optimal immobilization conditions were established as a temperature of 30 °C, pH 7.2, incubation time of 72 h, and an optical density of the culture of 1.4. The strain immobilized in such conditions was used for the biodegradation of naproxen, and an average rate of degradation of 3.8 µg/hour was obtained under cometabolic conditions with glucose. The obtained results indicate that a microbiological preparation based on immobilized cells on a luffa sponge can be used in bioremediation processes where it is necessary to remove the introduced carrier. © 2022 by the authors.},

note = {1},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85129086345,

title = {Non-steroidal anti-inflammatory drugs in the era of the Covid-19 pandemic in the context of the human and the environment},

author = { D. Wojcieszyńska and H. Guzik and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85129086345&doi=10.1016%2fj.scitotenv.2022.155317&partnerID=40&md5=86b35e29e680e7ef0fceb03bd3fdcab9},

doi = {10.1016/j.scitotenv.2022.155317},

issn = {00489697},

year  = {2022},

date = {2022-01-01},

journal = {Science of the Total Environment},

volume = {834},

publisher = {Elsevier B.V.},

abstract = {From 2019, life in the world has mainly been determined by successive waves of the COVID-19 epidemic. During this time, the virus structure, action, short- and long-term effects of the infection were discovered, and treatments were developed. This epidemic undoubtedly affected people's lives, but increasing attention is also being paid to the effects of the epidemic on the environment. Following PRISMA (Preferred Reporting Items for Systematic Reviews and Meta-analyses) guidelines, a global scoping review of peer-reviewed information has been conducted on the use of over-the-counter non-steroidal anti-inflammatory drugs in the treatment of symptoms of SARS-CoV-2 infections and their positive and negative effects on the human body, the effects of non-steroidal anti-inflammatory drugs (NSAIDs) on aquatic organisms, and their adverse effects on non-target organisms. The literature from 1998 to 2021 was analysed using the Scopus®, Web of Science™ (WoS) and Google Scholar databases. As non-steroidal anti-inflammatory drugs place a heavy burden on the environment, all reports of the presence of these drugs in the environment during the pandemic period have been thoroughly analysed. Of the 70 peer-reviewed records within the scope, only 14% (n = 10) focussed on the analysis of non-steroidal anti-inflammatory drugs concentrations in wastewater and surface waters during the pandemic period. The percentage of these works indicates that it is still an open topic, and this issue should be supplemented with further reports in which the results obtained during the pandemic, which has been going on for several years, will be published. The authors hope this review will inspire scientists to investigate the problem of non-steroidal anti-inflammatory drugs in the environment to protect them for the next generation. © 2022 The Authors},

note = {15},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85126104603,

title = {Use of xanthan gum for whole cell immobilization and its impact in bioremediation - a review},

author = { A. Dzionek and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85126104603&doi=10.1016%2fj.biortech.2022.126918&partnerID=40&md5=557138976da2d3299c2302204cae8dd2},

doi = {10.1016/j.biortech.2022.126918},

issn = {09608524},

year  = {2022},

date = {2022-01-01},

journal = {Bioresource Technology},

volume = {351},

publisher = {Elsevier Ltd},

abstract = {Xanthan gum is one of the exo-polysaccharides produced by bacteria and is characterized by unique non-Newtonian properties. Its structure and conformation strongly depend on the fermentation conditions and such factors as temperature and ions concentration. The properties of the xanthan gum were appreciated in the controlled drug delivery but in the crosslinked form. Due to its ability to enhance the survival rate of immobilized bacteria, the potential of a crosslinked form is promising. Unfortunately, xanthan gum crosslinking procedures often require toxic substances or harsh environmental conditions, which cannot be used in the entrapment of living cells. In this study, we summarised a crosslinking method that could potentially be modified to reduce its toxicity to living cells. Moreover, this review also includes using xanthan gum in bioremediation studies and possible utilization methods to avoid carrier accumulation in the environment. © 2022 The Authors},

note = {15},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85092155502,

title = {Degradation of diclofenac by new bacterial strains and its influence on the physiological status of cells},

author = { J. Żur and A. Marchlewicz and A. Piński and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85092155502&doi=10.1016%2fj.jhazmat.2020.124000&partnerID=40&md5=ea0a1291c85c273eacde445aa45e1c1c},

doi = {10.1016/j.jhazmat.2020.124000},

issn = {03043894},

year  = {2021},

date = {2021-01-01},

journal = {Journal of Hazardous Materials},

volume = {403},

publisher = {Elsevier B.V.},

abstract = {Diclofenac (DCF) is one of the most commonly utilized non-steroidal anti-inflammatory drugs (NSAIDs), which is known to pose an ecotoxicological threat. In this study, from activated sludge and contaminated soil, we isolated four new bacterial strains able to degrade DCF under mono-substrate and co-metabolic conditions with glucose supplementation. We found that the effectiveness of DCF removal is strictly strain-specific and the addition of the primary substrate is not always beneficial. To assess the multidirectional influence of DCF on bacterial cells we evaluated the alterations of increasing concentrations of this drug on membrane structure. A significant increase was observed in the content of 17:0 cyclo fatty acid, which is responsible for reduced fluidity and profound changes in membrane rigidity. The cell injury and oxidative stress were assessed with biomarkers used as endpoints of toxicity, i.e. catalase (CAT), superoxide dismutase (SOD), lipids peroxidation (LPX), and both intra- and extracellular alkaline and acid phosphatase activity. Results indicated that DCF induced oxidative stress, frequently intensified by the addition of glucose. However, the response of the microbial cells to the presence of DCF should not be generalized, since the overall picture of the particular alterations greatly varied for each of the examined strains. © 2020 Elsevier B.V.},

note = {9},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85101245617,

title = {Effect of pseudomonas moorei KB4 cells’ immobilisation on their degradation potential and tolerance towards paracetamol},

author = { R. Surma and D. Wojcieszyńska and J. Karcz and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85101245617&doi=10.3390%2fmolecules26040820&partnerID=40&md5=064d83f53283ba3f5844d49b8d52ad4d},

doi = {10.3390/molecules26040820},

issn = {14203049},

year  = {2021},

date = {2021-01-01},

journal = {Molecules},

volume = {26},

number = {4},

publisher = {MDPI AG},

abstract = {Pseudomonas moorei KB4 is capable of degrading paracetamol, but high concentrations of this drug may cause an accumulation of toxic metabolites. It is known that immobilisation can have a protective effect on bacterial cells; therefore, the toxicity and degradation rate of paracetamol by the immobilised strain KB4 were assessed. Strain KB4 was immobilised on a plant sponge. A toxicity assessment was performed by measuring the concentration of ATP using the colony-forming unit (CFU) method. The kinetic parameters of paracetamol degradation were estimated using the Hill equation. Toxicity analysis showed a protective effect of the carrier at low concentrations of paracetamol. Moreover, a pronounced phenomenon of hormesis was observed in the immobilised systems. The obtained kinetic parameters and the course of the kinetic curves clearly indicate a decrease in the degradation activity of cells after their immobilisation. There was a delay in degradation in the systems with free cells without glucose and immobilised cells with glucose. However, it was demonstrated that the immobilised systems can degrade at least ten succeeding cycles of 20 mg/L paracetamol degradation. The obtained results indicate that the immobilised strain may become a useful tool in the process of paracetamol degradation. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.},

note = {4},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85090585955,

title = {Xanthan gum as a carrier for bacterial cell entrapment: Developing a novel immobilised biocatalyst},

author = { A. Dzionek and D. Wojcieszyńska and M. Adamczyk-Habrajska and J. Karczewski and I.W. Potocka and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85090585955&doi=10.1016%2fj.msec.2020.111474&partnerID=40&md5=4a58bcdb7fc091b5c8bf180f466e858d},

doi = {10.1016/j.msec.2020.111474},

issn = {09284931},

year  = {2021},

date = {2021-01-01},

journal = {Materials Science and Engineering C},

volume = {118},

publisher = {Elsevier Ltd},

abstract = {Xanthan gum (XAN) is a widely used polysaccharide in various industries. Because of its unique properties, in this study, an attempt was made to adopt the procedure of xanthan gum cross-linking for the entrapment of bacterial cells that are able to biodegrade naproxen. The developed procedure proved to be completely neutral for Bacillus thuringiensis B1(2015b) cells, which demonstrated a survival rate of 99%. A negative impact of entrapment was noted for strain Planococcus sp. S5, which showed a survival rate in the 93–51% range. To achieve good mechanical properties of the composites, they were additionally hardened using polydopamine (PDA). XAN/PDA composites revealed a high stability in a wide range of pH, and their sorption capacity included both cationic and anionic molecules. Analysis of the survival rate during storage at 4 °C in 0.9% NaCl showed that, after 35 days, 98–99% of B1(2015b) and 47% of S5 cells entrapped in XAN/PDA remained alive. This study also presents the results of naproxen biodegradation conducted using XAN/PDA/B1(2015b) in a trickling filter with autochthonous microflora. Hence, owing to the significant acceleration of drug biodegradation (1 mg/L in 14 days) and the chemical oxygen demand removal, the entrapped B1(2015b) cells in XAN/PDA composites showed a promising potential in bioremediation studies and industrial applications. © 2020 Elsevier B.V.},

note = {6},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85092520348,

title = {Suitability of immobilized systems for microbiological degradation of endocrine disrupting compounds},

author = { D. Wojcieszyńska and A. Marchlewicz and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85092520348&doi=10.3390%2fmolecules25194473&partnerID=40&md5=11c5639727e4fcd7a256dee3f126b652},

doi = {10.3390/molecules25194473},

issn = {14203049},

year  = {2020},

date = {2020-01-01},

journal = {Molecules},

volume = {25},

number = {19},

publisher = {MDPI AG},

abstract = {The rising pollution of the environment with endocrine disrupting compounds has increased interest in searching for new, e_ective bioremediation methods. Particular attention is paid to the search for microorganisms with high degradation potential and the possibility of their use in the degradation of endocrine disrupting compounds. Increasingly, immobilized microorganisms or enzymes are used in biodegradation systems. This review presents the main sources of endocrine disrupting compounds and identifies the risks associated with their presence in the environment. The main pathways of degradation of these compounds by microorganisms are also presented. The last part is devoted to an overview of the immobilization methods used for the purposes of enabling the use of biocatalysts in environmental bioremediation. © 2020 by the authors.},

note = {7},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85090899825,

title = {Diclofenac degradation—enzymes, genetic background and cellular alterations triggered in diclofenac-metabolizing strain pseudomonas moorei KB4},

author = { J. Żur and A. Piński and D. Wojcieszyńska and W. Smułek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85090899825&doi=10.3390%2fijms21186786&partnerID=40&md5=02cb0c3ff66c56b2a75244c5e93fb01b},

doi = {10.3390/ijms21186786},

issn = {16616596},

year  = {2020},

date = {2020-01-01},

journal = {International Journal of Molecular Sciences},

volume = {21},

number = {18},

pages = {1-22},

publisher = {MDPI AG},

abstract = {Diclofenac (DCF) constitutes one of the most significant ecopollutants detected in various environmental matrices. Biological clean-up technologies that rely on xenobiotics-degrading microorganisms are considered as a valuable alternative for chemical oxidation methods. Up to now, the knowledge about DCF multi-level influence on bacterial cells is fragmentary. In this study, we evaluate the degradation potential and impact of DCF on Pseudomonas moorei KB4 strain. In mono-substrate culture KB4 metabolized 0.5 mg L−1 of DCF, but supplementation with glucose (Glc) and sodium acetate (SA) increased degraded doses up to 1 mg L−1 within 12 days. For all established conditions, 4′-OH-DCF and DCF-lactam were identified. Gene expression analysis revealed the up-regulation of selected genes encoding biotransformation enzymes in the presence of DCF, in both mono-substrate and co-metabolic conditions. The multifactorial analysis of KB4 cell exposure to DCF showed a decrease in the zeta-potential with a simultaneous increase in the cell wall hydrophobicity. Magnified membrane permeability was coupled with the significant increase in the branched (19:0 anteiso) and cyclopropane (17:0 cyclo) fatty acid accompanied with reduced amounts of unsaturated ones. DCF injures the cells which is expressed by raised activities of acid and alkaline phosphatases as well as formation of lipids peroxidation products (LPX). The elevated activity of superoxide dismutase (SOD) and catalase (CAT) testified that DCF induced oxidative stress. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.},

note = {7},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85079226601,

title = {A whole-cell immobilization system on bacterial cellulose for the paracetamol-degrading Pseudomonas moorei KB4 strain},

author = { J. Żur and A. Piński and J. Michalska and K.T. Hupert-Kocurek and A. Nowak and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85079226601&doi=10.1016%2fj.ibiod.2020.104919&partnerID=40&md5=83d05c44cb2a78963ef96e3d769f2088},

doi = {10.1016/j.ibiod.2020.104919},

issn = {09648305},

year  = {2020},

date = {2020-01-01},

journal = {International Biodeterioration and Biodegradation},

volume = {149},

publisher = {Elsevier Ltd},

abstract = {Microorganisms with a high natural ability to degrade xenobiotics, which are usually characterized by a diverse metabolism and unique features, can be used as natural biocatalysts in wastewater treatment or bioaugmentation processes. The immobilization of such strains greatly increases their stability and degradation properties. The most critical issues in designing whole-cell immobilization systems are selecting the suitable carrier and determining the bacterial features that will promote effective immobilization. In this study, we immobilized the paracetamol-degrading Pseudomonas moorei KB4 strain on the bacterial cellulose disks that were produced by Komagataeibacter xylinus E-89370. The KB4 strain immobilized on the cellulose degraded 150 mg L−1 of paracetamol in three series of 50 mg L−1 in each cycle. The average protein concentration and dehydrogenase activity increased after the degradation of each dose. The specific activity (U mg−1 of protein) of the main enzymes involved in the degradation pathway was 0.22 for deaminase, 5.1 for acylamidohydrolase and 3.49 for ring-cleavage hydroquinone 1,2-dioxygenase. The relative expression level of the genes encoding deaminases and acylamidohydrolases increased in the presence of paracetamol, though more prominently in the immobilized than in the free cells. © 2020 Elsevier Ltd},

note = {19},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85077719857,

title = {Naproxen in the environment: its occurrence, toxicity to nontarget organisms and biodegradation},

author = { D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85077719857&doi=10.1007%2fs00253-019-10343-x&partnerID=40&md5=5e3cedbf318efd1f7c4dae796c0a9779},

doi = {10.1007/s00253-019-10343-x},

issn = {01757598},

year  = {2020},

date = {2020-01-01},

journal = {Applied Microbiology and Biotechnology},

volume = {104},

number = {5},

pages = {1849-1857},

publisher = {Springer},

abstract = {Abstract: This article summarizes the current knowledge about the presence of naproxen in the environment, its toxicity to nontarget organisms and the microbial degradation of this drug. Currently, naproxen has been detected in all types of water, including drinking water and groundwater. The concentrations that have been observed ranged from ng/L to μg/L. These concentrations, although low, may have a negative effect of long-term exposure on nontarget organisms, especially when naproxen is mixed with other drugs. The biological decomposition of naproxen is performed by fungi, algae and bacteria, but the only well-described pathway for its complete degradation is the degradation of naproxen by Bacillus thuringiensis B1(2015b). The key intermediates that appear during the degradation of naproxen by this strain are O-desmethylnaproxen and salicylate. This latter is then cleaved by 1,2-salicylate dioxygenase or is hydroxylated to gentisate or catechol. These intermediates can be cleaved by the appropriate dioxygenases, and the resulting products are incorporated into the central metabolism. Key points: •High consumption of naproxen is reflected in its presence in the environment. •Prolonged exposure of nontargeted organisms to naproxen can cause adverse effects. •Naproxen biodegradation occurs mainly through desmethylnaproxen as a key intermediate. © 2020, The Author(s).},

note = {50},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85079637258,

title = {Enhanced Degradation of Naproxen by Immobilization of Bacillus thuringiensis B1(2015b) on Loofah Sponge},

author = { A. Dzionek and D. Wojcieszyńska and M. Adamczyk-Habrajska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85079637258&doi=10.3390%2fmolecules25040872&partnerID=40&md5=b37cbe5c7bd659ee99d37e365bb7e99f},

doi = {10.3390/molecules25040872},

issn = {14203049},

year  = {2020},

date = {2020-01-01},

journal = {Molecules},

volume = {25},

number = {4},

publisher = {MDPI AG},

abstract = {The naproxen-degrading bacterium Bacillus thuringiensis B1(2015b) was immobilised onto loofah sponge and introduced into lab-scale trickling filters. The trickling filters constructed for this study additionally contained stabilised microflora from a functioning wastewater treatment plant to assess the behavior of introduced immobilized biocatalyst in a fully functioning bioremediation system. The immobilised cells degraded naproxen (1 mg/L) faster in the presence of autochthonous microflora than in a monoculture trickling filter. There was also abundant colonization of the loofah sponges by the microorganisms from the system. Analysis of the influence of an acute, short-term naproxen exposure on the indigenous community revealed a significant drop in its diversity and qualitative composition. Bioaugmentation was also not neutral to the microflora. Introducing a new microorganism and increasing the removal of the pollutant caused changes in the microbial community structure and species composition. The incorporation of the immobilised B1(2015b) was successful and the introduced strain colonized the basic carrier in the trickling filter after the complete biodegradation of the naproxen. As a result, the bioremediation system could potentially be used to biodegrade naproxen in the future. © 2020 by the authors.},

note = {9},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85063114635,

title = {A new pathway for naproxen utilisation by Bacillus thuringiensis B1(2015b) and its decomposition in the presence of organic and inorganic contaminants},

author = { D. Górny and U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063114635&doi=10.1016%2fj.jenvman.2019.03.034&partnerID=40&md5=74244b4c49f7546b44695325fb4d62f1},

doi = {10.1016/j.jenvman.2019.03.034},

issn = {03014797},

year  = {2019},

date = {2019-01-01},

journal = {Journal of Environmental Management},

volume = {239},

pages = {1-7},

publisher = {Academic Press},

abstract = {Bacillus thuringiensis B1 (2015b) is a bacterial strain that is able to degrade naproxen. However, the potential effect of water co-contaminations on the degradation process and its pathway have not yet been evaluated. The results of our study show that in the presence of aromatic compounds, the B1 (2015b) strain utilised naproxen with an efficiency that was similar to what it was with no aromatic co-contaminations. In the presence of methanol, biodegradation of naproxen was inhibited, while the addition of ethanol increased the decomposition of naproxen. Among the metal ions that were tested, only cobalt (II) and cadmium (II) negatively affected the degradation of the drug. An analysis of the intermediates and enzymes that are engaged in degrading naproxen revealed that the key metabolites are O-desmethylnaproxen, which is the product of tetrahydrofolate-dependent O-demethylase activity, and salicylic acid. Salicylic acid can then be hydroxylated to catechol or gentisic acid or can be cleaved to 2-oxo-3,5-heptadienedioic acid. The high activity level of catechol 1,2-dioxygenase indicated that the main degradative pathway of naproxen in the B1 (2015b) strain is via catechol cleavage. © 2019 Elsevier Ltd},

note = {13},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85055336990,

title = {Naproxen ecotoxicity and biodegradation by Bacillus thuringiensis B1(2015b) strain},

author = { D. Górny and U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85055336990&doi=10.1016%2fj.ecoenv.2018.10.067&partnerID=40&md5=d2e8928875b3a10dfacc3bd31f5d8b0d},

doi = {10.1016/j.ecoenv.2018.10.067},

issn = {01476513},

year  = {2019},

date = {2019-01-01},

journal = {Ecotoxicology and Environmental Safety},

volume = {167},

pages = {505-512},

publisher = {Academic Press},

abstract = {High level of naproxen consumption leads to the appearance of this drug in the environment but its possible effects on non-target organisms together with its biodegradation are not well studied. The aim of this work was to evaluate naproxen ecotoxicity by using the Microbial Assay for Risk Assessment. Moreover, Bacillus thuringiensis B1(2015b) was tested for both ecotoxicity and the ability of this strain to degrade naproxen in cometabolic conditions. The results indicate that the mean value of microbial toxic concentration estimated by MARA test amounts to 1.66 g/L whereas EC50 of naproxen for B1(2015b) strain was 4.69 g/L. At toxic concentration, Bacillus thuringiensis B1(2015b) showed 16:0 iso 3OH fatty acid presence and an increase in the ratio of total saturated to unsaturated fatty acids. High resistance of the examined strain to naproxen correlated with its ability to degrade this drug in cometabolic conditions. The results of bacterial reverse mutation assay (Ames test) revealed that naproxen at concentrations above 1 g/L showed genotoxic effect but the response was not dose-dependent. Maximal specific naproxen removal rate was observed at pH 6.5 and 30 °C, and in the presence of 0.5 g/L glucose as a growth substrate. Kinetic analysis allowed estimation of the half saturation constant (Ks) and the maximum specific naproxen removal rate (qmax) as 6.86 mg/L and 1.26 mg/L day, respectively. These results indicate that Bacillus thuringiensis B1(2015b) has a high ability to degrade naproxen and is a potential tool for bioremediation. © 2018 Elsevier Inc.},

note = {33},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85054792135,

title = {Fluorescein diacetate hydrolysis using the whole biofilm as a sensitive tool to evaluate the physiological state of immobilized bacterial cells},

author = { A. Dzionek and J. Dzik and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85054792135&doi=10.3390%2fcatal8100434&partnerID=40&md5=263d76d78b4a0410fa4b969485ca4a69},

doi = {10.3390/catal8100434},

issn = {20734344},

year  = {2018},

date = {2018-01-01},

journal = {Catalysts},

volume = {8},

number = {10},

publisher = {MDPI},

abstract = {Due to the increasing interest and the use of immobilized biocatalysts in bioremediation studies, there is a need for the development of an assay for quick and reliable measurements of their overall enzymatic activity. Fluorescein diacetate (FDA) hydrolysis is a widely used assay for measuring total enzymatic activity (TEA) in various environmental samples or in monoculture researches. However, standard FDA assays for TEA measurements in immobilized samples include performing an assay on cells detached from the carrier. This causes an error, because it is not possible to release all cells from the carrier without affecting their metabolic activity. In this study, we developed and optimized a procedure for TEA quantification in the whole biofilm formed on the carrier without disturbing it. The optimized method involves pre-incubation of immobilized carrier in phosphate buffer (pH 7.6) on the orbital shaker for 15 min, slow injection of FDA directly into the middle of the immobilized carrier, and incubation on the orbital shaker (130 rpm; 30◦C) for 1 h. Biofilm dry mass was obtained by comparing the dried weight of the immobilized carrier with that of the unimmobilized carrier. The improved protocol provides a simple, quick, and more reliable quantification of TEA during the development of immobilized biocatalysts compared to the original method. © 2018 by the authors. Licensee MDPI, Basel, Switzerland.},

note = {11},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85048021599,

title = {Paracetamol – toxicity and microbial utilization. Pseudomonas moorei KB4 as a case study for exploring degradation pathway},

author = { J. Żur and D. Wojcieszyńska and K.T. Hupert-Kocurek and A. Marchlewicz and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048021599&doi=10.1016%2fj.chemosphere.2018.04.179&partnerID=40&md5=9941e36fe7554a810b10735fb721bbcc},

doi = {10.1016/j.chemosphere.2018.04.179},

issn = {00456535},

year  = {2018},

date = {2018-01-01},

journal = {Chemosphere},

volume = {206},

pages = {192-202},

publisher = {Elsevier Ltd},

abstract = {Paracetamol, a widely used analgesic and antipyretic drug, is currently one of the most emerging pollutants worldwide. Besides its wide prevalence in the literature only several bacterial strains able to degrade this compound have been described. In this study, we isolated six new bacterial strains able to remove paracetamol. The isolated strains were identified as the members of Pseudomonas, Bacillus, Acinetobacter and Sphingomonas genera and characterized phenotypically and biochemically using standard methods. From the isolated strains, Pseudomonas moorei KB4 was able to utilize 50 mg L−1 of paracetamol. As the main degradation products, p-aminophenol and hydroquinone were identified. Based on the measurements of specific activity of acyl amidohydrolase, deaminase and hydroquinone 1,2-dioxygenase and the results of liquid chromatography analyses, we proposed a mechanism of paracetamol degradation by KB4 strain under co-metabolic conditions with glucose. Additionally, toxicity bioassays and the influence of various environmental factors, including pH, temperature, heavy metals at no-observed-effective-concentrations, and the presence of aromatic compounds on the efficiency and mechanism of paracetamol degradation by KB4 strain were determined. This comprehensive study about paracetamol biodegradation will be helpful in designing a treatment systems of wastewaters contaminated with paracetamol. © 2018 Elsevier Ltd},

note = {63},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85048822480,

title = {Organic micropollutants paracetamol and ibuprofen—toxicity, biodegradation, and genetic background of their utilization by bacteria},

author = { J. Żur and A. Piński and A. Marchlewicz and K.T. Hupert-Kocurek and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048822480&doi=10.1007%2fs11356-018-2517-x&partnerID=40&md5=bed6633cc8ff497e87e086da67cbead2},

doi = {10.1007/s11356-018-2517-x},

issn = {09441344},

year  = {2018},

date = {2018-01-01},

journal = {Environmental Science and Pollution Research},

volume = {25},

number = {22},

pages = {21498-21524},

publisher = {Springer Verlag},

abstract = {Currently, analgesics and nonsteroidal anti-inflammatory drugs (NSAIDs) are classified as one of the most emerging group of xenobiotics and have been detected in various natural matrices. Among them, monocyclic paracetamol and ibuprofen, widely used to treat mild and moderate pain are the most popular. Since long-term adverse effects of these xenobiotics and their biological and pharmacokinetic activity especially at environmentally relevant concentrations are better understood, degradation of such contaminants has become a major concern. Moreover, to date, conventional wastewater treatment plants (WWTPs) are not fully adapted to remove that kind of micropollutants. Bioremediation processes, which utilize bacterial strains with increased degradation abilities, seem to be a promising alternative to the chemical methods used so far. Nevertheless, despite the wide prevalence of paracetamol and ibuprofen in the environment, toxicity and mechanism of their microbial degradation as well as genetic background of these processes remain not fully characterized. In this review, we described the current state of knowledge about toxicity and biodegradation mechanisms of paracetamol and ibuprofen and provided bioinformatics analysis concerning the genetic bases of these xenobiotics decomposition. © 2018, The Author(s).},

note = {90},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85048057032,

title = {Immobilization of Planococcus sp. S5 strain on the loofah sponge and its application in naproxen removal},

author = { A. Dzionek and D. Wojcieszyńska and K.T. Hupert-Kocurek and M. Adamczyk-Habrajska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048057032&doi=10.3390%2fcatal8050176&partnerID=40&md5=ae170a3a84ad2289b7ca0641afaad21c},

doi = {10.3390/catal8050176},

issn = {20734344},

year  = {2018},

date = {2018-01-01},

journal = {Catalysts},

volume = {8},

number = {5},

publisher = {MDPI},

abstract = {Planococcus sp. S5, a Gram-positive bacterium isolated from the activated sludge is known to degrade naproxen in the presence of an additional carbon source. Due to the possible toxicity of naproxen and intermediates of its degradation, the whole cells of S5 strain were immobilized onto loofah sponge. The immobilized cells degraded 6, 9, 12 or 15 mg/L of naproxen faster than the free cells. Planococcus sp. cells immobilized onto the loofah sponge were able to degrade naproxen efficiently for 55 days without significant damage and disintegration of the carrier. Analysis of the activity of enzymes involved in naproxen degradation showed that stabilization of S5 cells in exopolysaccharide (EPS) resulted in a significant increase of their activity. Changes in the structure of biofilm formed on the loofah sponge cubes during degradation of naproxen were observed. Developed biocatalyst system showed high resistance to naproxen and its intermediates and degraded higher concentrations of the drug in comparison to the free cells. © 2018 by the authors. Licensee MDPI, Basel, Switzerland.},

note = {15},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85033795055,

title = {Stenotrophomonas maltophilia: A gram-negative bacterium useful for transformations of flavanone and chalcone},

author = { E. Kostrzewa-Susow and M. Dymarska and U. Guzik and D. Wojcieszyńska and T. Janeczko},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85033795055&doi=10.3390%2fmolecules22111830&partnerID=40&md5=5b6b1f0127df7306d5d8ceb61da6a131},

doi = {10.3390/molecules22111830},

issn = {14203049},

year  = {2017},

date = {2017-01-01},

journal = {Molecules},

volume = {22},

number = {11},

publisher = {MDPI AG},

abstract = {A group of flavones, isoflavones, flavanones, and chalcones was subjected to small-scale biotransformation studies with the Gram-negative Stenotrophomonas maltophilia KB2 strain in order to evaluate the capability of this strain to transform flavonoid compounds and to investigate the relationship between compound structure and transformation type. The tested strain transformed flavanones and chalcones. The main type of transformation of compounds with a flavanone moiety was central heterocyclic C ring cleavage, leading to chalcone and dihydrochalcone structures, whereas chalcones underwent reduction to dihydrochalcones and cyclisation to a benzo-pyrone moiety. Substrates with a C-2-C-3 double bond (flavones and isoflavones) were not transformed by Stenotrophomonas maltophilia KB2. © 2017 by the authors.},

note = {12},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85032711058,

title = {Exploring the degradation of ibuprofen by bacillus thuringiensis B1(2015b): The new pathway and factors affecting degradation},

author = { A. Marchlewicz and U. Guzik and W. Smułek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032711058&doi=10.3390%2fmolecules22101676&partnerID=40&md5=6dfc7f57f372853f7a5a1e14f2c71368},

doi = {10.3390/molecules22101676},

issn = {14203049},

year  = {2017},

date = {2017-01-01},

journal = {Molecules},

volume = {22},

number = {10},

publisher = {MDPI AG},

abstract = {Ibuprofen is one of the most often detected pollutants in the environment, particularly at landfill sites and in wastewaters. Contamination with pharmaceuticals is often accompanied by the presence of other compounds which may influence their degradation. This work describes the new degradation pathway of ibuprofen by Bacillus thuringiensis B1(2015b), focusing on enzymes engaged in this process. It is known that the key intermediate which transformation limits the velocity of the degradation process is hydroxyibuprofen. As the degradation rate also depends on various factors, the influence of selected heavy metals and aromatic compounds on ibuprofen degradation by the B1(2015b) strain was examined. Based on the values of non-observed effect concentration (NOEC) it was found that the toxicity of tested metals increases from Hg(II) < Cu(II) < Cd(II) < Co(II) < Cr(VI). Despite the toxic effect of metals, the biodegradation of ibuprofen was observed. The addition of Co2+ ions into the medium significantly extended the time necessary for the complete removal of ibuprofen. It was shown that Bacillus thuringiensis B1(2015b) was able to degrade ibuprofen in the presence of phenol, benzoate, and 2-chlorophenol. Moreover, along with the removal of ibuprofen, degradation of phenol and benzoate was observed. Introduction of 4-chlorophenol into the culture completely inhibits degradation of ibuprofen. © 2017 by The Authors. Licensee MDPI, Basel, Switzerland.},

note = {31},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85020934837,

title = {Dynamics of ibuprofen biodegradation by Bacillus sp. B1(2015b)},

author = { A. Marchlewicz and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85020934837&doi=10.1515%2faep-2017-0020&partnerID=40&md5=df1595f516679cc4115587d01a52aa2e},

doi = {10.1515/aep-2017-0020},

issn = {03248461},

year  = {2017},

date = {2017-01-01},

journal = {Archives of Environmental Protection},

volume = {43},

number = {2},

pages = {60-64},

publisher = {De Gruyter Open Ltd},

abstract = {High intake of over-the-counter, non-steroidal anti-inflammatory drugs, such as ibuprofen, has resulted in their presence in wastewaters and surface waters. The potentially harmful effect of ibuprofen present in the waters has led to a search for new methods of drugs' removal from the environment. One of the most important technological and economical solutions comprises microbiological degradation of these resistant pollutants. Searching for new strains able to degrade ibuprofen could be one of the answers for increasing the detection of pharmaceuticals in the waters. In this study, the ability of bacterial strain Bacillus thuringiensis B1(2015b) to remove ibuprofen is described. Bacteria were cultured in both monosubstrate and cometabolic systems with 1, 3, 5, 7 and 9 mg L-1 ibuprofen and 1 g L-1 glucose as a carbon source. Bacillus thuringiensis B1(2015b) removed ibuprofen up to 9 mg L-1 in 232 hours in the monosubstrate culture, whereas in the cometabolic culture the removal of the drug was over 6 times faster. That is why the examined strain could be used to enhance the bioremediation of ibuprofen. © Archives of Environmental Protection 2017.},

note = {3},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85010723117,

title = {Toxicity and biodegradation of ibuprofen by Bacillus thuringiensis B1(2015b)},

author = { A. Marchlewicz and U. Guzik and K.T. Hupert-Kocurek and A. Nowak and S. Wilczyńska and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85010723117&doi=10.1007%2fs11356-017-8372-3&partnerID=40&md5=f8a6724832ad5bb834800f9207067ea7},

doi = {10.1007/s11356-017-8372-3},

issn = {09441344},

year  = {2017},

date = {2017-01-01},

journal = {Environmental Science and Pollution Research},

volume = {24},

number = {8},

pages = {7572-7584},

publisher = {Springer Verlag},

abstract = {In recent years, the increased intake of ibuprofen has resulted in the presence of the drug in the environment. This work presents results of a study on degradation of ibuprofen at 25 mg L−1 in the presence of glucose, as an additional carbon source by Bacillus thuringiensis B1(2015b). In the cometabolic system, the maximum specific growth rate of the bacterial strain was 0.07 ± 0.01 mg mL−1 h−1 and Ksμ 0.27 ± 0.15 mg L−1. The maximum specific ibuprofen removal rate and the value of the half-saturation constant were qmax = 0.24 ± 0.02 mg mL−1 h−1 and Ks = 2.12 ± 0.56 mg L−1, respectively. It has been suggested that monooxygenase and catechol 1,2-dioxygenase are involved in ibuprofen degradation by B. thuringiensis B1(2015b). Toxicity studies showed that B. thuringiensis B1(2015b) is more resistant to ibuprofen than other tested organisms. The EC50 of ibuprofen on the B1 strain is 809.3 mg L−1, and it is 1.5 times higher than the value of the microbial toxic concentration (MTCavg). The obtained results indicate that B. thuringiensis B1(2015b) could be a useful tool in biodegradation/bioremediation processes. © 2017, The Author(s).},

note = {37},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84987668157,

title = {Natural carriers in bioremediation: A review},

author = { A. Dzionek and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84987668157&doi=10.1016%2fj.ejbt.2016.07.003&partnerID=40&md5=5cebfeeab0cd9f059b8acfb99c69e9f0},

doi = {10.1016/j.ejbt.2016.07.003},

issn = {07173458},

year  = {2016},

date = {2016-01-01},

journal = {Electronic Journal of Biotechnology},

volume = {23},

pages = {28-36},

publisher = {Electronic Journal of Biotechnology},

abstract = {Bioremediation of contaminated groundwater or soil is currently the cheapest and the least harmful method of removing xenobiotics from the environment. Immobilization of microorganisms capable of degrading specific contaminants significantly promotes bioremediation processes, reduces their costs, and also allows for the multiple use of biocatalysts. Among the developed methods of immobilization, adsorption on the surface is the most common method in bioremediation, due to the simplicity of the procedure and its non-toxicity. The choice of carrier is an essential element for successful bioremediation. It is also important to consider the type of process (in situ or ex situ), type of pollution, and properties of immobilized microorganisms. For these reasons, the article summarizes recent scientific reports about the use of natural carriers in bioremediation, including efficiency, the impact of the carrier on microorganisms and contamination, and the nature of the conducted research. © 2016 Pontificia Universidad Católica de Valparaíso. Production and hosting by Elsevier B.V. All rights reserved.},

note = {223},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84971602981,

title = {Bacillus thuringiensis B1(2015b) is a Gram-Positive Bacteria Able to Degrade Naproxen and Ibuprofen},

author = { A. Marchlewicz and D. Domaradzka and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84971602981&doi=10.1007%2fs11270-016-2893-0&partnerID=40&md5=ef678be69f18fb39e03d8138a3438e72},

doi = {10.1007/s11270-016-2893-0},

issn = {00496979},

year  = {2016},

date = {2016-01-01},

journal = {Water, Air, and Soil Pollution},

volume = {227},

number = {6},

publisher = {Springer International Publishing},

abstract = {A Gram-positive bacterium, designated as strain B1(2015b), was isolated from the soil of the chemical factory “Organika-Azot” in Jaworzno, Poland. On the basis of 16S rRNA gene sequence analysis, the isolated strain was classified as a Bacillus thuringiensis species. Strain B1(2015b) is able to degrade ibuprofen and naproxen, however, these compounds are not sufficient carbon sources for this strain. In the presence of glucose, Bacillus thuringiensis B1(2015b) degrades ibuprofen and naproxen with higher efficiency. Twenty milligrams per liter of ibuprofen was degraded within 6 days and 6 mg l−1 of naproxen was removed within 35 days. Simultaneously, the growth of the bacterial culture was observed. The obtained results suggest that Bacillus thuringiensis B1(2015b) appears to be a powerful and useful tool in the bioremediation of non-steroidal anti-inflammatory drugs-contaminated environment. © 2016, The Author(s).},

note = {68},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-85013041866,

title = {Metabolic responses of bacterial cells to immobilization},

author = { J. Żur and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85013041866&doi=10.3390%2fmolecules21070958&partnerID=40&md5=1f7385e8358d6c18fb2becd7c931b2d4},

doi = {10.3390/molecules21070958},

issn = {14203049},

year  = {2016},

date = {2016-01-01},

journal = {Molecules},

volume = {21},

number = {7},

publisher = {MDPI AG},

abstract = {In recent years immobilized cells have commonly been used for various biotechnological applications, e.g., antibiotic production, soil bioremediation, biodegradation and biotransformation of xenobiotics in wastewater treatment plants. Although the literature data on the physiological changes and behaviour of cells in the immobilized state remain fragmentary, it is well documented that in natural settings microorganisms are mainly found in association with surfaces, which results in biofilm formation. Biofilms are characterized by genetic and physiological heterogeneity and the occurrence of altered microenvironments within the matrix. Microbial cells in communities display a variety of metabolic differences as compared to their free-living counterparts. Immobilization of bacteria can occur either as a natural phenomenon or as an artificial process. The majority of changes observed in immobilized cells result from protection provided by the supports. Knowledge about the main physiological responses occurring in immobilized cells may contribute to improving the efficiency of immobilization techniques. This paper reviews the main metabolic changes exhibited by immobilized bacterial cells, including growth rate, biodegradation capabilities, biocatalytic efficiency and plasmid stability. © 2016 by the authors; licensee MDPI.},

note = {93},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84992727831,

title = {Toxicity of diclofenac and its biotransformation by Raoultella sp. DD4},

author = { D. Domaradzka and U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84992727831&doi=10.15244%2fpjoes%2f62681&partnerID=40&md5=28aa684d23e71c5a99cb3676c6892d13},

doi = {10.15244/pjoes/62681},

issn = {12301485},

year  = {2016},

date = {2016-01-01},

journal = {Polish Journal of Environmental Studies},

volume = {25},

number = {5},

pages = {2211-2216},

publisher = {HARD Publishing Company},

abstract = {In recent years the increased consumption of diclofenac, a biologically active compound that is toxic to organisms and persistent to biodegradation, has resulted in its presence in the environment. This is the first report on the biotransformation of diclofenac by a pure bacterial strain, Raoultella sp. DD4, which is able to transform 0.6 mg/L of diclofenac in 28 days. Additionally, strain DD4 is more resistant to diclofenac than other tested organisms. The estimated value for EC50 for this strain is 1.95 g/L. This is approximately five-fold higher than the value of microbial toxic concentration MTCavg (0.416 g/L). Moreover, genotoxicity studies have indicated that diclofenac is not a mutagenic compound. © 2016, HARD Publishing Company. All rights reserved.},

note = {15},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84978405481,

title = {Enzymes involved in naproxen degradation by Planococcus sp. S5},

author = { D. Wojcieszyńska and D. Domaradzka and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84978405481&doi=10.5604%2f17331331.1204477&partnerID=40&md5=2691aff2112e1850d1b9042cb8b8f85f},

doi = {10.5604/17331331.1204477},

issn = {17331331},

year  = {2016},

date = {2016-01-01},

journal = {Polish Journal of Microbiology},

volume = {65},

number = {2},

pages = {177-182},

publisher = {Polish Society of Microbiologists},

abstract = {Naproxen is a one of the most popular non-steroidal anti-inflammatory drugs (NSAIDs) entering the environment as a result of high consumption. For this reason, there is an emerging need to recognize mechanisms of its degradation and enzymes engaged in this process. Planococcus sp. S5 is a gram positive strain able to degrade naproxen in monosubstrate culture (27%). However, naproxen is not a sufficient growth substrate for this strain. In the presence of benzoate, 4-hydroxybenzoic acid, 3,4-dihydroxybenzoic acid or vanillic acid as growth substrates, the degradation of 21.5%, 71.71%, 14.75% and 8.16% of naproxen was observed respectively. It was shown that the activity of monooxygenase, hydroxyquinol 1,2-dioxygenase, protocatechuate 3,4-dioxygenase and protocatechuate 4,5-dioxyegnase in strain S5 was induced after growth of the strain with naproxen and 4-hydroxybenzoate. Moreover, in the presence of naproxen activity of gentisate 1,2-dioxygenase, enzyme engaged in 4-hydroxybenzoate metabolism, was completely inhibited. The obtained results suggest that monooxygenase and hydroxyquinol 1,2-dioxygenase are the main enzymes in naproxen degradation by Planococcus sp. S5.},

note = {10},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84940743637,

title = {A single amino acid substitution within catalytically non-active N-terminal domain of catechol 2,3-dioxygenase (C23O) increases enzyme activity towards 4-chlorocatechol},

author = { K.T. Hupert-Kocurek and D. Wojcieszyńska and U. Guzik and T. Borowski},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84940743637&doi=10.1016%2fj.molcatb.2015.08.012&partnerID=40&md5=275aad1c1e7797a2d062496f181bdd67},

doi = {10.1016/j.molcatb.2015.08.012},

issn = {13811177},

year  = {2015},

date = {2015-01-01},

journal = {Journal of Molecular Catalysis B: Enzymatic},

volume = {122},

pages = {64-71},

publisher = {Elsevier},

abstract = {In this work we have shown for the first time the effect of Met65Thr substitution on the activity of catechol 2,3-dioxygenase (C23O) from Planococcus sp. strain S5. Even though the 3D model does not reveal the influence of an amino acid substitution on the enzyme active site structure, the Thr65 variant differed in lower pH optimum and lower Km from the wild type enzyme. Activity measurements with various catechols as the substrates showed almost 1.5-times higher activity of the mutant protein in comparison to the wild type enzyme against 4-methylcatechol and its remarkably high activity towards 4-chlorocatechol. From the computational studies it follows that the difference in activity of the wild type and mutant form of C23O towards 4-chlorocatechol is most likely linked to the shift of the pH optimum caused by the presence of the two additional H-bonds between Ser307 and Thr65 which anchor the C-terminal fragment of the protein. This work reveals the role of the N-terminal domain, which is considered to be catalytically inactive, in modulation of the C23O activity and the obtained results may facilitate the engineering of C23Os for bioremediation of environments contaminated with chloroaromatic compounds. © 2015 Elsevier B.V. All rights reserved.},

note = {2},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84942905402,

title = {Over-the-Counter Monocyclic Non-Steroidal Anti-Inflammatory Drugs in Environment - Sources, Risks, Biodegradation},

author = { A. Marchlewicz and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84942905402&doi=10.1007%2fs11270-015-2622-0&partnerID=40&md5=6929a3f705a50f9a8f11507a5a6bcdff},

doi = {10.1007/s11270-015-2622-0},

issn = {00496979},

year  = {2015},

date = {2015-01-01},

journal = {Water, Air, and Soil Pollution},

volume = {226},

number = {10},

publisher = {Kluwer Academic Publishers},

abstract = {Recently, the increased use of monocyclic non-steroidal anti-inflammatory drugs has resulted in their presence in the environment. This may have potential negative effects on living organisms. The biotransformation mechanisms of monocyclic non-steroidal anti-inflammatory drugs in the human body and in other mammals occur by hydroxylation and conjugation with glycine or glucuronic acid. Biotransformation/biodegradation of monocyclic non-steroidal anti-inflammatory drugs in the environment may be caused by fungal or bacterial microorganisms. Salicylic acid derivatives are degraded by catechol or gentisate as intermediates which are cleaved by dioxygenases. The key intermediate of the paracetamol degradation pathways is hydroquinone. Sometimes, after hydrolysis of this drug, 4-aminophenol is formed, which is a dead-end metabolite. Ibuprofen is metabolized by hydroxylation or activation with CoA, resulting in the formation of isobutylocatechol. The aim of this work is to attempt to summarize the knowledge about environmental risk connected with the presence of over-the-counter anti-inflammatory drugs, their sources and the biotransformation and/or biodegradation pathways of these drugs. © 2015 The Author(s).},

note = {19},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84939420469,

title = {Cometabolic Degradation of Naproxen by Planococcus sp. Strain S5},

author = { D. Domaradzka and U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84939420469&doi=10.1007%2fs11270-015-2564-6&partnerID=40&md5=c6345d970a9664b6683b8176b417f511},

doi = {10.1007/s11270-015-2564-6},

issn = {00496979},

year  = {2015},

date = {2015-01-01},

journal = {Water, Air, and Soil Pollution},

volume = {226},

number = {9},

publisher = {Kluwer Academic Publishers},

abstract = {Naproxen is a non-steroidal anti-inflammatory drug frequently detected in the influent and effluent of sewage treatment plants. The Gram-positive strain Planococcus sp. S5 was able to remove approximately 30 % of naproxen after 35 days of incubation in monosubstrate culture. Under cometabolic conditions, with glucose or phenol as a growth substrate, the degradation efficiency of S5 increased. During 35 days of incubation, 75.14∈±∈1.71 % and 86.27∈±∈2.09 % of naproxen was degraded in the presence of glucose and phenol, respectively. The highest rate of naproxen degradation observed in the presence of phenol may be connected with the fact that phenol is known to induce enzymes responsible for aromatic ring cleavage. The activity of phenol monooxygenase, naphthalene monooxygenase, and hydroxyquinol 1,2-dioxygenase was indicated in Planococcus sp. S5 culture with glucose or phenol as a growth substrate. It is suggested that these enzymes may be engaged in naproxen degradation. © 2015 The Author(s).},

note = {37},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84937764047,

title = {Biodegradation and biotransformation of polycyclic non-steroidal anti-inflammatory drugs},

author = { D. Domaradzka and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84937764047&doi=10.1007%2fs11157-015-9364-8&partnerID=40&md5=d889e71c2a8a0d85773294ffacafb68f},

doi = {10.1007/s11157-015-9364-8},

issn = {15691705},

year  = {2015},

date = {2015-01-01},

journal = {Reviews in Environmental Science and Biotechnology},

volume = {14},

number = {2},

pages = {229-239},

publisher = {Kluwer Academic Publishers},

abstract = {In recent years the increased use of polycyclic non-steroidal anti-inflammatory drugs has resulted in their presence in the environment. This in turn may cause potential negative effects on living organisms. While the biotransformation mechanisms of polycyclic non-steroidal anti-inflammatory drugs in the human body and in other mammals have been extensively studied, degradation of these drugs by microorganisms has seldom been investigated and is largely unknown. Biotransformation/biodegradation of polycyclic non-steroidal anti-inflammatory drugs is caused by fungal microorganisms, mainly white-rot fungi, and a few strains of bacteria. However, hitherto only complete degradation of olsazine was described. The first step of the transformation is most often hydroxylation catalyzed by cytochrom P-450 monooxygenases, or oxygenation by laccases and three peroxidases: lignin peroxidase, manganese-dependent peroxidase and versatile peroxidase manganese-dependent peroxidase. The aim of this work is to summarize the knowledge about the biotransformation and/or biodegradation of polycyclic non-steroidal anti-inflammatory drugs and to present their biotransformation pathways. © 2015, The Author(s).},

note = {49},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84937202609,

title = {Properties, occurrence and biodegradation of ibuprofen in aquatic environment [Włäciwöci, występowanie i biodegradacja ibuprofenu w ̈rodowisku wodnym]},

author = { A. Marchlewicz and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84937202609&partnerID=40&md5=d9667d774d8c187ab4d602e0aa4a3774},

issn = {12306169},

year  = {2015},

date = {2015-01-01},

journal = {Ochrona Srodowiska},

volume = {37},

number = {1},

pages = {65-70},

publisher = {Polskie Zrzeszenie Inzynierow},

abstract = {Common use of non-steroidal anti-inflammatory drugs (NSAIDs), including ibuprofen, leads to drug presence in sewage but also in surface waters, which they enter with municipal treatment plants effluent. As a result, the drugs may also be found in tap water. Due to low ibuprofen concentration in aquatic environment, acute toxicity is not observed. Yet, continuous exposure of aquatic organisms to the drug makes it important to study chronic toxicity mechanisms. Moreover, knowledge of ibuprofen migration and the time course of its biodegradation in the aquatic environment is incomplete. Only a few microorganism species (mainly fungi) able to metabolize ibuprofen have been described. The current research suggests that ibuprofen biotransformation proceeds by its hydroxylation to 1,2-dihydroxyibuprofen. Sphingomonas spp. Ibu-2 is the only described bacterial strain able to use ibuprofen as a sole carbon and energy source. Thioestrification is the first step in ibuprofen degradation. Then, propionic chain is removed with simultaneous oxidation of aromatic ring to 4-isobutylcatechol, which is then cleaved by extradiol enzymes. Knowledge of pathways of NSAID metabolism will allow for more effective removal of such pollutants from municipal wastewater, resulting in a significant improvement of surface water quality.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84904109255,

title = {Bacterial degradation of naproxen - Undisclosed pollutant in the environment},

author = { D. Wojcieszyńska and D. Domaradzka and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84904109255&doi=10.1016%2fj.jenvman.2014.06.023&partnerID=40&md5=8396bf85baa6f3cffdfdc91db000d0b7},

doi = {10.1016/j.jenvman.2014.06.023},

issn = {03014797},

year  = {2014},

date = {2014-01-01},

journal = {Journal of Environmental Management},

volume = {145},

pages = {157-161},

publisher = {Academic Press},

abstract = {The presence of non-steroidal anti-inflammatory drugs (NSAIDs) in the environment is an emerging problem due to their potential influence on human health and biocenosis. This is the first report on the biotransformation of naproxen, a polycyclic NSAID, by a bacterial strain. Stenotrophomonas maltophilia KB2 transformed naproxen within 35 days with about 28% degradation efficiency. Under cometabolic conditions with glucose or phenol as a carbon source degradation efficiency was 78% and 40%, respectively. Moreover, in the presence of naproxen phenol monooxygenase, naphthalene dioxygenase, hydroxyquinol 1,2-dioxygenase and gentisate 1,2-dioxygenase were induced. This suggests that degradation of naproxen occurs by its hydroxylation to 5,7,8-trihydroxynaproxen, an intermediate that can be cleaved by hydroxyquinol 1,2-dioxygenase. The cleavage product is probably further oxidatively cleaved by gentisate 1,2-dioxygenase. The obtained results provide the basis for the use of cometabolic systems in the bioremediation of polycyclic NSAID-contaminated environments. © 2014 Elsevier Ltd.},

note = {68},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84923059995,

title = {Altering substrate specificity of catechol 2,3-dioxygenase from Planococcus sp. strain S5 by random mutagenesis},

author = { K.T. Hupert-Kocurek and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84923059995&partnerID=40&md5=583f83c3e86789051898035ee0a692d8},

issn = {0001527X},

year  = {2014},

date = {2014-01-01},

journal = {Acta Biochimica Polonica},

volume = {61},

number = {4},

pages = {705-710},

publisher = {Polskie Towarzystwo Biochemiczne},

abstract = {c23o gene, encoding catechol 2,3-dioxygenase from Planococcus sp. strain S5 was randomly mutagenized to generate variant forms of the enzyme with higher degradation activity. Additionally, the effect of introduced mutations on the enzyme structure was analyzed based on the putative 3D models the wild-type and mutant enzymes. C23OB58 and C23OB81 mutant proteins with amino acid substitutions in close proximity to the enzyme surface or at the interface and in the vicinity of the enzyme active site respectively showed the lowest activity towards all catecholic substrates. The relative activity of C23OC61 mutant towards para-substituted catechols was 20-30% lower of the wild-type enzyme. In this mutant all changes: F191I, C268R, Y272H, V280A and Y293D were located within the conserved regions of C-terminal domain. From these F191I seems to have significant implications for enzyme activity. The highest activity towards different catechols was found for mutant C23OB65. R296Q mutation improved the activity of C23O especially against 4-chlorocatechol. The relative activity of above-mentioned mutant detected against this substrate was almost 6-fold higher than the wild-type enzyme. These results should facilitate future engineering of the enzyme for bioremediation.},

note = {2},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84904793107,

title = {Immobilization as a strategy for improving enzyme properties- Application to oxidoreductases},

author = { U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84904793107&doi=10.3390%2fmolecules19078995&partnerID=40&md5=5182d5114ec3a4f8a2b47ed06ec70d6a},

doi = {10.3390/molecules19078995},

issn = {14203049},

year  = {2014},

date = {2014-01-01},

journal = {Molecules},

volume = {19},

number = {7},

pages = {8995-9018},

publisher = {MDPI AG},

abstract = {The main objective of the immobilization of enzymes is to enhance the economics of biocatalytic processes. Immobilization allows one to re-use the enzyme for an extended period of time and enables easier separation of the catalyst from the product. Additionally, immobilization improves many properties of enzymes such as performance in organic solvents, pH tolerance, heat stability or the functional stability. Increasing the structural rigidity of the protein and stabilization of multimeric enzymes which prevents dissociation-related inactivation. In the last decade, several papers about immobilization methods have been published. In our work, we present a relation between the influence of immobilization on the improvement of the properties of selected oxidoreductases and their commercial value. We also present our view on the role that different immobilization methods play in the reduction of enzyme inhibition during biotechnological processes.},

note = {352},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84902906788,

title = {Protocatechuate 3,4-dioxygenase: A wide substrate specificity enzyme isolated from stenotrophomonas maltophilia kb2 as a useful tool in aromatic acid biodegradation},

author = { U. Guzik and K.T. Hupert-Kocurek and M. Sitnik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84902906788&doi=10.1159%2f000362791&partnerID=40&md5=5f82d3db26962e7883a672ef42262ad1},

doi = {10.1159/000362791},

issn = {14641801},

year  = {2014},

date = {2014-01-01},

journal = {Journal of Molecular Microbiology and Biotechnology},

volume = {24},

number = {3},

pages = {150-160},

publisher = {S. Karger AG},

abstract = {Protocatechuate 3,4-dioxygenases (P34Os) catalyze the reaction of the ring cleavage of aromatic acid derivatives. It is a key reaction in many xenobiotic metabolic pathways. P34Os characterize narrow substrate specificity. This property is an unfavorable feature in the biodegradation process because one type of pollution is rarely present in the environment. Thus, the following study aimed at the characterization of a P34O from Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic carboxylic acids. A total of 3 mM vanillic acid and 4-hydroxybenzoate were completely degraded during 8 and 4.5 h, respectively. When cells of strain KB2 were grown on 9 mM 4-hydroxybenzoate, P34O was induced. Biochemical analysis revealed that the examined enzyme was similar to other known P34Os, but showed untypical wide substrate specificity. A high activity of P34O against 2,4-and 3,5-dihydroxybenzoate was observed. As these substrates do not possess ortho configuration hydroxyl groups, it is postulated that their cleavage could be connected with their monodentate binding of substrate to the active site. Since this enzyme characterizes untypical wide substrate specificity it makes it a useful tool in applications for environmental clean-up purposes. © 2014 S. Karger AG, Basel.},

note = {8},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84900542945,

title = {Microbial degradation non-steroidal anti-inflammatory drugs [Mikrobiologiczna degradacja niesteroidowych leków przeciwzapalnych]},

author = { U. Guzik and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84900542945&partnerID=40&md5=5f88d768025e13d5c3de1fb8fb1e8b59},

issn = {00794252},

year  = {2014},

date = {2014-01-01},

journal = {Postepy Mikrobiologii},

volume = {53},

number = {1},

pages = {61-69},

publisher = {Polish Society of Microbiologists},

abstract = {In the recent years, commonly used non-steroidal anti-inflammatory drugs (NSAIDs) are widely detected in the environment. These biologically active substances and their continuous inflow into the environment may lead to their accumulation in the environment and chronic exposure of organisms. This in turn may cause the potential negative effects on living organisms. While the transformation mechanisms of non-steroidal anti-inflammatory drugs in the human body and in other animals have been extensively studied, degradation of these drugs by bacteria (including their degradation pathways and degradation products) has seldom been investigated and are largely unknown. Therefore, the objective of this paper is presentation actual stage of knowledge about microbiological degradation pathways of NSAIDs such as naproxen, ibuprofen, diclofenac, paracetamol.},

note = {1},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84900540401,

title = {Directed evolution of microbial enzymes [Ukierunkowana ewolucja enzymów pochodzenia mikrobiologicznego]},

author = { K.T. Hupert-Kocurek and A. Banaś and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84900540401&partnerID=40&md5=5c7b16858f67f10bb0d6751ffd78290b},

issn = {00794252},

year  = {2014},

date = {2014-01-01},

journal = {Postepy Mikrobiologii},

volume = {53},

number = {1},

pages = {43-48},

publisher = {Polish Society of Microbiologists},

abstract = {Enzymes of microbial origin are extensively used in different industrial processes. However, very often these biocatalysts do not meet the requirements for a large-scale application and its properties have to be optimized. This includes not only the chemoselectivity, regioselectivity and stereoselectivity, but also long-term stability of the biocatalyst at certain temperatures or pH-values and activity in the presence of high substrate concentrations. Protein engineering has emerged as an important tool to overcome the limitations of natural enzymes as biocatalysts. There are two general strategies for protein engineering, rational design and directed evolution. In rational design detailed knowledge of the structure and function of the protein is used to make desired changes. Directed evolution involves either a random mutagenesis of the gene encoding the enzyme (e.g. by error-prone PCR) or recombination of gene fragments derived from DNase degradation, random priming recombination, random chimeragenesis on transient templates or recombined extension on truncated templates. In this review the essential methods for directed evolution of enzymes are described and various examples for the application of these protein engineering tools are provided.},

note = {1},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84896333493,

title = {Activity of a carboxyl-terminal truncated form of catechol 2,3-dioxygenase from Planococcus sp. S5},

author = { K.T. Hupert-Kocurek and D. Wojcieszyńska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84896333493&doi=10.1155%2f2014%2f598518&partnerID=40&md5=0cf405fd62db07759b5d5d007c553600},

doi = {10.1155/2014/598518},

issn = {1537744X},

year  = {2014},

date = {2014-01-01},

journal = {The Scientific World Journal},

volume = {2014},

publisher = {ScientificWorld Ltd.},

abstract = {Catechol 2,3-dioxygenases (C23Os; E.C.1.13.12.2) are two domain enzymes that catalyze degradation of monoaromatic hydrocarbons. The catalytically active C-domain of all known C23Os comprises ferrous ion ligands as well as residues forming active site pocket. The aim of this work was to examine and discuss the effect of nonsense mutation at position 289 on the activity of catechol 2,3-dioxygenase from Planococcus strain. Although the mutant C23O showed the same optimal temperature for activity as the wild-type protein (35°C), it exhibited activity slightly more tolerant to alkaline pH. Mutant enzyme exhibited also higher affinity to catechol as a substrate. Its K m (66.17 μM) was approximately 30% lower than that of wild-type enzyme. Interestingly, removal of the C-terminal residues resulted in 1.5- to 1.8-fold (P < 0.05) increase in the activity of C23OB61 against 4-methylcatechol and 4-chlorocatechol, respectively, while towards catechol the activity of the protein dropped to about 80% of that of the wild-type enzyme. The results obtained may facilitate the engineering of the C23O for application in the bioremediation of polluted areas. © 2014 Katarzyna Hupert-Kocurek et al.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84896328434,

title = {Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel},

author = { U. Guzik and K.T. Hupert-Kocurek and A. Marchlewicz and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84896328434&doi=10.1016%2fj.ejbt.2014.02.001&partnerID=40&md5=bc1dbc1301015a0aa17997acb14c24e0},

doi = {10.1016/j.ejbt.2014.02.001},

issn = {07173458},

year  = {2014},

date = {2014-01-01},

journal = {Electronic Journal of Biotechnology},

volume = {17},

number = {2},

pages = {83-88},

publisher = {Electronic Journal of Biotechnology},

abstract = {Background:In biodegradation processes free enzymes often undergo deactivation. Thus, it is very important to obtain highly stable enzymes by different methods. Immobilization allows for successful stabilization of many multimeric enzymes by increasing the rigidity of the enzyme structure. This study aimed to evaluate some environmental factors that affect catechol 1,2-dioxygenase from Stenotrophomonas maltophilia KB2 immobilized in alginate hydrogel. The goal of the present work was to improve the functional stability of the enzyme by increas-ing its structural rigidity.Results:Immobilization yield and expressed activity were 100% and 56%, respectively. Under the same storage conditions, the activity of the immobilized enzyme was still observed on the 28th day of incubation at 4 °C, whereas the free enzyme lost its activity after 14 days. The immobilized enzyme required approximately 10 °C lower temperature for its optimal activity than the free enzyme. Immobilization shifted the optimal pH from 8 for the soluble enzyme to 7 for the immobilized enzyme. The immobilized catechol 1,2-dioxygenase showed ac-tivity against 3-methylcatechol, 4-methylcatechol, 3-chlorocatechol, 4-chlorocatechol, and 3,5-dichlorocatechol. The immobilization of the enzyme promoted its stabilization against any distorting agents:aliphatic alcohols, phenols, and chelators.Conclusions:The entrapment of the catechol 1,2-dioxygenase from S. maltophilia KB2 has been shown to be an effective method for improving the functional properties of the enzyme. Increased resistance to inactivation by higher substrate concentration and other factors affecting enzyme activity as well as broadened substrate spec-ificity compared to the soluble enzyme. makes the immobilized catechol 1,2-dioxygenase suitable for the biore-mediation and detoxification of xenobiotic-contaminated environments. © 2014 Pontificia Universidad Católica de Valparaiso. Production and hosting by Elsevier B.V.All rights reserved.},

note = {38},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84896106164,

title = {Degradation potential of protocatechuate 3,4-dioxygenase from crude extract of Stenotrophomonas maltophilia strain KB2 immobilized in calcium alginate hydrogels and on glyoxyl agarose},

author = { U. Guzik and K.T. Hupert-Kocurek and M. Krysiak and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84896106164&doi=10.1155%2f2014%2f138768&partnerID=40&md5=a294b2c485472dba4d58232c4766944d},

doi = {10.1155/2014/138768},

issn = {23146133},

year  = {2014},

date = {2014-01-01},

journal = {BioMed Research International},

volume = {2014},

publisher = {Hindawi Publishing Corporation},

abstract = {Microbial intradiol dioxygenases have been shown to have a great potential for bioremediation; however, their structure is sensitive to various environmental and chemical agents. Immobilization techniques allow for the improvement of enzyme properties. This is the first report on use of glyoxyl agarose and calcium alginate as matrixes for the immobilization of protocatechuate 3,4-dioxygenase. Multipoint attachment of the enzyme to the carrier caused maintenance of its initial activity during the 21 days. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose resulted in decrease in the optimum temperature by 5°C and 10°C, respectively. Entrapment of the enzyme in alginate gel shifted its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose did not influence pH profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate showed increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme was observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protected it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. © 2014 Urszula Guzik et al.},

note = {29},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84886902253,

title = {Original research influence of the entrapment of catechol 2, 3-dioxygenase in K-carrageenan on its properties},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84886902253&partnerID=40&md5=cda5edce73b129f04c79b1e44f10af3d},

issn = {12301485},

year  = {2013},

date = {2013-01-01},

journal = {Polish Journal of Environmental Studies},

volume = {22},

number = {4},

pages = {1219-1225},

abstract = {Microbial extradiol dioxygenases have a great potential in bioremediation, but their structure is very sensitive to various environmental and chemical agents. Immobilization techniques make the enzyme properties' improvement possible. This is the first report of the usage of κ-carrageenan as a matrix for the immobilization of catechol 2, 3-dioxygenase. The storage stability of entrapped catechol 2, 3-dioxygenase from Stenotrophomonas maltophilia KB2 in K-carrageenan hydrogel at 4°C was found up to 14 days, while the free enzyme lost its activity within 24 hours. The immobilization of dioxygenase decreased the optimum temperature by 10°C, while both soluble and immobilized enzyme showed similar pH properties. The Km, V max' and Hill constant values for the immobilized enzyme were 0.17 μM, 106.68 mU, and 1.00, respectively. The immobilized catechol 2, 3-dioxygenase showed higher activity against 3-methylcatechol, hydroquinone, and tetrachlorohydroquinone than the soluble enzyme. Immobilization of catechol 2, 3-dioxygenase protected the enzyme from inhibition and enhanced its resistance to inactivation during catalysis.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84880412155,

title = {Microbiological degradation of cinnamic acid and its hydroxyl-derivatives [Mikrobiologiczny rozkład kwasu cynamonowego i jego hydroksypochodnych]},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84880412155&partnerID=40&md5=263b0c3101f164e4545c723d556bd0bb},

issn = {00794252},

year  = {2013},

date = {2013-01-01},

journal = {Postepy Mikrobiologii},

volume = {52},

number = {2},

pages = {135-141},

abstract = {Microbiological degradation of cinnamic acid and its hydroxyl-derivatives occurs via aerobic or anaerobic pathway. The first step in the biodegradation of these compounds, both aerobic and anaerobic, is β-oxidation. The key intermediate in this process is benzoyl-CoA. In anaerobic environment this intermediate can be transformed to acetyl-CoA, incorporated into the central metabolism. Under aerobic condition benzoyl-CoA is transformed to protocatechuate acid, gentisic acid or catechol, compounds which are cleaved by a specific dioxygenase. Many microorganisms can transform phenolic acid to an amino acid or other compounds such as which 4-hydroxybenzoic acid, amide, acetophenone, which can be used in industry.},

note = {2},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84878773526,

title = {Factors affecting activity of catechol 2,3-dioxygenase from 2-chlorophenol-degrading Stenotrophomonas maltophilia strain KB2},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84878773526&doi=10.3109%2f10242422.2013.796456&partnerID=40&md5=10f2c988ff519061818471fe0cee20d2},

doi = {10.3109/10242422.2013.796456},

issn = {10242422},

year  = {2013},

date = {2013-01-01},

journal = {Biocatalysis and Biotransformation},

volume = {31},

number = {3},

pages = {141-147},

abstract = {The effect of phenol on 2-chloro-and 2,4-dichlorophenol degradation by Stenotrophomonas maltophilia KB2 has been studied. During this study, we observed induction of catechol 2,3-dioxygenase (C23O). Since, in the environment, compounds which inhibit C23O activity are frequently present together with the main dioxygenase substrates, the main aim of this work was to determine the influence of various inhibitors and activators on the enzyme activity. Hydrogen peroxide of 60 μM concentration caused total inhibition of the enzyme. Addition of ascorbic acid suppressed the inhibitory effect of hydrogen peroxide. In its presence, 60 μM hydrogen peroxide caused only 40% inhibition of C23O activity. A positive effect in preventing C23O activity was observed also in the presence of chelators (8-hydroxyquinoline; EDTA; and phenanthroline). Most metal ions and aliphatic and aromatic hydroxylated derivatives caused a 20-40% decrease in enzyme activity. The results obtained indicate that C23O from Stenotrophomonas maltophilia strain KB2 holds great potential for bioremediation. © 2013 Informa UK, Ltd.},

note = {19},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84878300907,

title = {High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production},

author = { U. Guzik and K.T. Hupert-Kocurek and M. Sitnik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84878300907&doi=10.1007%2fs10482-013-9910-8&partnerID=40&md5=7ce52572f3232df5ba623a1babae57c1},

doi = {10.1007/s10482-013-9910-8},

issn = {00036072},

year  = {2013},

date = {2013-01-01},

journal = {Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology},

volume = {103},

number = {6},

pages = {1297-1307},

abstract = {This is the first report of a catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 with high activity against catechol and its methyl derivatives. This enzyme was maximally active at pH 8.0 and 40 C and the half-life of the enzyme at this temperature was 3 h. Kinetic studies showed that the value of K m and V max was 12.8 μM and 1,218.8 U/mg of protein, respectively. During our studies on kinetic properties of the catechol 1,2-dioxygenase we observed substrate inhibition at >80 μM. The nucleotide sequence of the gene encoding the S. maltophilia strain KB2 catechol 1,2-dioxygenase has high identity with other catA genes from members of the genus Pseudomonas. The deduced 314-residue sequence of the enzyme corresponds to a protein of molecular mass 34.5 kDa. This enzyme was inhibited by competitive inhibitors (phenol derivatives) only by ca. 30 %. High tolerance against condition changes is desirable in industrial processes. Our data suggest that this enzyme could be of use as a tool in production of cis,cis-muconic acid and its derivatives. © 2013 The Author(s).},

note = {43},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84877246424,

title = {Cinnamic acid and its hydroxy derivatives. Synthesis and application [Kwas cynamonowy i jego hydroksypochodne. Synteza i praktyczne zastosowania]},

author = { U. Guzik and K.T. Hupert-Kocurek and P. Siupka and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84877246424&partnerID=40&md5=0b74e0b28297a7e939a1f5cef04d4779},

issn = {00332496},

year  = {2013},

date = {2013-01-01},

journal = {Przemysl Chemiczny},

volume = {92},

number = {4},

pages = {458-462},

abstract = {A review, with 39 refs., of methods for chem. and biochem. synthesis of cinnamic, p-cumaric and 2,3-dihydroxycinnamic acids as well as their further enzymatic conversion to the org. intermediates.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84874217080,

title = {Influence of metal ions on bioremediation activity of protocatechuate 3,4-dioxygenase from Stenotrophomonas maltophilia KB2},

author = { U. Guzik and K.T. Hupert-Kocurek and K. Sałek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84874217080&doi=10.1007%2fs11274-012-1178-z&partnerID=40&md5=86f3dd431848ce37007a515dd5292ff3},

doi = {10.1007/s11274-012-1178-z},

issn = {09593993},

year  = {2013},

date = {2013-01-01},

journal = {World Journal of Microbiology and Biotechnology},

volume = {29},

number = {2},

pages = {267-273},

publisher = {Kluwer Academic Publishers},

abstract = {The aim of this paper was to describe the effect of various metal ions on the activity of protocatechuate 3,4-dioxygenase from Stenotrophomonas maltophilia KB2. We also compared activity of different dioxygenases isolated from this strain, in the presence of metal ions, after induction by various aromatic compounds. S. maltophilia KB2 degraded 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation. In the presence of dihydroxybenzoate and benzoate, the activity of protocatechuate 3,4-dioxygenase and catechol 1,2-dioxygenase was observed. Although Fe3+, Cu2+, Zn2+, Co2+, Al3+, Cd2+, Ni2+ and Mn2+ ions caused 20-80 % inhibition of protocatechuate 3,4-dioxygenase activity, the above-mentioned metal ions (with the exception of Ni2+) inhibited catechol 1,2-dioxygenase to a lesser extent or even activate the enzyme. Retaining activity of at least one of three dioxygenases from strain KB2 in the presence of metal ions makes it an ideal bacterium for bioremediation of contaminated areas. © 2012 The Author(s).},

note = {18},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84873602961,

title = {Modern research methods for determining structures of intradiol dioxygenases},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and M. Sitnik and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84873602961&partnerID=40&md5=6b3050b542ed55718620248ffa34b80c},

issn = {00092886},

year  = {2012},

date = {2012-01-01},

journal = {Chemik},

volume = {66},

number = {12},

pages = {1346-1351},

abstract = {[No abstract available]},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84860695543,

title = {Properties of catechol 2,3-dioxygenase from crude extract of Stenotrophomonas maltophilia strain KB2 immobilized in calcium alginate hydrogels},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and A. Jankowska and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84860695543&doi=10.1016%2fj.bej.2012.04.008&partnerID=40&md5=14ce296ada4edc670232a088b10ab730},

doi = {10.1016/j.bej.2012.04.008},

issn = {1369703X},

year  = {2012},

date = {2012-01-01},

journal = {Biochemical Engineering Journal},

volume = {66},

pages = {1-7},

abstract = {In this paper we report the immobilization of catechol 2,3-dioxygenase from Stenotrophomonas maltophilia KB2 in alginate hydrogel with the aim of improving its functional stability by increasing structural rigidity of the enzyme. Immobilization yield and expressed activity were 49.4% and 49.4%, respectively. The storage stability of entrapped catechol 2,3-dioxygenase at 4°C was found up to 35 days (266.3mU/mg protein), while at 4°C the free enzyme lost its activity within 24h. Immobilization of dioxygenase increased the optimum temperature for activity by 10°C, while both soluble and immobilized enzyme showed maximum activity at the same pH. The K m, V max, and Hill constant values for immobilized enzyme were 0.2μM, 604.6mU/mg protein, and 1.00, respectively, whereas those for the free enzyme were 46.3μM, 1602.0mU/mg protein, and 4.1, respectively.The immobilized catechol 2,3-dioxygenase from KB2 strain showed relatively higher activity against 3-methylcatechol, 4-methylcatechol, 4,5-dichlorocatechol, 3,5-dichlorocatechol, hydroquinone and tetrachlorohydroquinone than soluble enzyme. Immobilization of catechol 2,3-dioxygenase from KB2 strain protected the enzyme from the inhibition and enhanced its resistance to inactivation during catalysis. That makes the enzyme suitable for the bioremediation and detoxification of xenobiotic-contaminated environments. © 2012 Elsevier B.V.},

note = {47},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84873735799,

title = {Characterization of catechol 2,3-dioxygenase from Planococcus sp. Strain S5 induced by high phenol concentration},

author = { K.T. Hupert-Kocurek and U. Guzik and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84873735799&doi=10.18388%2fabp.2012_2119&partnerID=40&md5=3f041e2a5c776d1ff6b9128cb2de66d0},

doi = {10.18388/abp.2012_2119},

issn = {0001527X},

year  = {2012},

date = {2012-01-01},

journal = {Acta Biochimica Polonica},

volume = {59},

number = {3},

pages = {345-351},

publisher = {Acta Biochimica Polonica},

abstract = {This study aimed at characterization of a new catechol 2,3-dioxygenase isolated from a Gram-positive bacterium able to utilize phenol as the sole carbon and energy source. Planococcus sp. strain S5 grown on 1 or 2 mM phenol showed activity of both a catechol 1,2- and catechol 2,3-dioxygenase while at a higher concentrations of phenol only catechol 2,3-dioxygenase activity was observed. The enzyme was optimally active at 60oC and pH 8.0. Kinetic studies showed that the Km and Vmax of the enzyme were 42.70 μM and 329.96 mU, respectively. The catechol 2,3-dioxygenase showed the following relative meta-cleavage activities for various catechols tested: catechol (100%), 3-methylcatechol (13.67%), 4-methylcatechol (106.33%) and 4-chlorocatechol (203.80%). The high reactivity of this enzyme towards 4-chlorocatechol is different from that observed for other catechol 2,3-dioxygenases. Nucleotide sequencing and homology search revealed that the gene encoding the S5 catechol 2,3-dioxygenase shared the greatest homology with the known genes encoding isoenzymes from Gram-negative Pseudomonas strains.},

note = {49},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84871698384,

title = {Flavin-dependent enzymes in cancer prevention},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84871698384&doi=10.3390%2fijms131216751&partnerID=40&md5=b25adf177d623e0f4756ba5f2245acb6},

doi = {10.3390/ijms131216751},

issn = {16616596},

year  = {2012},

date = {2012-01-01},

journal = {International Journal of Molecular Sciences},

volume = {13},

number = {12},

pages = {16751-16768},

publisher = {MDPI AG},

abstract = {Statistical studies have demonstrated that various agents may reduce the risk of cancer's development. One of them is activity of flavin-dependent enzymes such as flavin-containing monooxygenase (FMO)GS-OX1, FAD-dependent 5,10-methylenetetrahydrofolate reductase and flavin-dependent monoamine oxidase. In the last decade, many papers concerning their structure, reaction mechanism and role in the cancer prevention were published. In our work, we provide a more in-depth analysis of flavin-dependent enzymes and their contribution to the cancer prevention. We present the actual knowledge about the glucosinolate synthesized by flavin-containing monooxygenase (FMO)GS-OX1 and its role in cancer prevention, discuss the influence of mutations in FAD-dependent 5,10-methylenetetrahydrofolate reductase on the cancer risk, and describe FAD as an important cofactor for the demethylation of histons. We also present our views on the role of riboflavin supplements in the prevention against cancer. © 2012 by the authors; licensee MDPI, Basel, Switzerland.},

note = {14},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-80052438366,

title = {Microbial degradation of chlorophenols, hazardous wastes of chemical industry [Mikrobiologiczny rozkład chlorofenoli, uciaz•liwych odpadów przemyłu chemicznege]},

author = { D. Wojcieszyńska and U. Guzik and K.T. Hupert-Kocurek and P. Siupka},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-80052438366&partnerID=40&md5=cbe5c3b9fad5e79642baf6df3e961fb0},

issn = {00332496},

year  = {2011},

date = {2011-01-01},

journal = {Przemysl Chemiczny},

volume = {90},

number = {8},

pages = {1515-1519},

abstract = {A review, with 56 refs., of metabolic path ways for biochem. degrdn. of persistant Cl-contg. phenols, esp. via resp. chlorocatechols.},

note = {1},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-79961208826,

title = {High activity catechol 2,3-dioxygenase from the cresols - Degrading Stenotrophomonas maltophilia strain KB2},

author = { D. Wojcieszyńska and K.T. Hupert-Kocurek and I. Greń and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-79961208826&doi=10.1016%2fj.ibiod.2011.06.006&partnerID=40&md5=d6ef4d868b72531ce18499c1a567eb7c},

doi = {10.1016/j.ibiod.2011.06.006},

issn = {09648305},

year  = {2011},

date = {2011-01-01},

journal = {International Biodeterioration and Biodegradation},

volume = {65},

number = {6},

pages = {853-858},

abstract = {This study aimed at characterization of catechol 2,3-dioxygenase from Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. 2-methylphenol, 3-methylphenol, and 4-methylphenol was completely degraded during 24 h in concentration 6 mM, 7 mM, and 5 mM, respectively. When cells of strain KB2 were growing on methylphenols, catechol 2,3-dioxygenase was induced. Biochemical analysis revealed that the examined enzyme was similar to another catechol 2,3-dioxygenases, but showed extremely high activity. The enzyme was optimally active at 30 °C and pH 7.6. Kinetic studies showed that the value of Km, Vmax and Hill constant was 85.11 μM, 3.08 μM min-1 and 4.09 respectively. Comparative structural and phylogenetic analysis of catechol 2,3-dioxygenase from S. maltophilia KB2 had placed the protein with the single-ring substrate subfamily of the extradiol dioxygenase. We observed the presence of externally located α-helices and internally located β-sheets. We also suggest that the Fe2+ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water. © 2011 Elsevier Ltd.},

note = {31},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-79953107665,

title = {Catechol 1,2-dioxygenase from the new aromatic compounds - Degrading Pseudomonas putida strain N6},

author = { U. Guzik and I. Greń and K.T. Hupert-Kocurek and D. Wojcieszyńska},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-79953107665&doi=10.1016%2fj.ibiod.2011.02.001&partnerID=40&md5=7fa3eb471f0eb2071b4a850b40265e4b},

doi = {10.1016/j.ibiod.2011.02.001},

issn = {09648305},

year  = {2011},

date = {2011-01-01},

journal = {International Biodeterioration and Biodegradation},

volume = {65},

number = {3},

pages = {504-512},

abstract = {This study aimed to characterization of catechol 1,2-dioxygenase from a Gram-negative bacterium, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. Strain designated as N6, was isolated from the activated sludge samples of a sewage treatment plant at Bentwood Furniture Factory Jasienica, Poland. Morphology, physio-biochemical characteristics and phylogenetic analysis based on 16S rDNA sequence indicate that strain belongs to Pseudomonas putida. When cells of strain N6 grown on protocatechuate or 4-hydroxybenzoic acid mainly protocatechuate 3,4-dioxygenase was induced. The activity of catechol 1,2-dioxygenase was rather small. The cells grown on benzoic acid, catechol or phenol showed high activity of only catechol 1,2-dioxygenase. This enzyme was optimally active at 35°C and pH 7.4. Kinetic studies showed that the value of Km and Vmax was 85.19μM and 14.54μMmin-1 respectively. Nucleotide sequence of gene encoding catechol 1,2-dioxygenase in strain N6 has 100% identity with catA genes from two P. putida strains. The deduced 301-residue sequence of enzyme corresponds to a protein of molecular mass 33.1kDa. The deduced molecular structure of the catechol 1,2-dioxygenase from P. putida N6 was very similar and characteristic for the other intradiol dioxygenases. © 2011 Elsevier Ltd.},

note = {45},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-79952572933,

title = {Induction of aromatic ring: Cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems},

author = { D. Wojcieszyńska and U. Guzik and I. Greń and M. Perkosz and K.T. Hupert-Kocurek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-79952572933&doi=10.1007%2fs11274-010-0520-6&partnerID=40&md5=c1266ef2c54e06fa02156c466ae15eed},

doi = {10.1007/s11274-010-0520-6},

issn = {09593993},

year  = {2011},

date = {2011-01-01},

journal = {World Journal of Microbiology and Biotechnology},

volume = {27},

number = {4},

pages = {805-811},

abstract = {Stenotrophomonas maltophilia KB2 is known to produce different enzymes of dioxygenase family. The aim of our studies was to determine activity of these enzymes after induction by benzoic acids in cometabolic systems with nitrophenols. We have shown that under cometabolic conditions KB2 strain degraded 0.25-0.4 mM of nitrophenols after 14 days of incubation. Simultaneously degradation of 3 mM of growth substrate during 1-3 days was observed depending on substrate as well as cometabolite used. From cometabolic systems with nitrophenols as cometabolites and 3,4-dihydroxybenzoate as a growth substrate, dioxygenases with the highest activity of protocatechuate 3,4-dioxygenase were isolated. Activity of catechol 1,2- dioxygenase and protocatechuate 4,5-dioxygenase was not observed. Catechol 2,3-dioxygenase was active only in cultures with 4-nitrophenol. Ability of KB2 strain to induce and synthesize various dioxygenases depending on substrate present in medium makes this strain useful in bioremediation of sites contaminated with different aromatic compounds. © 2010 The Author(s).},

note = {48},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-81355139502,

title = {Modulation of FAD-dependent monooxygenase activity from aromatic compounds-degrading Stenotrophomonas maltophilia strain KB2},

author = { D. Wojcieszyńska and I. Greń and K.T. Hupert-Kocurek and U. Guzik},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-81355139502&doi=10.18388%2fabp.2011_2256&partnerID=40&md5=cf851e7c3fa3a0bbc0603a8971168364},

doi = {10.18388/abp.2011_2256},

issn = {0001527X},

year  = {2011},

date = {2011-01-01},

journal = {Acta Biochimica Polonica},

volume = {58},

number = {3},

pages = {421-426},

publisher = {Acta Biochimica Polonica},

abstract = {The purpose of this study was purification and characterization of phenol monooxygenase from Stenotrophomonas maltophilia strain KB2, enzyme that catabolises phenol and its derivatives through the initial hydroxylation to catechols. The enzyme requires NADH and FAD as a cofactors for activity, catalyses hydroxylation of a wide range of monocyclic phenols, aromatic acids and dihydroxylated derivatives of benzene except for catechol. High activity of this monooxygenase was observed in cell extract of strain KB2 grown on phenol, 2-methylphenol, 3-metylphenol or 4-methylphenol. Ionic surfactants as well as cytochrome P450 inhibitors or 1,4-dioxane, acetone and n-butyl acetate inhibited the enzyme activity, while non-ionic surfactants, chloroethane, ethylbenzene, ethyl acetate, cyclohexane, and benzene enhanced it. These results indicate that the phenol monooxygenase from Stenotrophomonas maltophilia strain KB2 holds great potential for bioremediation.},

note = {6},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-84862875187,

title = {Activity of catechol dioxygenases in the presence of some heavy metal ions: Bioremediation of an environment polluted with aromatic compounds [Badania aktywności dioksygenaz katecholowych w obecności jonów wybranych metali ciȩżkich w aspekcie bioremediacji środowisk zanieczyszczonych zwia̧zkami aromatycznymi]},

author = { U. Guzik and D. Wojcieszyńska and I. Greń and K.T. Hupert-Kocurek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84862875187&partnerID=40&md5=86313da0b90e3633bb0a7ddecc001794},

issn = {12306169},

year  = {2010},

date = {2010-01-01},

journal = {Ochrona Srodowiska},

volume = {32},

number = {1},

pages = {9-13},

abstract = {The strains of Stenotrophomonas maltophilia KB2 and Pseudomonas putida N6 are characterized by an enhanced capacity for degrading aromatic compounds: within five hours of incubation both the strains were found to provide a complete degradation of phenol (3 mmol/dm3). Upon induction with phenol, catechol 2,3-dioxygenase, an enzyme responsible for the meta-cleavage of aromatic compounds, was detected in the Stenotrophomonas maltophilia KB2 strain, whereas in the Pseudomonas putida N6 strain the presence was revealed of catechol 1,2-dioxygenase, an enzyme characteristic of the pathway for the ortho-fission of the aromatic ring. Tests on the sensitivity of the enzymes to metal ions have demonstrated that Zn 2+ ions activated catechol 2,3-dioxygenase in the KB2 strain. The other metal ions were found to be inhibitors of this enzyme. Among the metal ions tested, the Cu 2+ ion was the strongest inhibitor of the two isolated dioxynases. Slightly weaker was the inhibition of catechol 1,2-dioxygenase induced by Cd 2+ and Zn 2+ ions in the N6 strain. The activity of this enzyme increased in the presence of Co 2+ ions. The other ions had no significant influence on the activity of the catechol 1,2-dioxygenase isolated from the N6 strain. The partial activity of both dioxygenases observed upon the application of metal salts suggests that both the strains, Stenotrophomonas maltophilia KB2 and Pseudomonas putida N6, may contribute much to the remediation of an environment polluted with aromatic compounds.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-77951141722,

title = {Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin},

author = { I. Greń and D. Wojcieszyńska and U. Guzik and M. Perkosz and K.T. Hupert-Kocurek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-77951141722&doi=10.1007%2fs11274-009-0172-6&partnerID=40&md5=10c990c0b3a65918797b592059052a18},

doi = {10.1007/s11274-009-0172-6},

issn = {09593993},

year  = {2010},

date = {2010-01-01},

journal = {World Journal of Microbiology and Biotechnology},

volume = {26},

number = {2},

pages = {289-295},

abstract = {Stenotrophomonas maltophilia KB2 used in this study is known to metabolise broad range of aromatic compounds including phenol, some chloro and methylphenols, benzoic acids, catochols and others. To study the applicability of the strain for degradation of mononitrophenols in monosubstrate as well as cometabolic systems its degradation potential in the presence of mononitrophenols or different aromatic compounds of plant origin was tested. Stenotrophomonas maltophilia KB2 strain was not able to degrade any of mononitrophenols used in the single substrate experiments. Effect of additional carbon source on nitrophenols degradation revealed that presence of benzoate, 4-hydroxybenzoate or 3,4-dixydroxybenzoate stimulate transformation of 2-nitrophenol, 3-nitrophenol as well as 4-nitrophenol. Depending on growth substrate and mononitrophenol used, decrease in cometabolite concentration was from 25 to 45%. Obtained results suggest that Stenotrophomonas maltophilia KB2 strain could be potentially used for cometabolic degradation of nitrophenols in the presence of aromatic acids, for the bioremediation of contaminated sites. © 2009 Springer Science+Business Media B.V.},

note = {49},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-77956606126,

title = {Biosynthesis of gallic acid and its application [Biosynteza kwasu galusowego i jego zastosowanie]},

author = { U. Guzik and D. Wojcieszyńska and P. Jaroszek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-77956606126&partnerID=40&md5=456b5b2dce5d9a655e8cb1b4222df1c7},

issn = {08607796},

year  = {2010},

date = {2010-01-01},

journal = {Biotechnologia},

number = {1},

pages = {119-131},

publisher = {Termedia Publishing House Ltd.},

abstract = {Gallic acid belongs to aromatic plant substances (poliphenols). Two main biosynthesis pathways in plants of this compound were described as shikimate and polyketide pathways. Gallic acid is applied in agriculture, where it is used as inhibitor of aflatoxin produced by Aspergillus. Gallic acid is also used in food manufactur, as antioxidant, sweetener or antiseptical and antifungal substance. Furthermore, gallic acid effectively prevents and inhibits diseases' progress. It can be used in the therapy of diabetes type II, neoplastic and allergic diseases or in treatment of arteriosclerosis.},

note = {4},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-77950129328,

title = {Biosynthesis of gallic acid and its application [Biosynteza kwasu galusowego i jego zastosowanie]},

author = { U. Guzik and D. Wojcieszyńska and P. Jaroszek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-77950129328&partnerID=40&md5=6904eda990f61b87e773d483f1011309},

issn = {10158812},

year  = {2010},

date = {2010-01-01},

journal = {South African Journal of Economic and Management Sciences},

volume = {13},

number = {1},

pages = {119-131},

publisher = {AOSIS (pty) Ltd},

abstract = {Gallic acid belongs to aromatic plant substances (poliphenols). Two main biosynthesis pathways in plants of this compound were described as shikimate and polyketide pathways. Gallic acid is applied in agriculture, where it is used as inhibitor of aflatoxin produced by Aspergillus. Gallic acid is also used in food manufactur, as antioxidant, sweetener or antiseptical and antifungal substance. Furthermore, gallic acid effectively prevents and inhibits diseases' progress. It can be used in the therapy of diabetes type II, neoplastic and allergic diseases or in treatment of arteriosclerosis.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-51149097365,

title = {Dioxygenases - The key enzymes in the biodegradation of aromatic compounds [Dioksygenazy - Główne enzymy degradacji zwia̧zkó w aromatycznych]},

author = { U. Guzik and I. Greń and D. Wojcieszyńska and S. Łabuzek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-51149097365&partnerID=40&md5=f18a5821b0637c819e7d792486cd3579},

issn = {08607796},

year  = {2008},

date = {2008-01-01},

journal = {Biotechnologia},

number = {3},

pages = {71-88},

publisher = {Termedia Publishing House Ltd.},

abstract = {Progressing degradation of the natural environment has caused an increased interest in the field of biological treatment of both water and soil polluted with different xenobiotics. Aromatic compounds are considered to be one of the most toxic and weakly degraded xenobiotics. The potential solution of the accelerated environment's pollution problem seems to be the bioremediation - the process using the biological organisms to return the environment altered by contaminants to its original condition. Dioxygenases isolated from the microorganisms can be responsible for hydroxylation of the aromatic ring or for its cleavage. Different types of the cleaving dioxygenases have been distinguished due to the kind of the substrate they preferentially can degrade. Cleavage of the aromatic ring facilitates further degradation of xenobiotics, and therefore the dioxygenases are the key enzymes in the biodegradation process of these xenobiotics.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-34547240731,

title = {Substrate specificity and sensitiveness of phenol monooxygenase from Stenotropbomonas maltopbilia strain KB2 versus their potential application to bioremediation of the environment [Specyficzność substratowa oraz wrażiwość monooksygenazy fenolowej ze szczepu Stenotrophomonas maltophilia KB2 a jej potencjalne zastosowanie w bioremediacji środowiska]},

author = { D. Wojcieszyńska and I. Greń and S. Łabuzek and M. Respondek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-34547240731&partnerID=40&md5=4fc32759232a602f03b9d98cba5d9906},

issn = {08607796},

year  = {2007},

date = {2007-01-01},

journal = {Biotechnologia},

number = {2},

pages = {181-191},

publisher = {Termedia Publishing House Ltd.},

abstract = {Phenol monooxygenase, isolated from Stenotrophomonas maltophilia strain KB2, was sensitive to sodium azide, metals salts except for iron (II) sulfate at concentration of 1 mM, chelate compounds, sulfhydryl agents, lauroylsarcosine Na-salt, SDS and hydrogen peroxide. Slight increase of the enzyme activity was observed in the presence of hexane and ether. The presence of ascorbic acid caused an increase of the enzyme activity. Phenol monooxygenase activity changed significantly depending on the tested aromatic substrate in the reaction mixture and the type of the applied inductor.},

note = {5},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{2-s2.0-24744457078,

title = {Dioxygenases-key enzymes for degradation of aromatic compounds by microorganisms [Dioksygenazy-kluczowe enzymy rozkŁadu zwia̧zków aromatycznych przez drobnoustroje]},

author = { D. Wojcieszyńska and I. Greń and S. Łabuzek},

url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-24744457078&partnerID=40&md5=a4941e3b5b29d9e25531b0f3aad4cc19},

issn = {00794252},

year  = {2005},

date = {2005-01-01},

journal = {Postepy Mikrobiologii},

volume = {44},

number = {1},

pages = {63-70},

abstract = {Oxygen-activating enzymes with mononuclear non-heme active participate in many important metabolic pathways of the environmental significance. The ring dihydroxylation is non-specific preliminary step in the catabolic pathway and plays an important role in the activation of resonance-stabilized aromatic compounds before the subsequent catabolism. Dihydroxylate intermediates such as catechol, hydroxyquinol or protocatechuate are cleavaged between their two hydroxyl groups (ortho cleavage) by catechol 1,2-dioxygenase, hydroxyquinol 1,2-dioxygenase or protocatechuate 3,4-dioxygenase. The iron atom in the pentacoordinate active centre of these enzymes remains in the high-spin Fe (III) state during catalysis. Extradiol dioxygenases catalyze the ring-cleavage at the C-C bond adjacent to the vicinal hydroxyl groups. These dioxygenases typically contain non-heme iron Fe (II) in their active site but have been also shown to be active with Mn (II). The catechol 2,3-dioxygenase catalytic cycle is supposed to comprise a complexion of iron ion by monoanionic catecholate as a bidentate ligand. The ring cleavage reaction is proposed to proceed via an attack of the iron-bound activated oxygen on the nonhydroxylated position vicinal to the carbon atom bearing the phenolate anion. When extradiol dioxygenases cleave 3-chlorocatechol, they usually become inactivated. This inactivation might be caused by the strong chelating activity of 3-chlorocatechol or by suicide inactivation of the enzyme due to the formation of reactive intermediate.},

note = {2},

keywords = {},

pubstate = {published},

tppubtype = {article}

}