The DOI matches its Crossref record; 156 of the 156 references it cites were found in a registry or an index.
Developments in support materials for immobilization of oxidoreductases: A comprehensive review
Open accessAbstract
Bioremediation, a biologically mediated transformation or degradation of persistent chemicals into nonhazardous or less-hazardous substances, has been recognized as a key strategy to control levels of pollutants in water and soils. The use of enzymes, notably oxidoreductases such as laccases, tyrosinases, various oxygenases, aromatic dioxygenases, and different peroxidases (all of EC class 1) is receiving significant research attention in this regard. It should be stated that immobilization is emphasized as a powerful tool for enhancement of enzyme activity and stability as well as for protection of the enzyme proteins against negative effects of harsh reaction conditions. As proper selection of support materials for immobilization and their performance is overlooked when it comes to comparing performance of immobilized enzyme in academic studies, this review summarizes the current state of knowledge regarding the materials used for enzyme immobilization of these oxidoreductase enzymes for environmental applications. In the presented study, thorough physicochemical characteristics of the support materials was presented. Moreover, various types of reactions and notably operational modes of enzymatic processes for biodegradation of harmful pollutants are summarized, and future trends in use of immobilized oxidoreductases for environmental applications are discussed. Our goal is to provide an improved foundation on which new technological advancements can be made to achieve efficient enzyme-assisted bioremediation.
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Cites
Alginate: Properties and biomedical applications
Lee, K. Y., & Mooney, D. J. (2012) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2011.06.003 · Cited by 8,095
Improvement of enzyme activity, stability and selectivity via immobilization techniques
Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2007.01.018 · Cited by 3,375
Fungal laccases – occurrence and properties
Baldrian, P. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-4976.2005.00010.x · Cited by 2,179
Enzyme Immobilization: The Quest for Optimum Performance
Sheldon, R. A. (2007) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.200700082 · Cited by 2,077
Bisphenol A and human health: A review of the literature
Rochester, J. R. (2013) · Reproductive Toxicology · doi:10.1016/j.reprotox.2013.08.008 · Cited by 2,018
Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance
Garcia‐Galan, C., Berenguer‐Murcia, Á., Fernandez‐Lafuente, R., & Rodrigues, R. C. (2011) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201100534 · Cited by 1,614
Protein release from alginate matrices
Gombotz, W. R., & Wee, S. F. (2012) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.09.007 · Cited by 1,609
Protein release from alginate matrices
Gombotz, W. (1998) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(97)00124-5 · Cited by 1,550
Horseradish peroxidase: a modern view of a classic enzyme
Veitch, N. C. (2004) · Phytochemistry · doi:10.1016/j.phytochem.2003.10.022 · Cited by 1,379
Industrial use of immobilized enzymes
DiCosimo, R., McAuliffe, J., Poulose, A. J., & Bohlmann, G. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35506c · Cited by 1,266
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Biochar: Production, properties and emerging role as a support for enzyme immobilization
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Bilal, M., Ashraf, S. S., Barceló, D., & Iqbal, H. M. N. (2019) · Science of The Total Environment · doi:10.1016/j.scitotenv.2019.07.224 · Cited by 239
Engineering Biocatalytic Material for the Remediation of Pollutants: A Comprehensive Review
Mishra, B., Varjani, S., Agrawal, D. C., Mandal, S. K., Ngo, H. H., Taherzadeh, M. J., Chang, J.-S., You, S., & Guo, W. (2020) · Environmental Technology & Innovation · doi:10.1016/j.eti.2020.101063 · Cited by 118
Metadata
- Authors
- Zdarta, J., Meyer, A. S., Jesionowski, T., & Pinelo, M.
- Venue
- Advances in Colloid and Interface Science
- Publisher
- Elsevier BV
- Published
- 2018-08
- Volume
- 258
- Pages
- 1-20
- ISSN
- 0001-8686 (ISSN-L)
- OpenAlex
- W2884123032
- Cited by
- 285
- References
- 156
- FWCI
- 10.28
- Type
- journal article
- Language
- en
- Open access
- green
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- Zdarta, J., Meyer, A. S., Jesionowski, T., & Pinelo, M. (2018). Developments in support materials for immobilization of oxidoreductases: A comprehensive review. Advances in Colloid and Interface Science. https://doi.org/10.1016/j.cis.2018.07.004
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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