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Enzyme Immobilization: The Quest for Optimum Performance
Abstract
Immobilization is often the key to optimizing the operational performance of an enzyme in industrial processes, particularly for use in non‐aqueous media. Different methods for the immobilization of enzymes are critically reviewed. The methods are divided into three main categories, viz. (i) binding to a prefabricated support (carrier), (ii) entrapment in organic or inorganic polymer matrices, and (iii) cross‐linking of enzyme molecules. Emphasis is placed on relatively recent developments, such as the use of novel supports, e.g., mesoporous silicas, hydrogels, and smart polymers, novel entrapment methods and cross‐linked enzyme aggregates (CLEAs).
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Cites
Chemistry of Aerogels and Their Applications
Pierre, A. C., & Pajonk, G. M. (2002) · Chemical Reviews · doi:10.1021/cr0101306 · Cited by 2,239
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Self-citationModifying enzyme activity and selectivity by immobilization
Rodrigues, R. C., Ortiz, C., Berenguer-Murcia, Á., Torres, R., & Fernández-Lafuente, R. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35231a · Cited by 1,810
Understanding enzyme immobilisation
Hanefeld, U., Gardossi, L., & Magner, E. (2009) · Chem. Soc. Rev. · doi:10.1039/b711564b · Cited by 1,237
Enzyme immobilization: an update
Homaei, A. A., Sariri, R., Vianello, F., & Stevanato, R. (2013) · Journal of Chemical Biology · doi:10.1007/s12154-013-0102-9 · Cited by 875
(2012) · doi:10.5772/32373 · Cited by 640
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Hartmann, M., & Kostrov, X. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60021a · Cited by 605
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Fernández-Fernández, M., Sanromán, M. Á., & Moldes, D. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.02.013 · Cited by 563
Cantone, S., Ferrario, V., Corici, L., Ebert, C., Fattor, D., Spizzo, P., & Gardossi, L. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35464d · Cited by 447
Immobilisation of enzymes on mesoporous silicate materials
Magner, E. (2013) · Chemical Society Reviews · doi:10.1039/c2cs35450k · Cited by 323
Removal of pharmaceutical compounds in water and wastewater using fungal oxidoreductase enzymes
Naghdi, M., Taheran, M., Brar, S. K., Kermanshahi-pour, A., Verma, M., & Surampalli, R. Y. (2018) · Environmental Pollution · doi:10.1016/j.envpol.2017.11.060 · Cited by 275
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Lassouane, F., Aït-Amar, H., Amrani, S., & Rodriguez-Couto, S. (2019) · Bioresource Technology · doi:10.1016/j.biortech.2018.09.129 · Cited by 251
Biotechnology of non-Saccharomyces yeasts—the ascomycetes
Johnson, E. A. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4497-y · Cited by 193
Datta, S., Veena, R., Samuel, M. S., & Selvarajan, E. (2021) · Environmental Chemistry Letters · doi:10.1007/s10311-020-01081-y · Cited by 159
Horseradish peroxidase (HRP) as a tool in green chemistry
Lopes, G. R., Pinto, D. C. G. A., & Silva, A. M. S. (2014) · RSC Adv. · doi:10.1039/c4ra06094f · Cited by 154
Pellis, A., Herrero Acero, E., Gardossi, L., Ferrario, V., & Guebitz, G. M. (2016) · Polymer International · doi:10.1002/pi.5087 · Cited by 151
Periyasamy, A. P., & Periyasami, S. (2023) · ACS Omega · doi:10.1021/acsomega.2c06374 · Cited by 125
Recent Advances and Applications of Immobilized Enzyme Technologies: A Review
Ali Khan, A., & Alzohairy, M. A. (2010) · Research Journal of Biological Sciences · doi:10.3923/rjbsci.2010.565.575 · Cited by 103
Janović, B. S., Mićić Vićovac, M. L., Vujčić, Z. M., & Vujčić, M. T. (2017) · Environmental Science and Pollution Research · doi:10.1007/s11356-016-8100-4 · Cited by 16
Metadata
- Authors
- Sheldon, R. A.
- Venue
- Advanced Synthesis & Catalysis
- Publisher
- Wiley
- Published
- 2007-06-04
- Volume
- 349
- Issue
- 8-9
- Pages
- 1289-1307
- ISSN
- 1615-4150 (ISSN-L)
- 1615-4169
- OpenAlex
- W2099439711
- Cited by
- 2,077
- References
- 1
- FWCI
- 22.99
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
