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Enzyme immobilization by adsorption: a review
Open accessAbstract
Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes’ low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.
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Citations
Cited by
Zdarta, J., Meyer, A., Jesionowski, T., & Pinelo, M. (2018) · Catalysts · doi:10.3390/catal8020092 · Cited by 934
Self-citation(2012) · doi:10.5772/32373 · Cited by 640
Metal-organic frameworks as novel matrices for efficient enzyme immobilization: An update review
Liang, S., Wu, X.-L., Xiong, J., Zong, M.-H., & Lou, W.-Y. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2019.213149 · Cited by 441
Britton, J., Majumdar, S., & Weiss, G. A. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00906b · Cited by 389
Biochar: Production, properties and emerging role as a support for enzyme immobilization
Pandey, D., Daverey, A., & Arunachalam, K. (2020) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2020.120267 · Cited by 339
Metadata
- Authors
- Jesionowski, T., Zdarta, J., & Krajewska, B.
- Venue
- Adsorption
- Published
- 2014-06-27
- Volume
- 20
- Issue
- 5-6
- Pages
- 801-821
- ISSN
- 0929-5607 (ISSN-L)
- 1572-8757
- OpenAlex
- W1982350871
- Cited by
- 929
- References
- 0
- FWCI
- 12.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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