The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Agarose and Its Derivatives as Supports for Enzyme Immobilization
Open accessAbstract
Agarose is a polysaccharide obtained from some seaweeds, with a quite particular structure that allows spontaneous gelation. Agarose-based beads are highly porous, mechanically resistant, chemically and physically inert, and sharply hydrophilic. These features—that could be further improved by means of covalent cross-linking—render them particularly suitable for enzyme immobilization with a wide range of derivatization methods taking advantage of chemical modification of a fraction of the polymer hydroxyls. The main properties of the polymer are described here, followed by a review of cross-linking and derivatization methods. Some recent, innovative procedures to optimize the catalytic activity and operational stability of the obtained preparations are also described, together with multi-enzyme immobilized systems and the main guidelines to exploit their performances.
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Cites
Improvement of enzyme activity, stability and selectivity via immobilization techniques
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Enzyme immobilisation in biocatalysis: why, what and how
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Enzyme Immobilization: The Quest for Optimum Performance
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Modifying enzyme activity and selectivity by immobilization
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Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance
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Self-citationMohamad, N. R., Marzuki, N. H. C., Buang, N. A., Huyop, F., & Wahab, R. A. (2015) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2015.1008192 · Cited by 1,440
Enzyme immobilization: an overview on techniques and support materials
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Self-citationBiotechnological Applications of Proteases in Food Technology
Tavano, O. L., Berenguer‐Murcia, A., Secundo, F., & Fernandez‐Lafuente, R. (2018) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12326 · Cited by 294
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Metadata
- Authors
- Zucca, P., Fernandez-Lafuente, R., & Sanjust, E.
- Venue
- Molecules
- Publisher
- MDPI AG
- Published
- 2016-11-19
- Volume
- 21
- Issue
- 11
- Pages
- 1577
- ISSN
- 1420-3049 (ISSN-L)
- OpenAlex
- W2555005084
- Cited by
- 320
- References
- 93
- FWCI
- 11.59
- Type
- journal article
- Language
- en
- Open access
- gold
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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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