Stabilization of enzymes via immobilization : Multipoint covalent attachment and other stabilization strategies
Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved..
The use of enzymes in industrial processes requires the improvement of their features in many instances. Enzyme immobilization, a requirement to facilitate the recovery and reuse of these water-soluble catalysts, is one of the tools that researchers may utilize to improve many of their properties. This review is focused on how enzyme immobilization may improve enzyme stability. Starting from the stabilization effects that an enzyme may experience by the mere fact of being inside a solid particle, we detail other possibilities to stabilize enzymes: generation of favorable enzyme environments, prevention of enzyme subunit dissociation in multimeric enzymes, generation of more stable enzyme conformations, or enzyme rigidification via multipoint covalent attachment. In this last point, we will discuss the features of an "ideal" immobilization protocol to maximize the intensity of the enzyme-support interactions. The most interesting active groups in the support (glutaraldehyde, epoxide, glyoxyl and vinyl sulfone) will be also presented, discussing their main properties and uses. Some instances in which the number of enzyme-support bonds is not directly related to a higher stabilization will be also presented. Finally, the possibility of coupling site-directed mutagenesis or chemical modification to get a more intense multipoint covalent immobilization will be discussed.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:52 |
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| Enthalten in: |
Biotechnology advances - 52(2021) vom: 15. Nov., Seite 107821 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Rodrigues, Rafael C [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 14.12.2021 Date Revised 14.12.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.biotechadv.2021.107821 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 0 | |a Stabilization of enzymes via immobilization |b Multipoint covalent attachment and other stabilization strategies |
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| 500 | |a Date Completed 14.12.2021 | ||
| 500 | |a Date Revised 14.12.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved. | ||
| 520 | |a The use of enzymes in industrial processes requires the improvement of their features in many instances. Enzyme immobilization, a requirement to facilitate the recovery and reuse of these water-soluble catalysts, is one of the tools that researchers may utilize to improve many of their properties. This review is focused on how enzyme immobilization may improve enzyme stability. Starting from the stabilization effects that an enzyme may experience by the mere fact of being inside a solid particle, we detail other possibilities to stabilize enzymes: generation of favorable enzyme environments, prevention of enzyme subunit dissociation in multimeric enzymes, generation of more stable enzyme conformations, or enzyme rigidification via multipoint covalent attachment. In this last point, we will discuss the features of an "ideal" immobilization protocol to maximize the intensity of the enzyme-support interactions. The most interesting active groups in the support (glutaraldehyde, epoxide, glyoxyl and vinyl sulfone) will be also presented, discussing their main properties and uses. Some instances in which the number of enzyme-support bonds is not directly related to a higher stabilization will be also presented. Finally, the possibility of coupling site-directed mutagenesis or chemical modification to get a more intense multipoint covalent immobilization will be discussed | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Review | |
| 650 | 4 | |a Enzyme stabilization | |
| 650 | 4 | |a Enzyme-support interactions | |
| 650 | 4 | |a Epoxides | |
| 650 | 4 | |a Glutaraldehyde | |
| 650 | 4 | |a Glyoxyl | |
| 650 | 4 | |a Lipase interfacial activation | |
| 650 | 4 | |a Multimeric enzymes | |
| 650 | 4 | |a Multipoint covalent immobilization | |
| 650 | 4 | |a Vinyl sulfone | |
| 650 | 7 | |a Enzymes, Immobilized |2 NLM | |
| 650 | 7 | |a Sepharose |2 NLM | |
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| 700 | 1 | |a Berenguer-Murcia, Ángel |e verfasserin |4 aut | |
| 700 | 1 | |a Carballares, Diego |e verfasserin |4 aut | |
| 700 | 1 | |a Morellon-Sterling, Roberto |e verfasserin |4 aut | |
| 700 | 1 | |a Fernandez-Lafuente, Roberto |e verfasserin |4 aut | |
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