Issue 14, 2021

Enzyme entrapment, biocatalyst immobilization without covalent attachment

Abstract

In entrapment an active species, which is often a catalyst, is trapped within a material by a solid or gel forming event; thus, it becomes dispersed within the solid or semi-solid matrix. Entrapment methods can be used to immobilize isolated enzymes and render them more stable, and easier to separate and recycle. Entrapment immobilization methods are well established for whole cell biocatalysis. Despite this the applications of entrapment towards isolated enzyme immobilization have lagged the use of covalent attachment and crosslinking methods. In this review entrapment methods are contrasted with other methods of enzyme immobilization and literature methods of enzyme entrapment are reviewed. A key advantage of this approach is that no formal interaction with the protein is required, but this must be balanced against the threat of enzyme leaching, or introduction of mass transfer limitations. The main methods of entrapment are characterized, and some recent innovations are highlighted.

Graphical abstract: Enzyme entrapment, biocatalyst immobilization without covalent attachment

Article information

Article type
Tutorial Review
Submitted
25 May 2021
Accepted
24 Jun 2021
First published
24 Jun 2021
This article is Open Access
Creative Commons BY license

Green Chem., 2021,23, 4980-5005

Enzyme entrapment, biocatalyst immobilization without covalent attachment

H. T. Imam, P. C. Marr and A. C. Marr, Green Chem., 2021, 23, 4980 DOI: 10.1039/D1GC01852C

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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