Enzyme co-immobilization: Always the biocatalyst designers' choice…or not?

Diffusion limitations Enzyme inactivation Enzyme reuse Enzyme spatial distribution Enzyme stability Step by step co-immobilization

Journal

Biotechnology advances
ISSN: 1873-1899
Titre abrégé: Biotechnol Adv
Pays: England
ID NLM: 8403708

Informations de publication

Date de publication:
01 11 2021
Historique:
received: 24 03 2020
revised: 24 06 2020
accepted: 24 06 2020
pubmed: 16 7 2020
medline: 3 11 2021
entrez: 16 7 2020
Statut: ppublish

Résumé

The increasing relevance of cascade reactions in biocatalysis has sparked a great interest for enzyme co-immobilization. Enzyme co-immobilization allows access to some kinetic advantages that in some instances are necessary to get the desired product, avoiding side-reactions. However, the kinetic effect is very relevant mainly at the initial reaction rates, while it may be less relevant in the whole reaction course, depending on the kinetic parameters of the involved enzymes. This review not only critically discusses the advantages but also the drawbacks of enzymes co-immobilization: immobilization on the same support and surface, under similar conditions, discarding the whole biocatalyst when one of the co-immobilized enzymes is inactivated. We will discuss when co-immobilization is almost compulsory, when the advantages of co-immobilization may not be enough to compensate their problems and when it should be fully discarded. The co-immobilization of cofactors and enzymes bears special interest, as this can open up the opportunity to the building of artificial cells and extremely complex one-pot transformations. Finally, some recent strategies to overcome some the co-immobilization problems will be presented.

Identifiants

pubmed: 32668324
pii: S0734-9750(20)30081-1
doi: 10.1016/j.biotechadv.2020.107584
pii:
doi:

Substances chimiques

Enzymes, Immobilized 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

107584

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Auteurs

Sara Arana-Peña (S)

Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain.

Diego Carballares (D)

Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain.

Roberto Morellon-Sterlling (R)

Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain.

Ángel Berenguer-Murcia (Á)

Departamento de Química Inorgánica e Instituto Universitario de Materiales, Universidad de Alicante, Alicante 03080, Spain.

Andrés R Alcántara (AR)

Facultad de Farmacia, Departamento de Química en Ciencias Farmacéuticas, Universidad Complutense de Madrid, Plaza de Ramón y Cajal, s/n, 28040 Madrid, Spain.

Rafael C Rodrigues (RC)

Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, P.O. Box 15090, Porto Alegre, RS, Brazil.

Roberto Fernandez-Lafuente (R)

Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain. Electronic address: rfl@icp.csic.es.

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