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Metal-organic frameworks for enzyme immobilization and nanozymes: A laccase-focused review.

Authors :
Alvarado-Ramírez L
Machorro-García G
López-Legarrea A
Trejo-Ayala D
Rostro-Alanis MJ
Sánchez-Sánchez M
Blanco RM
Rodríguez-Rodríguez J
Parra-Saldívar R
Source :
Biotechnology advances [Biotechnol Adv] 2024 Jan-Feb; Vol. 70, pp. 108299. Date of Electronic Publication: 2023 Dec 10.
Publication Year :
2024

Abstract

Laccases are natural catalysts with remarkable catalytic activity. However, their application is limited by their lack of stability. Metal-organic frameworks (MOFs) have emerged as a promising alternative for enzyme immobilization. Enzymes can be immobilized in MOFs via two approaches: postsynthetic immobilization and in situ immobilization. In postsynthetic immobilization, an enzyme is embedded after MOF formation by covalent interactions or adsorption. In contrast, in in situ immobilization, a MOF is formed in the presence of an enzyme. Additionally, MOFs have exhibited intrinsic enzyme-like activity. These materials, known as nanozymes when they have the ability to replace enzymes in certain catalytic processes, have multiple key advantages, such as low cost, easy preparation, and large surface areas. This review presents a general overview of the most recent advances in both enzyme@MOF biocatalysts and MOF-based nanozymes in different applications, with a focus on laccase, which is one of the most widely investigated enzymes with excellent industrial potential.<br />Competing Interests: Declaration of Competing Interest The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.<br /> (Copyright © 2023. Published by Elsevier Inc.)

Details

Language :
English
ISSN :
1873-1899
Volume :
70
Database :
MEDLINE
Journal :
Biotechnology advances
Publication Type :
Academic Journal
Accession number :
38072099
Full Text :
https://doi.org/10.1016/j.biotechadv.2023.108299