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Immobilization of Lipases Using Poly(vinyl) Alcohol

Lipases are very versatile enzymes because they catalyze various hydrolysis and synthesis reactions in a chemo-, regio-, and stereoselective manner. From a practical point of view, immobilization allows the recovery and stabilization of the biocatalyst for its application in different types of biore...

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Detalles Bibliográficos
Autor principal: Guajardo, Nadia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10181104/
https://www.ncbi.nlm.nih.gov/pubmed/37177168
http://dx.doi.org/10.3390/polym15092021
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author Guajardo, Nadia
author_facet Guajardo, Nadia
author_sort Guajardo, Nadia
collection PubMed
description Lipases are very versatile enzymes because they catalyze various hydrolysis and synthesis reactions in a chemo-, regio-, and stereoselective manner. From a practical point of view, immobilization allows the recovery and stabilization of the biocatalyst for its application in different types of bioreactors. Among the various support options for immobilizing lipases is polyvinyl alcohol (PVA), which, when functionalized or combined with other materials, provides different characteristics and properties to the biocatalyst. This review analyzes the multiple possibilities that PVA offers as a material to immobilize lipases when combined with alginate, chitosan, and hydroxypropylmethylcellulose (HPMC), incorporating magnetic properties together with the formation of fibers and microspheres. The articles analyzed in this review were selected using the Scopus database in a range of years from 1999 to 2023, finding a total of 42 articles. The need to expand knowledge in this area is due to the great versatility and scaling possibilities that PVA has as a support for lipase immobilization and its application in different bioreactor configurations.
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spelling pubmed-101811042023-05-13 Immobilization of Lipases Using Poly(vinyl) Alcohol Guajardo, Nadia Polymers (Basel) Review Lipases are very versatile enzymes because they catalyze various hydrolysis and synthesis reactions in a chemo-, regio-, and stereoselective manner. From a practical point of view, immobilization allows the recovery and stabilization of the biocatalyst for its application in different types of bioreactors. Among the various support options for immobilizing lipases is polyvinyl alcohol (PVA), which, when functionalized or combined with other materials, provides different characteristics and properties to the biocatalyst. This review analyzes the multiple possibilities that PVA offers as a material to immobilize lipases when combined with alginate, chitosan, and hydroxypropylmethylcellulose (HPMC), incorporating magnetic properties together with the formation of fibers and microspheres. The articles analyzed in this review were selected using the Scopus database in a range of years from 1999 to 2023, finding a total of 42 articles. The need to expand knowledge in this area is due to the great versatility and scaling possibilities that PVA has as a support for lipase immobilization and its application in different bioreactor configurations. MDPI 2023-04-24 /pmc/articles/PMC10181104/ /pubmed/37177168 http://dx.doi.org/10.3390/polym15092021 Text en © 2023 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Guajardo, Nadia
Immobilization of Lipases Using Poly(vinyl) Alcohol
title Immobilization of Lipases Using Poly(vinyl) Alcohol
title_full Immobilization of Lipases Using Poly(vinyl) Alcohol
title_fullStr Immobilization of Lipases Using Poly(vinyl) Alcohol
title_full_unstemmed Immobilization of Lipases Using Poly(vinyl) Alcohol
title_short Immobilization of Lipases Using Poly(vinyl) Alcohol
title_sort immobilization of lipases using poly(vinyl) alcohol
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10181104/
https://www.ncbi.nlm.nih.gov/pubmed/37177168
http://dx.doi.org/10.3390/polym15092021
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