A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles
A review of the literature covering research on the immobilization of lipases on hydrophobic supports was performed using systematic mapping (SM) concepts. This approach consists of a rigorous review of the methodology used to catalog evidence, to identify gaps at the frontier of knowledge, to ident...
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Royal Society of Chemistry
2023
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ftcsic:oai:digital.csic.es:10261/359345 2024-06-23T07:47:51+00:00 A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles Guimarães, J.R. Oliveira, K.S.G.C. Gonçalves, M.C.P. Romanelli, J.P. Lopes, L.A. Berenguer-Murcia, I. Fernández-Lafuente, Roberto Tardioli, P.W. Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) Agencia Estatal de Investigación (España) Generalitat Valenciana 2023-09-08 http://hdl.handle.net/10261/359345 https://doi.org/10.1039/d3re00420a https://www.scopus.com/inward/record.uri?eid=2-s2.0-85172897720&doi=10.1039%2fd3re00420a&partnerID=40&md5=f2f1526a26c2a1dcca16df611d9d6741 en eng Royal Society of Chemistry #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-123079OB-I00/ES/CATALIZADORES BASADOS EN MATERIALES DE CARBON PREPARADOS A PARTIR DE BIOMASA PARA LA PRODUCCION DE HIDROGENO VERDE MEDIANTE ELECTROLISIS DE AGUA Y REFORMADO DE BIOMASA/ info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-136535OB-I00/ES/INTEGRACION DE NANOTECNOLOGIA Y DISEÑO DE BIOCATALIZADORES: NUEVAS ESTRATEGIAS PARA ABORDAR LOS PROBLEMAS DE LA COIMMOVILIZACION DE ENZIMAS/ Reaction Chemistry and Engineering Publisher's version https://doi.org/10.1039/D3RE00420A Sí Reaction Chemistry and Engineering, 2023, 8, 2689-2702 20589883 (ISSN) http://hdl.handle.net/10261/359345 doi:10.1039/d3re00420a https://www.scopus.com/inward/record.uri?eid=2-s2.0-85172897720&doi=10.1039%2fd3re00420a&partnerID=40&md5=f2f1526a26c2a1dcca16df611d9d6741 open artículo de revisión 2023 ftcsic https://doi.org/10.1039/d3re00420a10.1039/D3RE00420A 2024-06-04T23:53:00Z A review of the literature covering research on the immobilization of lipases on hydrophobic supports was performed using systematic mapping (SM) concepts. This approach consists of a rigorous review of the methodology used to catalog evidence, to identify gaps at the frontier of knowledge, to identify unknown trends, and to list research groups. Our results show a wide variety of available lipases, including commercial, wild-type and recombinant strains. However, the most commonly used lipases are lipases from Thermomyces lanuginosus (TLL), Candida rugosa (CRL) or Rhizomucor miehei (RML) and lipase B from Candida antarctica (CALB). A wide variety of supports with different degrees of hydrophobicity were identified and the supports activated with a layer of octyl or octadecyl groups were the most commonly used. The advantages of lipase immobilization on these supports are discussed. Among them, the immobilization, purification, stabilization and hyperactivation of lipases in a single step stand out. Moreover, problems related to lipase immobilization by interfacial activation are highlighted (mainly enzyme release). Strategies to overcome these problems include immobilization on heterofunctional supports or intermolecular crosslinking of enzymes immobilized by physical and/or chemical agents. The possibility of increasing the capacity of supports by lipase multilayer immobilization is also discussed. Finally, the structure, distribution of the network and the frequency of co-occurrence between lipases and supports are elucidated to determine the possible hotspots and hitherto unexplored advances in knowledge. © 2023 The Royal Society of Chemistry This work was funded by São Paulo Research Foundation (FAPESP, grant number 2016/10636-8), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior – Brasil (CAPES, Finance Code 001), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, project numbers 405889/2016-0 and 308212/2017-7), Ministerio de Ciencia e Innovación and Agencia Estatal de ... Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
English |
description |
A review of the literature covering research on the immobilization of lipases on hydrophobic supports was performed using systematic mapping (SM) concepts. This approach consists of a rigorous review of the methodology used to catalog evidence, to identify gaps at the frontier of knowledge, to identify unknown trends, and to list research groups. Our results show a wide variety of available lipases, including commercial, wild-type and recombinant strains. However, the most commonly used lipases are lipases from Thermomyces lanuginosus (TLL), Candida rugosa (CRL) or Rhizomucor miehei (RML) and lipase B from Candida antarctica (CALB). A wide variety of supports with different degrees of hydrophobicity were identified and the supports activated with a layer of octyl or octadecyl groups were the most commonly used. The advantages of lipase immobilization on these supports are discussed. Among them, the immobilization, purification, stabilization and hyperactivation of lipases in a single step stand out. Moreover, problems related to lipase immobilization by interfacial activation are highlighted (mainly enzyme release). Strategies to overcome these problems include immobilization on heterofunctional supports or intermolecular crosslinking of enzymes immobilized by physical and/or chemical agents. The possibility of increasing the capacity of supports by lipase multilayer immobilization is also discussed. Finally, the structure, distribution of the network and the frequency of co-occurrence between lipases and supports are elucidated to determine the possible hotspots and hitherto unexplored advances in knowledge. © 2023 The Royal Society of Chemistry This work was funded by São Paulo Research Foundation (FAPESP, grant number 2016/10636-8), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior – Brasil (CAPES, Finance Code 001), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, project numbers 405889/2016-0 and 308212/2017-7), Ministerio de Ciencia e Innovación and Agencia Estatal de ... |
author2 |
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) Agencia Estatal de Investigación (España) Generalitat Valenciana |
format |
Article in Journal/Newspaper |
author |
Guimarães, J.R. Oliveira, K.S.G.C. Gonçalves, M.C.P. Romanelli, J.P. Lopes, L.A. Berenguer-Murcia, I. Fernández-Lafuente, Roberto Tardioli, P.W. |
spellingShingle |
Guimarães, J.R. Oliveira, K.S.G.C. Gonçalves, M.C.P. Romanelli, J.P. Lopes, L.A. Berenguer-Murcia, I. Fernández-Lafuente, Roberto Tardioli, P.W. A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
author_facet |
Guimarães, J.R. Oliveira, K.S.G.C. Gonçalves, M.C.P. Romanelli, J.P. Lopes, L.A. Berenguer-Murcia, I. Fernández-Lafuente, Roberto Tardioli, P.W. |
author_sort |
Guimarães, J.R. |
title |
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
title_short |
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
title_full |
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
title_fullStr |
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
title_full_unstemmed |
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
title_sort |
review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles |
publisher |
Royal Society of Chemistry |
publishDate |
2023 |
url |
http://hdl.handle.net/10261/359345 https://doi.org/10.1039/d3re00420a https://www.scopus.com/inward/record.uri?eid=2-s2.0-85172897720&doi=10.1039%2fd3re00420a&partnerID=40&md5=f2f1526a26c2a1dcca16df611d9d6741 |
long_lat |
ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
geographic |
Rugosa |
geographic_facet |
Rugosa |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
#PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-123079OB-I00/ES/CATALIZADORES BASADOS EN MATERIALES DE CARBON PREPARADOS A PARTIR DE BIOMASA PARA LA PRODUCCION DE HIDROGENO VERDE MEDIANTE ELECTROLISIS DE AGUA Y REFORMADO DE BIOMASA/ info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-136535OB-I00/ES/INTEGRACION DE NANOTECNOLOGIA Y DISEÑO DE BIOCATALIZADORES: NUEVAS ESTRATEGIAS PARA ABORDAR LOS PROBLEMAS DE LA COIMMOVILIZACION DE ENZIMAS/ Reaction Chemistry and Engineering Publisher's version https://doi.org/10.1039/D3RE00420A Sí Reaction Chemistry and Engineering, 2023, 8, 2689-2702 20589883 (ISSN) http://hdl.handle.net/10261/359345 doi:10.1039/d3re00420a https://www.scopus.com/inward/record.uri?eid=2-s2.0-85172897720&doi=10.1039%2fd3re00420a&partnerID=40&md5=f2f1526a26c2a1dcca16df611d9d6741 |
op_rights |
open |
op_doi |
https://doi.org/10.1039/d3re00420a10.1039/D3RE00420A |
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