Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.3390/catal11101173 http://hdl.handle.net/11449/222490 |
Resumo: | Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that pre-sented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50◦ C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process. |
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Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approachAspergillus japonicusImmobilizationLipaseMontmorillonite KSFLipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that pre-sented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50◦ C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Department of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP)Department of Pharmaceutical-Biochemical Technology School of Pharmaceutical Sciences University of São PauloDepartment of Engineering of Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP)CAPES: 2017/11482-7FAPESP: 2017/11482-7CAPES: 2018/06908-8FAPESP: 2018/06908-8CAPES: 2019/15493-9FAPESP: 2019/15493-9CAPES: 2020/08655-0FAPESP: 2020/08655-0CAPES: 2020/09592-1FAPESP: 2020/09592-1Universidade Estadual Paulista (UNESP)Universidade de São Paulo (USP)Remonatto, Daniela [UNESP]Ferrari, Bárbara Ribeiro [UNESP]Bassan, Juliana Cristina [UNESP]Mussagy, Cassamo Ussemane [UNESP]Santos-Ebinuma, Valéria de Carvalho [UNESP]de Paula, Ariela Veloso [UNESP]2022-04-28T19:44:55Z2022-04-28T19:44:55Z2021-10-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.3390/catal11101173Catalysts, v. 11, n. 10, 2021.2073-4344http://hdl.handle.net/11449/22249010.3390/catal111011732-s2.0-85115791063Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengCatalystsinfo:eu-repo/semantics/openAccess2022-04-28T19:44:55Zoai:repositorio.unesp.br:11449/222490Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T20:27:33.092060Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
title |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
spellingShingle |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach Remonatto, Daniela [UNESP] Aspergillus japonicus Immobilization Lipase Montmorillonite KSF |
title_short |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
title_full |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
title_fullStr |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
title_full_unstemmed |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
title_sort |
Utilization of clay materials as support for aspergillus japonicus lipase: An eco-friendly approach |
author |
Remonatto, Daniela [UNESP] |
author_facet |
Remonatto, Daniela [UNESP] Ferrari, Bárbara Ribeiro [UNESP] Bassan, Juliana Cristina [UNESP] Mussagy, Cassamo Ussemane [UNESP] Santos-Ebinuma, Valéria de Carvalho [UNESP] de Paula, Ariela Veloso [UNESP] |
author_role |
author |
author2 |
Ferrari, Bárbara Ribeiro [UNESP] Bassan, Juliana Cristina [UNESP] Mussagy, Cassamo Ussemane [UNESP] Santos-Ebinuma, Valéria de Carvalho [UNESP] de Paula, Ariela Veloso [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Remonatto, Daniela [UNESP] Ferrari, Bárbara Ribeiro [UNESP] Bassan, Juliana Cristina [UNESP] Mussagy, Cassamo Ussemane [UNESP] Santos-Ebinuma, Valéria de Carvalho [UNESP] de Paula, Ariela Veloso [UNESP] |
dc.subject.por.fl_str_mv |
Aspergillus japonicus Immobilization Lipase Montmorillonite KSF |
topic |
Aspergillus japonicus Immobilization Lipase Montmorillonite KSF |
description |
Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that pre-sented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50◦ C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-10-01 2022-04-28T19:44:55Z 2022-04-28T19:44:55Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.3390/catal11101173 Catalysts, v. 11, n. 10, 2021. 2073-4344 http://hdl.handle.net/11449/222490 10.3390/catal11101173 2-s2.0-85115791063 |
url |
http://dx.doi.org/10.3390/catal11101173 http://hdl.handle.net/11449/222490 |
identifier_str_mv |
Catalysts, v. 11, n. 10, 2021. 2073-4344 10.3390/catal11101173 2-s2.0-85115791063 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Catalysts |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129204648148992 |