Microbial lipase: a new approach for a heterogeneous biocatalyst

Detalhes bibliográficos
Autor(a) principal: Tacin, Mariana Vendrasco [UNESP]
Data de Publicação: 2020
Outros Autores: Costa-Silva, Tales A., de Paula, Ariela Veloso [UNESP], Palomo, Jose M., Santos-Ebinuma, Valéria de Carvalho [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1080/10826068.2020.1855442
http://hdl.handle.net/11449/205580
Resumo: Lipases are enzymes employed in several industrial process and their applicability can be increased if these biocatalysts are in the immobilize form. The objective of this work was to study the immobilization of lipase produced by submerged cultivation of Aspergillus sp. by hydrophobic interaction, evaluating its stability and reuse capacity. The immobilization process on octyl-sepharose (C8) and octadecyl-sepabeads (C18) carriers was possible after the removal of oil excess presented in the fermented broth. The results showed that the enzyme was isolated and concentrated in octyl-sepharose with 22% of the initial activity. To increase the amount of enzyme adsorbed on the carrier, 4 immobilization cycles were performed in a row, on the same carrier, with a final immobilization yield of 151.32% and an increase in the specific activity of 136%. The activity test with immobilized lipase showed that the immobilized enzyme maintained 75% of the initial activity after 20 cycles.
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spelling Microbial lipase: a new approach for a heterogeneous biocatalystAdsorptionhydrophobic carrierimmobilizationlipasesLipases are enzymes employed in several industrial process and their applicability can be increased if these biocatalysts are in the immobilize form. The objective of this work was to study the immobilization of lipase produced by submerged cultivation of Aspergillus sp. by hydrophobic interaction, evaluating its stability and reuse capacity. The immobilization process on octyl-sepharose (C8) and octadecyl-sepabeads (C18) carriers was possible after the removal of oil excess presented in the fermented broth. The results showed that the enzyme was isolated and concentrated in octyl-sepharose with 22% of the initial activity. To increase the amount of enzyme adsorbed on the carrier, 4 immobilization cycles were performed in a row, on the same carrier, with a final immobilization yield of 151.32% and an increase in the specific activity of 136%. The activity test with immobilized lipase showed that the immobilized enzyme maintained 75% of the initial activity after 20 cycles.Department of Engineering Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP)Department of Biocatalysis Institute of Catalysis (ICP-CSIC)Department of Pharmacy School of Pharmaceutical Sciences University of São Paulo (USP)Department of Engineering Bioprocesses and Biotechnology School of Pharmaceutical Sciences São Paulo State University (UNESP)Universidade Estadual Paulista (Unesp)Institute of Catalysis (ICP-CSIC)Universidade de São Paulo (USP)Tacin, Mariana Vendrasco [UNESP]Costa-Silva, Tales A.de Paula, Ariela Veloso [UNESP]Palomo, Jose M.Santos-Ebinuma, Valéria de Carvalho [UNESP]2021-06-25T10:17:49Z2021-06-25T10:17:49Z2020-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1080/10826068.2020.1855442Preparative Biochemistry and Biotechnology.1532-22971082-6068http://hdl.handle.net/11449/20558010.1080/10826068.2020.18554422-s2.0-85097537229Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPreparative Biochemistry and Biotechnologyinfo:eu-repo/semantics/openAccess2021-10-23T14:54:29Zoai:repositorio.unesp.br:11449/205580Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T13:38:08.553369Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Microbial lipase: a new approach for a heterogeneous biocatalyst
title Microbial lipase: a new approach for a heterogeneous biocatalyst
spellingShingle Microbial lipase: a new approach for a heterogeneous biocatalyst
Tacin, Mariana Vendrasco [UNESP]
Adsorption
hydrophobic carrier
immobilization
lipases
title_short Microbial lipase: a new approach for a heterogeneous biocatalyst
title_full Microbial lipase: a new approach for a heterogeneous biocatalyst
title_fullStr Microbial lipase: a new approach for a heterogeneous biocatalyst
title_full_unstemmed Microbial lipase: a new approach for a heterogeneous biocatalyst
title_sort Microbial lipase: a new approach for a heterogeneous biocatalyst
author Tacin, Mariana Vendrasco [UNESP]
author_facet Tacin, Mariana Vendrasco [UNESP]
Costa-Silva, Tales A.
de Paula, Ariela Veloso [UNESP]
Palomo, Jose M.
Santos-Ebinuma, Valéria de Carvalho [UNESP]
author_role author
author2 Costa-Silva, Tales A.
de Paula, Ariela Veloso [UNESP]
Palomo, Jose M.
Santos-Ebinuma, Valéria de Carvalho [UNESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Institute of Catalysis (ICP-CSIC)
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Tacin, Mariana Vendrasco [UNESP]
Costa-Silva, Tales A.
de Paula, Ariela Veloso [UNESP]
Palomo, Jose M.
Santos-Ebinuma, Valéria de Carvalho [UNESP]
dc.subject.por.fl_str_mv Adsorption
hydrophobic carrier
immobilization
lipases
topic Adsorption
hydrophobic carrier
immobilization
lipases
description Lipases are enzymes employed in several industrial process and their applicability can be increased if these biocatalysts are in the immobilize form. The objective of this work was to study the immobilization of lipase produced by submerged cultivation of Aspergillus sp. by hydrophobic interaction, evaluating its stability and reuse capacity. The immobilization process on octyl-sepharose (C8) and octadecyl-sepabeads (C18) carriers was possible after the removal of oil excess presented in the fermented broth. The results showed that the enzyme was isolated and concentrated in octyl-sepharose with 22% of the initial activity. To increase the amount of enzyme adsorbed on the carrier, 4 immobilization cycles were performed in a row, on the same carrier, with a final immobilization yield of 151.32% and an increase in the specific activity of 136%. The activity test with immobilized lipase showed that the immobilized enzyme maintained 75% of the initial activity after 20 cycles.
publishDate 2020
dc.date.none.fl_str_mv 2020-01-01
2021-06-25T10:17:49Z
2021-06-25T10:17:49Z
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/10.1080/10826068.2020.1855442
Preparative Biochemistry and Biotechnology.
1532-2297
1082-6068
http://hdl.handle.net/11449/205580
10.1080/10826068.2020.1855442
2-s2.0-85097537229
url http://dx.doi.org/10.1080/10826068.2020.1855442
http://hdl.handle.net/11449/205580
identifier_str_mv Preparative Biochemistry and Biotechnology.
1532-2297
1082-6068
10.1080/10826068.2020.1855442
2-s2.0-85097537229
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Preparative Biochemistry and Biotechnology
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
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