Microbial lipase: a new approach for a heterogeneous biocatalyst
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , |
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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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 |
|
_version_ |
1808128256508952576 |