Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization
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/10.1590/1678-4324-2020190127 http://hdl.handle.net/11449/196904 |
Resumo: | Bioprocess studies have been highlighted due to the importance of physiological processes and industrial applications of enzymes. The potential of peptidase production from Aspergillus section Flavi using different amino acids as a supplemental nitrogen source was investigated. A production profile revealed that amino acids had positive effects on peptidase production when compared to the control without amino acids. Optimal production (100 U/mL) was obtained with Arginine amino acid in 96 h of fermentation. Extracellular peptidase from Aspergillus section Flavi was identified in submerged bioprocesses by in situ activity. Biochemical studies revealed that the maximum activities of the enzyme extract were obtained at pH 6.5 and a temperature of 55 degrees C. The inhibition by EDTA and PMSF suggests the presence of more than one peptidase while the Ni2+ and Cu2+ had a negative influence on the enzyme activity. When the crude extract was reversibly immobilized on ionic supports, DEAE-Agarose and MANAE-Agarose the derivative showed different profiles of thermal and pH stabilities. Hence, this study revealed the basic properties and biochemical characteristics that allowed the production improvement of this class of enzyme. Moreover, with known properties stabilization and immobilization process is required to further explore its biotechnological capacities. |
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Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilizationfilamentous fungiimmobilizationMANAE-agarosesubmerged bioprocessproteaseBioprocess studies have been highlighted due to the importance of physiological processes and industrial applications of enzymes. The potential of peptidase production from Aspergillus section Flavi using different amino acids as a supplemental nitrogen source was investigated. A production profile revealed that amino acids had positive effects on peptidase production when compared to the control without amino acids. Optimal production (100 U/mL) was obtained with Arginine amino acid in 96 h of fermentation. Extracellular peptidase from Aspergillus section Flavi was identified in submerged bioprocesses by in situ activity. Biochemical studies revealed that the maximum activities of the enzyme extract were obtained at pH 6.5 and a temperature of 55 degrees C. The inhibition by EDTA and PMSF suggests the presence of more than one peptidase while the Ni2+ and Cu2+ had a negative influence on the enzyme activity. When the crude extract was reversibly immobilized on ionic supports, DEAE-Agarose and MANAE-Agarose the derivative showed different profiles of thermal and pH stabilities. Hence, this study revealed the basic properties and biochemical characteristics that allowed the production improvement of this class of enzyme. Moreover, with known properties stabilization and immobilization process is required to further explore its biotechnological capacities.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Ribeirao Preto, SP, BrazilSao Paulo State Univ, Dept Biochem & Microbiol, Rio Claro, SP, BrazilCSIC, Inst Invest Ciencias Alimentac CIAL, Campus Univ Autonoma Madrid, Madrid, SpainSao Paulo State Univ, Dept Biochem & Microbiol, Rio Claro, SP, BrazilFAPESP: 2011/06986-0CAPES: 001Inst Tecnologia ParanaUniversidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)CSICGonsales Rosa-Garzon, NathaliaRodrigues de Siqueira, Ana ClaudiaNaomi Hirano, VivianeRodrigues, Andre [UNESP]Costa Pessela, BenevidesCabral, Hamilton2020-12-10T19:59:51Z2020-12-10T19:59:51Z2020-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10application/pdfhttp://dx.doi.org/10.1590/1678-4324-2020190127Brazilian Archives Of Biology And Technology. Curitiba-parana: Inst Tecnologia Parana, v. 63, 10 p., 2020.1516-8913http://hdl.handle.net/11449/19690410.1590/1678-4324-2020190127S1516-89132020000100204WOS:000535195200001S1516-89132020000100204.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBrazilian Archives Of Biology And Technologyinfo:eu-repo/semantics/openAccess2023-11-01T06:08:04Zoai:repositorio.unesp.br:11449/196904Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:34:41.524245Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
title |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
spellingShingle |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization Gonsales Rosa-Garzon, Nathalia filamentous fungi immobilization MANAE-agarose submerged bioprocess protease |
title_short |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
title_full |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
title_fullStr |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
title_full_unstemmed |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
title_sort |
Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization |
author |
Gonsales Rosa-Garzon, Nathalia |
author_facet |
Gonsales Rosa-Garzon, Nathalia Rodrigues de Siqueira, Ana Claudia Naomi Hirano, Viviane Rodrigues, Andre [UNESP] Costa Pessela, Benevides Cabral, Hamilton |
author_role |
author |
author2 |
Rodrigues de Siqueira, Ana Claudia Naomi Hirano, Viviane Rodrigues, Andre [UNESP] Costa Pessela, Benevides Cabral, Hamilton |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) CSIC |
dc.contributor.author.fl_str_mv |
Gonsales Rosa-Garzon, Nathalia Rodrigues de Siqueira, Ana Claudia Naomi Hirano, Viviane Rodrigues, Andre [UNESP] Costa Pessela, Benevides Cabral, Hamilton |
dc.subject.por.fl_str_mv |
filamentous fungi immobilization MANAE-agarose submerged bioprocess protease |
topic |
filamentous fungi immobilization MANAE-agarose submerged bioprocess protease |
description |
Bioprocess studies have been highlighted due to the importance of physiological processes and industrial applications of enzymes. The potential of peptidase production from Aspergillus section Flavi using different amino acids as a supplemental nitrogen source was investigated. A production profile revealed that amino acids had positive effects on peptidase production when compared to the control without amino acids. Optimal production (100 U/mL) was obtained with Arginine amino acid in 96 h of fermentation. Extracellular peptidase from Aspergillus section Flavi was identified in submerged bioprocesses by in situ activity. Biochemical studies revealed that the maximum activities of the enzyme extract were obtained at pH 6.5 and a temperature of 55 degrees C. The inhibition by EDTA and PMSF suggests the presence of more than one peptidase while the Ni2+ and Cu2+ had a negative influence on the enzyme activity. When the crude extract was reversibly immobilized on ionic supports, DEAE-Agarose and MANAE-Agarose the derivative showed different profiles of thermal and pH stabilities. Hence, this study revealed the basic properties and biochemical characteristics that allowed the production improvement of this class of enzyme. Moreover, with known properties stabilization and immobilization process is required to further explore its biotechnological capacities. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-12-10T19:59:51Z 2020-12-10T19:59:51Z 2020-01-01 |
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/10.1590/1678-4324-2020190127 Brazilian Archives Of Biology And Technology. Curitiba-parana: Inst Tecnologia Parana, v. 63, 10 p., 2020. 1516-8913 http://hdl.handle.net/11449/196904 10.1590/1678-4324-2020190127 S1516-89132020000100204 WOS:000535195200001 S1516-89132020000100204.pdf |
url |
http://dx.doi.org/10.1590/1678-4324-2020190127 http://hdl.handle.net/11449/196904 |
identifier_str_mv |
Brazilian Archives Of Biology And Technology. Curitiba-parana: Inst Tecnologia Parana, v. 63, 10 p., 2020. 1516-8913 10.1590/1678-4324-2020190127 S1516-89132020000100204 WOS:000535195200001 S1516-89132020000100204.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Brazilian Archives Of Biology And Technology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
10 application/pdf |
dc.publisher.none.fl_str_mv |
Inst Tecnologia Parana |
publisher.none.fl_str_mv |
Inst Tecnologia Parana |
dc.source.none.fl_str_mv |
Web of Science 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_ |
1808128674059255808 |