Amino Acid Supplementation Improves the Production of Extracellular Peptidases by Aspergillus Section Flavi and their Ionic Immobilization

Detalhes bibliográficos
Autor(a) principal: Gonsales Rosa-Garzon, Nathalia
Data de Publicação: 2020
Outros Autores: Rodrigues de Siqueira, Ana Claudia, Naomi Hirano, Viviane, Rodrigues, Andre [UNESP], Costa Pessela, Benevides, Cabral, Hamilton
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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spelling 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:29462023-11-01T06:08:04Repositório 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
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