Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation

Detalhes bibliográficos
Autor(a) principal: Siqueira,Ana Claudia Rodrigues de
Data de Publicação: 2014
Outros Autores: Rosa,Nathalia Gonsales da, Motta,Cristina Maria Souza, Cabral,Hamilton
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400514
Resumo: The aim of this study was to evaluate peptidase production by Aspergillus terreus in solid-state bioprocess and evaluate its parameters. The best conditions were 5.0 g of wheat bran as substrate, incubation temperature 30°C, inoculum 2.0x105spores/g and 75% saline volume, with production reaching 677 U/mL (5400 U/g culture medium) after 72 h of fermentation. Biochemical characterization of the crude enzymatic extract showed the optimum pH and temperature of 6.5 and 55°C, respectively. The stability at different temperatures and pH values showed that the extract could endure different pH. The evaluation of the ions influence and inhibitors proved that the enzyme required an ion for better activity, which was corroborated with the inhibition of EDTA and PMSF, characterizing serine and/or metallo peptidase. The extract was also tested for specific activities and showed promising results for keratinolytic and collagenolytic activities (0.252 and 0.165 OD/mL, respectively).
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spelling Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentationproteasesolid-state fermentationkeratinasewheat branAspergillus terreusThe aim of this study was to evaluate peptidase production by Aspergillus terreus in solid-state bioprocess and evaluate its parameters. The best conditions were 5.0 g of wheat bran as substrate, incubation temperature 30°C, inoculum 2.0x105spores/g and 75% saline volume, with production reaching 677 U/mL (5400 U/g culture medium) after 72 h of fermentation. Biochemical characterization of the crude enzymatic extract showed the optimum pH and temperature of 6.5 and 55°C, respectively. The stability at different temperatures and pH values showed that the extract could endure different pH. The evaluation of the ions influence and inhibitors proved that the enzyme required an ion for better activity, which was corroborated with the inhibition of EDTA and PMSF, characterizing serine and/or metallo peptidase. The extract was also tested for specific activities and showed promising results for keratinolytic and collagenolytic activities (0.252 and 0.165 OD/mL, respectively).Instituto de Tecnologia do Paraná - Tecpar2014-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400514Brazilian Archives of Biology and Technology v.57 n.4 2014reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-8913201402028info:eu-repo/semantics/openAccessSiqueira,Ana Claudia Rodrigues deRosa,Nathalia Gonsales daMotta,Cristina Maria SouzaCabral,Hamiltoneng2015-09-03T00:00:00Zoai:scielo:S1516-89132014000400514Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-09-03T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
title Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
spellingShingle Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
Siqueira,Ana Claudia Rodrigues de
protease
solid-state fermentation
keratinase
wheat bran
Aspergillus terreus
title_short Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
title_full Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
title_fullStr Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
title_full_unstemmed Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
title_sort Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
author Siqueira,Ana Claudia Rodrigues de
author_facet Siqueira,Ana Claudia Rodrigues de
Rosa,Nathalia Gonsales da
Motta,Cristina Maria Souza
Cabral,Hamilton
author_role author
author2 Rosa,Nathalia Gonsales da
Motta,Cristina Maria Souza
Cabral,Hamilton
author2_role author
author
author
dc.contributor.author.fl_str_mv Siqueira,Ana Claudia Rodrigues de
Rosa,Nathalia Gonsales da
Motta,Cristina Maria Souza
Cabral,Hamilton
dc.subject.por.fl_str_mv protease
solid-state fermentation
keratinase
wheat bran
Aspergillus terreus
topic protease
solid-state fermentation
keratinase
wheat bran
Aspergillus terreus
description The aim of this study was to evaluate peptidase production by Aspergillus terreus in solid-state bioprocess and evaluate its parameters. The best conditions were 5.0 g of wheat bran as substrate, incubation temperature 30°C, inoculum 2.0x105spores/g and 75% saline volume, with production reaching 677 U/mL (5400 U/g culture medium) after 72 h of fermentation. Biochemical characterization of the crude enzymatic extract showed the optimum pH and temperature of 6.5 and 55°C, respectively. The stability at different temperatures and pH values showed that the extract could endure different pH. The evaluation of the ions influence and inhibitors proved that the enzyme required an ion for better activity, which was corroborated with the inhibition of EDTA and PMSF, characterizing serine and/or metallo peptidase. The extract was also tested for specific activities and showed promising results for keratinolytic and collagenolytic activities (0.252 and 0.165 OD/mL, respectively).
publishDate 2014
dc.date.none.fl_str_mv 2014-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400514
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000400514
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-8913201402028
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.57 n.4 2014
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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