Peptidase with Keratinolytic Activity Secreted by Aspergillus terreus During Solid-State Fermentation
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , |
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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Brazilian Archives of Biology and Technology |
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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 |
_version_ |
1750318276418732032 |