Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography

Detalhes bibliográficos
Autor(a) principal: Çorbacı, Cengiz
Data de Publicação: 2021
Outros Autores: Özcan, Kadriye
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Acta scientiarum. Technology (Online)
Texto Completo: http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/51486
Resumo: Microbial enzymes are used as organic catalysts in different industrial processes. In this study, we aimed to produce and investigate alkaline proteases from a novel actinobacterium strain isolated from a Black Sea marine sediment. The optimal production conditions for Streptomyces sp. K47 alkaline proteases was 4-days incubation at 28ºC in a salt-free medium buffered with 50 mM Tris-HCl buffer (pH 9.0) and containing glucose (1.0%, w v-1) and yeast extract (0.5%, w v-1). The enzyme solution was partially purified using (NH4)2SO4 precipitation (40-70%). After desalting, it was purified 1-84 fold with a recovery of 19.42%. Zymogram analyses revealed the presence of more than one protease enzyme. The enzyme solution exhibited maximum activity at pH 9.0 and 37ºC, remaining stable after a 2-hour incubation at all tested conditions. Streptomyces sp. K47 has the potential to be used in industrial processes because of its ability to produce multiple protease enzymes displaying stability in a broad pH and temperature range.
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spelling Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymographyStreptomyces sp. K47 alkaline proteases: partial purification and analysis by zymographyStreptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.Microbial enzymes are used as organic catalysts in different industrial processes. In this study, we aimed to produce and investigate alkaline proteases from a novel actinobacterium strain isolated from a Black Sea marine sediment. The optimal production conditions for Streptomyces sp. K47 alkaline proteases was 4-days incubation at 28ºC in a salt-free medium buffered with 50 mM Tris-HCl buffer (pH 9.0) and containing glucose (1.0%, w v-1) and yeast extract (0.5%, w v-1). The enzyme solution was partially purified using (NH4)2SO4 precipitation (40-70%). After desalting, it was purified 1-84 fold with a recovery of 19.42%. Zymogram analyses revealed the presence of more than one protease enzyme. The enzyme solution exhibited maximum activity at pH 9.0 and 37ºC, remaining stable after a 2-hour incubation at all tested conditions. Streptomyces sp. K47 has the potential to be used in industrial processes because of its ability to produce multiple protease enzymes displaying stability in a broad pH and temperature range.Microbial enzymes are used as organic catalysts in different industrial processes. In this study, we aimed to produce and investigate alkaline proteases from a novel actinobacterium strain isolated from a Black Sea marine sediment. The optimal production conditions for Streptomyces sp. K47 alkaline proteases was 4-days incubation at 28ºC in a salt-free medium buffered with 50 mM Tris-HCl buffer (pH 9.0) and containing glucose (1.0%, w v-1) and yeast extract (0.5%, w v-1). The enzyme solution was partially purified using (NH4)2SO4 precipitation (40-70%). After desalting, it was purified 1-84 fold with a recovery of 19.42%. Zymogram analyses revealed the presence of more than one protease enzyme. The enzyme solution exhibited maximum activity at pH 9.0 and 37ºC, remaining stable after a 2-hour incubation at all tested conditions. Streptomyces sp. K47 has the potential to be used in industrial processes because of its ability to produce multiple protease enzymes displaying stability in a broad pH and temperature range.Universidade Estadual De Maringá2021-06-14info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/5148610.4025/actascitechnol.v43i1.51486Acta Scientiarum. Technology; Vol 43 (2021): Publicação contínua; e51486Acta Scientiarum. Technology; v. 43 (2021): Publicação contínua; e514861806-25631807-8664reponame:Acta scientiarum. Technology (Online)instname:Universidade Estadual de Maringá (UEM)instacron:UEMenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/51486/751375152297Copyright (c) 2021 Acta Scientiarum. Technologyhttp://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessÇorbacı, CengizÖzcan, Kadriye2021-08-09T16:53:19Zoai:periodicos.uem.br/ojs:article/51486Revistahttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/indexPUBhttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/oai||actatech@uem.br1807-86641806-2563opendoar:2021-08-09T16:53:19Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)false
dc.title.none.fl_str_mv Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
title Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
spellingShingle Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
Çorbacı, Cengiz
Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.
Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.
title_short Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
title_full Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
title_fullStr Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
title_full_unstemmed Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
title_sort Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
author Çorbacı, Cengiz
author_facet Çorbacı, Cengiz
Özcan, Kadriye
author_role author
author2 Özcan, Kadriye
author2_role author
dc.contributor.author.fl_str_mv Çorbacı, Cengiz
Özcan, Kadriye
dc.subject.por.fl_str_mv Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.
Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.
topic Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.
Streptomyces sp.; alkaline protease; partial purification; SDS-PAGE; zymography.
description Microbial enzymes are used as organic catalysts in different industrial processes. In this study, we aimed to produce and investigate alkaline proteases from a novel actinobacterium strain isolated from a Black Sea marine sediment. The optimal production conditions for Streptomyces sp. K47 alkaline proteases was 4-days incubation at 28ºC in a salt-free medium buffered with 50 mM Tris-HCl buffer (pH 9.0) and containing glucose (1.0%, w v-1) and yeast extract (0.5%, w v-1). The enzyme solution was partially purified using (NH4)2SO4 precipitation (40-70%). After desalting, it was purified 1-84 fold with a recovery of 19.42%. Zymogram analyses revealed the presence of more than one protease enzyme. The enzyme solution exhibited maximum activity at pH 9.0 and 37ºC, remaining stable after a 2-hour incubation at all tested conditions. Streptomyces sp. K47 has the potential to be used in industrial processes because of its ability to produce multiple protease enzymes displaying stability in a broad pH and temperature range.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-14
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/51486
10.4025/actascitechnol.v43i1.51486
url http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/51486
identifier_str_mv 10.4025/actascitechnol.v43i1.51486
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/51486/751375152297
dc.rights.driver.fl_str_mv Copyright (c) 2021 Acta Scientiarum. Technology
http://creativecommons.org/licenses/by/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Copyright (c) 2021 Acta Scientiarum. Technology
http://creativecommons.org/licenses/by/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Estadual De Maringá
publisher.none.fl_str_mv Universidade Estadual De Maringá
dc.source.none.fl_str_mv Acta Scientiarum. Technology; Vol 43 (2021): Publicação contínua; e51486
Acta Scientiarum. Technology; v. 43 (2021): Publicação contínua; e51486
1806-2563
1807-8664
reponame:Acta scientiarum. Technology (Online)
instname:Universidade Estadual de Maringá (UEM)
instacron:UEM
instname_str Universidade Estadual de Maringá (UEM)
instacron_str UEM
institution UEM
reponame_str Acta scientiarum. Technology (Online)
collection Acta scientiarum. Technology (Online)
repository.name.fl_str_mv Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)
repository.mail.fl_str_mv ||actatech@uem.br
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