Streptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | |
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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Acta scientiarum. Technology (Online) |
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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 |
_version_ |
1799315337432268800 |