Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000401217 |
Resumo: | Qualitative analyses were carried out on solid medium with insoluble collagen 0.25% (w/v) to detect proteases with collagenolytic activity produced by Bacillus sp. In cultures incubated for 24 h, a 23 full factorial design with four repetitions at the center point was developed to analyze the effects and interactions between initial pH, temperature and the concentration of gelatin. Based on the results of the first 23 full factorial design, a successive 23 full factorial design was performed. The most favorable production conditions were found to be 1.5% (w/v) gelatin, pH 9.0 and 37 °C with enzymatic activity of 86.27 U/mL. The enzyme showed optimal activity at 50 °C and pH 9.0, and it was stable over wide pH (7.2-10.0) and temperature (45 °C-60 °C) ranges. These results indicate that Bacillus sp DPUA 1728 is a potential source for producing collagenolytic protease with possible biotechnological applications, such as in the food, cosmetics and leather industries. |
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Brazilian Journal of Microbiology |
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Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soilcollagenolytic proteaseBacillus spfactorial designAmazonian soilQualitative analyses were carried out on solid medium with insoluble collagen 0.25% (w/v) to detect proteases with collagenolytic activity produced by Bacillus sp. In cultures incubated for 24 h, a 23 full factorial design with four repetitions at the center point was developed to analyze the effects and interactions between initial pH, temperature and the concentration of gelatin. Based on the results of the first 23 full factorial design, a successive 23 full factorial design was performed. The most favorable production conditions were found to be 1.5% (w/v) gelatin, pH 9.0 and 37 °C with enzymatic activity of 86.27 U/mL. The enzyme showed optimal activity at 50 °C and pH 9.0, and it was stable over wide pH (7.2-10.0) and temperature (45 °C-60 °C) ranges. These results indicate that Bacillus sp DPUA 1728 is a potential source for producing collagenolytic protease with possible biotechnological applications, such as in the food, cosmetics and leather industries.Sociedade Brasileira de Microbiologia2015-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000401217Brazilian Journal of Microbiology v.46 n.4 2015reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822015005030656info:eu-repo/semantics/openAccessLima,Lorena A.Cruz Filho,Raimundo F.Santos,Januário G. dosSilva,Wilson C.eng2015-12-17T00:00:00Zoai:scielo:S1517-83822015000401217Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2015-12-17T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
title |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
spellingShingle |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil Lima,Lorena A. collagenolytic protease Bacillus sp factorial design Amazonian soil |
title_short |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
title_full |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
title_fullStr |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
title_full_unstemmed |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
title_sort |
Protease with collagenolytic activity produced by Bacillus sp. DPUA 1728 from Amazonian soil |
author |
Lima,Lorena A. |
author_facet |
Lima,Lorena A. Cruz Filho,Raimundo F. Santos,Januário G. dos Silva,Wilson C. |
author_role |
author |
author2 |
Cruz Filho,Raimundo F. Santos,Januário G. dos Silva,Wilson C. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Lima,Lorena A. Cruz Filho,Raimundo F. Santos,Januário G. dos Silva,Wilson C. |
dc.subject.por.fl_str_mv |
collagenolytic protease Bacillus sp factorial design Amazonian soil |
topic |
collagenolytic protease Bacillus sp factorial design Amazonian soil |
description |
Qualitative analyses were carried out on solid medium with insoluble collagen 0.25% (w/v) to detect proteases with collagenolytic activity produced by Bacillus sp. In cultures incubated for 24 h, a 23 full factorial design with four repetitions at the center point was developed to analyze the effects and interactions between initial pH, temperature and the concentration of gelatin. Based on the results of the first 23 full factorial design, a successive 23 full factorial design was performed. The most favorable production conditions were found to be 1.5% (w/v) gelatin, pH 9.0 and 37 °C with enzymatic activity of 86.27 U/mL. The enzyme showed optimal activity at 50 °C and pH 9.0, and it was stable over wide pH (7.2-10.0) and temperature (45 °C-60 °C) ranges. These results indicate that Bacillus sp DPUA 1728 is a potential source for producing collagenolytic protease with possible biotechnological applications, such as in the food, cosmetics and leather industries. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-12-01 |
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=S1517-83822015000401217 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000401217 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822015005030656 |
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 |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.46 n.4 2015 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122207917572096 |