Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae
Autor(a) principal: | |
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Data de Publicação: | 2015 |
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=S1516-89132015000200175 |
Resumo: | In this study, extracellular alkaline protease was produced from Rhizopus oryzae in submerged fermentation using dairy waste (whey) as a substrate. Fermentation kinetics was studied and various parameters were optimized. The strain produced maximum protease at initial medium pH of 6.0 medium depth of 26 mm, inoculum size of 2% at incubation temperature of 35ºC for 168 h of fermentation. Alkaline protease was purified to homogeneity by ammonium sulphate fractionation followed by sephadex G-100 chromatography. The molecular mass of alkaline protease was 69 kDa determined by 10% SDS-PAGE. The optimum pH and temperature of alkaline protease was 9.0 and 40ºC, respectively. Metal profile of the enzyme showed that the enzyme was non-metallic in nature. The Km , Kcat , Vmax and Kcat/Km values of purified protease were 7.0 mg/mL, 3.8 x102S-1, 54.30 µmol/min and 54.28 s-1mg -1.mL respectively, using casein as substrate. The purified alkaline protease had stability with commercial detergents. |
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Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzaeKineticsPurificationCharacterizationProteasedetergent stabilityRhizopus oryzaeIn this study, extracellular alkaline protease was produced from Rhizopus oryzae in submerged fermentation using dairy waste (whey) as a substrate. Fermentation kinetics was studied and various parameters were optimized. The strain produced maximum protease at initial medium pH of 6.0 medium depth of 26 mm, inoculum size of 2% at incubation temperature of 35ºC for 168 h of fermentation. Alkaline protease was purified to homogeneity by ammonium sulphate fractionation followed by sephadex G-100 chromatography. The molecular mass of alkaline protease was 69 kDa determined by 10% SDS-PAGE. The optimum pH and temperature of alkaline protease was 9.0 and 40ºC, respectively. Metal profile of the enzyme showed that the enzyme was non-metallic in nature. The Km , Kcat , Vmax and Kcat/Km values of purified protease were 7.0 mg/mL, 3.8 x102S-1, 54.30 µmol/min and 54.28 s-1mg -1.mL respectively, using casein as substrate. The purified alkaline protease had stability with commercial detergents.Instituto de Tecnologia do Paraná - Tecpar2015-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000200175Brazilian Archives of Biology and Technology v.58 n.2 2015reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-8913201400071info:eu-repo/semantics/openAccessMushtaq,ZareenaIrfan,MuhammadNadeem,MuhammadNaz,MammonaSyed,Quratulaineng2015-10-08T00:00:00Zoai:scielo:S1516-89132015000200175Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-10-08T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
title |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
spellingShingle |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae Mushtaq,Zareena Kinetics Purification Characterization Protease detergent stability Rhizopus oryzae |
title_short |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
title_full |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
title_fullStr |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
title_full_unstemmed |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
title_sort |
Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae |
author |
Mushtaq,Zareena |
author_facet |
Mushtaq,Zareena Irfan,Muhammad Nadeem,Muhammad Naz,Mammona Syed,Quratulain |
author_role |
author |
author2 |
Irfan,Muhammad Nadeem,Muhammad Naz,Mammona Syed,Quratulain |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Mushtaq,Zareena Irfan,Muhammad Nadeem,Muhammad Naz,Mammona Syed,Quratulain |
dc.subject.por.fl_str_mv |
Kinetics Purification Characterization Protease detergent stability Rhizopus oryzae |
topic |
Kinetics Purification Characterization Protease detergent stability Rhizopus oryzae |
description |
In this study, extracellular alkaline protease was produced from Rhizopus oryzae in submerged fermentation using dairy waste (whey) as a substrate. Fermentation kinetics was studied and various parameters were optimized. The strain produced maximum protease at initial medium pH of 6.0 medium depth of 26 mm, inoculum size of 2% at incubation temperature of 35ºC for 168 h of fermentation. Alkaline protease was purified to homogeneity by ammonium sulphate fractionation followed by sephadex G-100 chromatography. The molecular mass of alkaline protease was 69 kDa determined by 10% SDS-PAGE. The optimum pH and temperature of alkaline protease was 9.0 and 40ºC, respectively. Metal profile of the enzyme showed that the enzyme was non-metallic in nature. The Km , Kcat , Vmax and Kcat/Km values of purified protease were 7.0 mg/mL, 3.8 x102S-1, 54.30 µmol/min and 54.28 s-1mg -1.mL respectively, using casein as substrate. The purified alkaline protease had stability with commercial detergents. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-04-01 |
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=S1516-89132015000200175 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000200175 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-8913201400071 |
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.58 n.2 2015 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_ |
1750318276854939648 |