Proteolytic activity from an alkali-thermotolerant Streptomyces gulbargensis sp. nov.

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dc.contributor.authorS G Dastager-
dc.contributor.authorA Dayanand-
dc.contributor.authorW J Li-
dc.contributor.authorChang-Jin Kim-
dc.contributor.authorJae Chan Lee-
dc.contributor.authorDong Jin Park-
dc.contributor.authorX P Tian-
dc.contributor.authorQ S Raziuddin-
dc.date.accessioned2017-04-19T09:12:14Z-
dc.date.available2017-04-19T09:12:14Z-
dc.date.issued2008-
dc.identifier.issn0343-8651-
dc.identifier.uri10.1007/s00284-008-9257-yko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8714-
dc.description.abstractMultiple proteases were produced and partially purified from an alkali-thermotolerant novel species of Streptomyces (i.e., Streptomyces gulbargensis DAS 131) after 48 h of growth at 45°C. The enzyme preparation exhibited activity over a broad range of pH (4-12) and temperature (27-55°C). Optimum activity was observed at a pH of 9.0 and a temperature of 45°C. Starch and protease peptone was found to be a good source of carbon and nitrogen to enhance the enzyme activity. Two active zones in the range of 19 to 35 kDa were detected on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE).-
dc.publisherSpringer-
dc.titleProteolytic activity from an alkali-thermotolerant Streptomyces gulbargensis sp. nov.-
dc.title.alternativeProteolytic activity from an alkali-thermotolerant Streptomyces gulbargensis sp. nov.-
dc.typeArticle-
dc.citation.titleCurrent Microbiology-
dc.citation.number6-
dc.citation.endPage642-
dc.citation.startPage638-
dc.citation.volume57-
dc.contributor.affiliatedAuthorChang-Jin Kim-
dc.contributor.affiliatedAuthorJae Chan Lee-
dc.contributor.affiliatedAuthorDong Jin Park-
dc.contributor.alternativeNameDastager-
dc.contributor.alternativeNameDayanand-
dc.contributor.alternativeNameLi-
dc.contributor.alternativeName김창진-
dc.contributor.alternativeName이재찬-
dc.contributor.alternativeName박동진-
dc.contributor.alternativeNameTian-
dc.contributor.alternativeNameRaziuddin-
dc.identifier.bibliographicCitationCurrent Microbiology, vol. 57, no. 6, pp. 638-642-
dc.identifier.doi10.1007/s00284-008-9257-y-
dc.description.journalClassY-
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Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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