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Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4856
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dc.contributor.authorDastager, SG
dc.contributor.authorDayanand, A
dc.contributor.authorLi, WJ
dc.contributor.authorKim, CJ
dc.contributor.authorLee, JC
dc.contributor.authorPark, DJ
dc.contributor.authorTian, XP
dc.contributor.authorRaziuddin, QS
dc.date.accessioned2020-06-12T15:05:27Z-
dc.date.available2020-06-12T15:05:27Z-
dc.date.issued2008
dc.identifier.citationCURRENT MICROBIOLOGY , Vol. 57 , 6 , p. 638 - 642en_US
dc.identifier.uri10.1007/s00284-008-9257-y
dc.identifier.urihttp://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4856-
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 45C. The enzyme preparation exhibited activity over a broad range of pH (4-12) and temperature (27-55C). Optimum activity was observed at a pH of 9.0 and a temperature of 45C. 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).en_US
dc.publisherSPRINGER
dc.titleProteolytic Activity from an Alkali-Thermotolerant Streptomyces gulbargensis sp nov.en_US
dc.typeArticle
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