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学科主题: Microbiology
题名: Proteolytic Activity from an Alkali-Thermotolerant Streptomyces gulbargensis sp nov.
作者: Dastager, SG ; Dayanand, A ; Li, WJ ; Kim, CJ ; Lee, JC ; Park, DJ ; Tian, XP ; Raziuddin, QS
刊名: CURRENT MICROBIOLOGY
发表日期: 2008
卷: 57, 期:6, 页:638-642
收录类别: sci
部门归属: [Dastager, S. G.; Dayanand, Agasar; Raziuddin, Q. S.] Gulbarga Univ, Dept Studies & Res Microbiol, Gulbarga 585106, Karnataka, India; [Dastager, S. G.; Li, Wen-Jun; Tian, Xin-Peng] Yunnan Univ, Yunnan Inst Microbiol, Lab Conservat & Utilizat Bio Resources, Kunming 650091, Renfrew, Peoples R China; [Tian, Xin-Peng] Chinese Acad Sci, S China Sea Inst Oceanol, Guangdong Key Lab Marine Mat Medica, Guangzhou 510301, Guangdong, Peoples R China; [Dastager, S. G.; Kim, Chang-Jin; Lee, Jae-Chan; Park, Dong-Jin] Korea Res Inst Biosci & Biotechnol, Taejon 305333, South Korea
项目归属: 广东省海洋药物重点实验室
摘要: Multiple 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).
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WOS记录号: WOS:000261177900022
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内容类型: 期刊论文
URI标识: http://ir.scsio.ac.cn/handle/344004/5248
Appears in Collections:广东省海洋药物重点实验室_期刊论文

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Recommended Citation:
Dastager, SG; Dayanand, A; Li, WJ; Kim, CJ; Lee, JC; Park, DJ; Tian, XP; Raziuddin, QS.Proteolytic Activity from an Alkali-Thermotolerant Streptomyces gulbargensis sp nov.,CURRENT MICROBIOLOGY,2008,57(6):638-642
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