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Alteromonas sp . 가 생산하는 alkaline protease 의 특성
여인옥(In Ok Yeo),최성현(Seong Hyun Choi),이재숙(Jae Sook Lee),김찬조(Chan Jo Kim) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.2
An alkaline protease-producing bacterium was isolated from Korean hot pepper paste and identified as Alteromanas sp. CN301. A alkaline protease was purified and characterized. The optimal pH and temperature for the enzyme activity were pH 12.0 and 35℃, respectively. Molecular weight of the enzyme was determined as 31,000 dalton by the SDS-PAGE. The enzyme was stable in the range of pH 6.0∼13.0 showing the residual activity above 80% of the enzyme activity. The residual activity of the enzyme was 64% when the enzyme was incubated at 50℃ for 1 hr. The activity of the end-me was not affected by most metal ions tested except Hg^(2+), and activated by Triton X-100, Tween 20 and Tween 80. The enzyme activity was severely inhibited by PMSF and EDTA, suggesting that the enzyme is serine protease having metal ion in its structure.