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KMID : 0903519950380020106
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1995 Volume.38 No. 2 p.106 ~ p.110
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Characteristics of a Alkaline Protease from Alteromonas sp .
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Abstract
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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.
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