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KMID : 0903519980410050349
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1998 Volume.41 No. 5 p.349 ~ p.354
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Purification and Characterization of Protease Produced by Bacillus subtilis YG-95
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Abstract
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The protease produced by Bacillus subtilis YG-95 was purified by precipitating with ammonium sulfate, DEAF-sepharose 6B and Sephadex G-100 column chromatogtaphies and its purified enzymological characteritics were investigated. The molecular weight of purified protease was estimated about 43kilodalton by SDS PAGE The optimum pH and temperature for the purified protease activity were pH 10.0 and 55℃, respectively. The enzyme was stable in broad range of pH 5.0 to 12.0. and at the below 45℃. The purified enzyme activty was inhibited by Fe^(3+) and Al^(3+). The activity was significantly inhibited more than 80% by O-Phenanthroline, PMSF and SDS. The K_m value of the purified enzyme against Soy Protein Isolate as a substrate was 1.28 ㎎/㎖.
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