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KMID : 0357319960310040451
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Journal of the Korean Society for Microbiology
1996 Volume.31 No. 4 p.451 ~ p.464
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Purification and Characterization of a Produced by Vibrio anguillarum PT-213 Strain
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주진우
박우영/주성아/옥주안/허문수
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Abstract
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The extracellular protease was purified from the culture supernatant of Vibrio anguillarum PT-213 by precipitation with ammonium sulfate, ion exchange chromatography and hydrophobic interaction chromatography. About 1459-fold purification was
achieved,
with a yield of about 85%. The yield of enzyme was maximal and stable during the stationary growth phase in brain heart infusion broth containing 1.5% NaC1. The enzyme was shown to be elastolytic when assayed with elastin-congo red. In addition,
the
enzyme hydrolysed milk casein. The purified protease was heterogeneous on SDS-polyacrylamide gel electrophoresis and has a molecular weight of ca. 69 kDa. The optimum pH for caseinolytic activity was 7.5 and elastolytic activity was 7.0,
respectively,
but under the pH 4.0, the protease activity was lost completely. And optimum temperature of the caseinolytic activity was 55℃. Intraperitoneal injection of mouse with 200 g of the protease led to the severe diarrhea and the LD50 values of the
purified
protease to mouse were 7.1μg protein/g weight.
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