Studies on Proteinases from Gliocladium roseum |
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| Authors: | Tadaaki Kishida Sadahiko Yoshimura |
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| Affiliation: | 1. The Laboratory of Nutritional Biochemistry, Himeji Women’s College, Shinzaike, Himeji-City, Hyogo Prefecture;2. The Laboratory of Food Chemistry, Hyogo University of Auriculture, Sasayama, Hyogo Prefecture |
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| Abstract: | The alkaline proteinases of Gliocladium roseum (Link) Bainier were purified in crystalline forms by procedures of alcoholic precipitation, fuller’s earth- and acrinol-treatment, and isolated in two types. (Proteinases I and II). Both of these proteinases were homogeneous on zone electrophoresis with polyacrylamide gel (Gyanogum 41), and had the optimal pH values of 11 (Proteinase I) and 10 (Proteinase II), and the optimal temperature of 45°C.The enzymatic reaction of proteinase I was remarkably promoted by Fe++ and Co++, and that of proteinase II was promoted by Fe++, Go++ and Ca++, and both proteinases were protected from heat-inactivation by Ca++ Proteinase II was activated remarkably by Cl? under the existence of Fe++, but proteinase I was unaffected by the anion.The order of strength of proteolytic power of these proteinases and chymotrypsin on casein was as follows; proteinase I> proteinase II> chymotrypsin. |
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