Abstract
The alkaline proteinases of Gliocladium roseum (Link) Bainier were purified in crystal-line 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 homo-geneous on zone electrophoresis with polyacrylamide gel (Cyanogum 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++, Co++ 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.
