The presence of a kinase of amylase in trypsin preparation

Abstract

Trypsin increased considerably the amylolytic power of barley. Its influence differed from that of papain mainly in markedly increasing the dextrinizing function, while papain increased it only slightly; papain, on the other hand, increased the saccharifying function slightly more than did trypsin. Trypsin increased the quantity of amylase in barley by 2 actions: (1) similar to that of papain, which caused either the decomposition of protein combined with amylase, or the formation of new quantities of amylase, thereby greatly increasing the saccharifying function; (2) the influence of a special kinase of amylase found in trypsin preparations, which increased the dextrinizing power strongly and the saccharifying power only slightly. Both in the active and inactivated trypsin, eluted substances were also present which partly protected the amylase against inactivation by shaking, just as peptone or inactivated papain did, though to a less degree.