Degradation of Taka-Amylase A by Taka-Proteinase

Abstract

A study was made of the action of taka-proteinase on crystalline taka-amylase A. The proteinase was purified by Amberlite IRC-50 from “Taka-diastase”. Taka-amylase A was found to be degraded about 50 per cent by taka-proteinase in Mcllvaine's buffer solution at pH 7.0, 37°C for 24 hours, without any denaturation. The modified takaamylase A had a higher specific activity than the original taka-amylase A, and was homogeneous in electrophoretic and sedimentation analyses. Several physicochemical constants of it were less than those of the original taka-amylase A. By the action of the proteinase, various amino acids and peptides were found to be released from taka-amylase A.