Abstract:
This research was carried out to determine biochemical properties of beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) isolated from Turkish tea leaves. Two protein peaks containing beta-glucosidase activity were recovered and characterized, which were denoted as isoenzyme A and isoenzyme B. Their pH optimum, thermal resistances, affinity towards p-nitrophenyl-beta-D-glucopyranoside differed markedly. They both displayed maximal activity at pH 5.0. The effects of the inhibitors tested varied in a dose dependent manner.
