Abstract
This research was carried out to determine biochemical properties of β-glucosidase (β-D-glucoside glucohydrolase, EC 3.2.1.21) isolated from Turkish tea leaves. Two protein peaks containing β-glucosidase activity were recovered and characterized, which were denoted as isoenzyme A and isoenzyme B. Their pH optimum, thermal resistances, affinity towards p-nitrophenyl-β-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.