Şener Aysun
Faculty of Engineering, Department of Food Engineering, Altinsehir, 02040 Adiyaman, Turkey.
J Food Sci Technol. 2015 Dec;52(12):8322-8. doi: 10.1007/s13197-015-1915-z. Epub 2015 Jun 14.
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.
本研究旨在确定从土耳其茶叶中分离出的β-葡萄糖苷酶(β-D-葡糖苷葡糖水解酶,EC 3.2.1.21)的生化特性。回收并鉴定了两个含有β-葡萄糖苷酶活性的蛋白峰,分别命名为同工酶A和同工酶B。它们的最适pH、耐热性、对对硝基苯基-β-D-吡喃葡萄糖苷的亲和力有显著差异。它们在pH 5.0时均表现出最大活性。所测试抑制剂的作用呈剂量依赖性变化。