Dayan Franck E, Kuhajek Jeanne M, Canel Camilo, Watson Susan B, Moraes Rita M
Natural Products Utilization Research Unit, Agricultural Research Service, United States Department of Agriculture, P.O. Box 8048, University, MS 38677, USA.
Biochim Biophys Acta. 2003 Mar 21;1646(1-2):157-63. doi: 10.1016/s1570-9639(03)00004-9.
A beta-glucosidase with high specificity for podophyllotoxin-4-O-beta-D-glucopyranoside was purified from the leaves of Podophyllum peltatum. The 65-kDa polypeptide had optimum activity at pH 5.0 and was essentially inactive at pH 6.5 or above. Maximum catalytic activity of this glucosidase was obtained at 45 degrees C, but the enzyme was not heat stable. This beta-glucosidase displayed higher substrate specificity for podophyllotoxin-4-O-beta-D-glucopyranoside than for the other lignans tested, and for the (1-->3) linkage of laminaribiose than for other glucosidic linkages.
从盾叶鬼臼的叶子中纯化出一种对鬼臼毒素-4-O-β-D-吡喃葡萄糖苷具有高特异性的β-葡萄糖苷酶。该65 kDa的多肽在pH 5.0时具有最佳活性,在pH 6.5及以上基本无活性。这种葡萄糖苷酶的最大催化活性在45℃时获得,但该酶不耐热。与所测试的其他木脂素相比,这种β-葡萄糖苷酶对鬼臼毒素-4-O-β-D-吡喃葡萄糖苷表现出更高的底物特异性,并且对层二糖的(1→3)键比对其他糖苷键表现出更高的底物特异性。