灰葡萄孢菌E-200菌株的多聚半乳糖醛酸酶

Polygalacturonase of Botrytis cinerea E-200 Pers.

作者信息

Urbanek H, Zalewska-Sobczak J

出版信息

Biochim Biophys Acta. 1975 Feb 19;377(2):402-9. doi: 10.1016/0005-2744(75)90320-4.

Abstract

A polygalacturonase (poly(1,4-alpha-D-galacturonide)glycanohydrolase, EC 3.2.1.15) was purified from the culture fluid of Botrytis cinerea. The polygalacturonase preparation, homogeneous on the basis of disc-gel electrophoresis also showed pectinesterase activity. Some properties of the purified polygalacturonase were studied. It had a molecular weight about 69 000. It was inactivated by p-chloromercuribenzoate, tetranitromethane and urea. A 50% loss in viscosity of sodium polypectate solution occurred when 4.6% of the glycosidic bonds were hydrolyzed. The only end product of sodium polypectate and oligogalacturonides hydrolysis was monogalacturonic acid.?

摘要

从灰葡萄孢的培养液中纯化出一种多聚半乳糖醛酸酶（聚（1,4-α-D-半乳糖醛酸）聚糖水解酶，EC 3.2.1.15）。基于圆盘凝胶电泳显示该多聚半乳糖醛酸酶制剂是均一的，同时也表现出果胶酯酶活性。对纯化的多聚半乳糖醛酸酶的一些性质进行了研究。它的分子量约为69000。它会被对氯汞苯甲酸、四硝基甲烷和尿素灭活。当4.6%的糖苷键被水解时，聚果胶酸钠溶液的粘度损失50%。聚果胶酸钠和低聚半乳糖醛酸水解的唯一终产物是单半乳糖醛酸。