Objective To investigate the purification method of endoglucanase (EGase) from Pantoea stewartii subsp. stewartii. Methods With the material of Pantoea stewartii subsp. stewartii. strain, EGase fermented liquid was prepared, and then eluted using SephadexTM G-75 and on DEAE-Sepharose Fast Flow anion exchange. SDS-PAGE was used to determine the EGase activity after purification. Results Endoglucanase was purified from Pantoea stewartii subsp. stewartii. It was monomer protein and its molecular size was 72.3 kDa. The optimum reaction temperature of endoglucanase was 60 ℃ and the optimum pH was 5.0. Conclusion Endoglucanase was purified firstly from Pantoea stewartii subsp. stewartii and its properties were described. This study will provide an important base for cloning and expression of endoglucanase gene research.
标题:玉米细菌性枯萎病菌EGase内切葡聚糖酶蛋白纯化研究初探
英文标题:Initial studies of Endoglucanase purification from Pantoea stewartii subsp. stewartii