Enhancing activity of Endoglucanase Cel12B from Thermotoga maritime by site-directed mutagenesis
作者单位:Faculty of Life Science and ChemistryHuaiyin Institute of Technology Jiangsu Provincial Engineering Laboratory for Biomass Conversion and Process Integration Huaian High-Tech Research Institute of Nanjing University
会议名称:《The Ninth National Symposium on Enzyme Engineering》
会议日期:2013年
学科分类:0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学]
关 键 词:Thermotoga maritime Endoglucanase site-directed mutagenesis enzymatic properties
摘 要:The thermal stability and catalytic activity of endoglucanase(EngD)from thermophilic Thermotoga maritima were significantly improved by rational design on the basis of our previous Directed *** activity of two mutants,K207G and E225H,increased to varying degrees comparing with original *** relative activity was improved 30.38%and 29.62%*** enzymatic properties of the purified mutant proteins were *** results show that the optimum temperature of recombinated endoglucanase Cel12B-207 is 95℃,the optimum pH is *** left enzyme activity hold 70%compared to the unkept one after putting in 90℃for 2 *** optimum temperature of recombinated endoglucanase Cel12B-225 is 75℃,the optimum pH is *** left enzyme activity hold 95%compared to the unkept one after putting in 75℃for 8 hours.