Cel8H,a novel endoglucanase from the halophilic bacterium Halomonas sp.S66-4:molecular cloning,heterogonous expression and biochemical characterization

作     者：Xiaoluo Huang~1,Zongze Shao~3,Yuzhi Hong~2,Ling Lin~1,Chanjuan Li~1,Fei Huang~1,Hui Wang~1,Ziduo Liu~* 1State Key Laboratory of Agricultural Microbiology,College of Life Science and Technology, Huazhong Agricultural University,Wuhan 430070,People’s Republic of China 2College of Plant Science and Technology,Huazhong Agricultural University,Wuhan 430070,People’s Republic of China 3Key Laboratory of Marine Biogenetic Resources,The Third Institute of Oceanography,State of Oceanic Administration,Xiamen 361005,People’s Republic of China 

会议名称：《湖北省遗传学会第八次代表大会暨学术讨论会》

会议日期：2009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] 

摘      要：A recombinant Escherichia coli clone expressing an endoglucanase was identified from a genomic library of the halophilic bacterium Halomonas sp.S66-4,and the enzyme was designated *** cel8H gene consisted of 1053bp and encoded 350 amino acids sharing the highest identity of 48%to other known *** protein was expressed in *** BL21(DE3) and purified to *** purified recombinant enzyme had an optimal activity of 4.9 U/mg at pH 5 and 45℃toward the substrate *** exhibited extraordinary properties which differed from endoglucanases reported previously at the point of high salt tolerance above 5 M,simultaneously with high pH stability at pH 4-12 and high temperature stability at 40-60℃.Various substrate tests indicated that the enzyme hydrolyzes β-1,4-glucosidic bonds specifically.