%0 Journal Article
%T PURIFICATION AND PROPERTIES OF CHITINASE FROM ENTEROBACTER AEROGENES<br>产气肠杆菌几丁质酶的分离纯化及性质研究
%A Tang Yaxiong
%A Zhao Jian
%A Ding Shihua
%A Liu Shigui
%A Yang Zhirong
%A <br>唐亚雄
%A 赵建
%A 丁诗华
%A 刘世贵
%A 杨志荣
%J 微生物学报
%D 2001
%I 
%X A bacterium producing chitinase was isolated from the dead body of Gymephorap ruoergensis. A chitinase was isolated from the culture of E. aerogenes and purified by means of ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-100 column gel filtration. The purified chitinase showed homogeneity on the native polyacrylamide gel electrophoresis. Its molecular weight was estimated to be about 42.5 kD by SDS-PAGE. The optimum pH and temperature for hydrolysis of chitin were 6.0 and 55 degrees C respectively. Michaelis constant was 2.88 mg/mL. Different metal ions showed different effects on the chitinase activity, The chitinase activity was enhanced by Zn2+, Ba2+, Ca2+, Mn2+ and was strongly inhibited by Hg2+, Co2+, Mg2+.
%K Enterobacter aerogenes
%K Chitinase
%K Isolation and purification
%K Properities<br>产气肠杆菌，几丁质酶，纯化，酶学性质
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=3CAA472802668A84&yid=14E7EF987E4155E6&vid=2001E0D53B7B80EC&iid=CA4FD0336C81A37A&sid=0D0D661F0B316AD5&eid=7AA74D31F1FF2DCE&journal_id=0001-6209&journal_name=微生物学报&referenced_num=12&reference_num=17