%0 Journal Article
%T Purification and Properties of Endoinulinase from Chaetomium sp.<br>毛壳霉内切菊粉酶的纯化与性质
%A Guo-Qing Zhang
%A Fu-Mian Cui
%A Xiu-Qing Yang
%A Shi-Jun Qian
%A <br>张国青
%A 崔福绵
%A 杨秀清
%A 钱世钧
%J 微生物学报
%D 2004
%I 
%X An endoinulinase produced by Chaetomium sp. C34 was purified to electrophoretic homogeneity, with recovery of 7.7% activity and purification factor of 30.8 fold by five steps including ammonium sulfate precipitation, DEAE-cellulose, Q-sepharose Fast Flow, Sephacryl S-200 and Pre-Packed Hydrophobic Column. Its subunit molecular weight was estimated to be about 66kD by SDS-PAGE. The optimum temperature and pH of the enzyme activity were 50 approximately 55 degrees C and 6.0 respectively. The K(m) and V(max) values for inulin were 0.199 mmol/L and 115 micromol/(mg x min) respectively. Cu2+ completely inhibited inulinase activity. An appreciable loss of activity was observed in presence of NBS, Mn2+, Zn2+, Fe2+ and EDTA. A ratio of inulinase activity to invertase activity (I/S) of 20 was found in purified inulinase. The endoinulinase hydrolyzed inulin and liberated inulooligosaccharides. But it lacked activity toward melezitose or raffinose.
%K Chaetomium sp
%K Endoinulinase
%K Purification
%K Properties<br>毛壳霉
%K 内切菊粉酶
%K 纯化
%K 性质
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=682903651F8B0CD8&yid=D0E58B75BFD8E51C&vid=1AE5323881A5ECDC&iid=B31275AF3241DB2D&sid=A1BB529A18D3A83E&eid=E339BF74025BB291&journal_id=0001-6209&journal_name=微生物学报&referenced_num=4&reference_num=13