%0 Journal Article
%T PURIFICATION AND PROPERTIES OF INULINASES FROM ASPERGILLUS NIGER M89<br>黑曲霉M89菊粉酶的提纯与性质
%A Jia Yingmin
%A <br>贾英民
%A 赵学慧
%J 微生物学报
%D 1998
%I 
%X Four inulinase components were purified from Aspergillus niger M89 by (NH4)2SO4 fractionation, Sephadex G-200 gel filtration, DEAE-cellulose chromatography and polyacrylamide gel electrophoresis (PAGE). The molecular weight of EI EII EIII and EIV were indicated to be 102.6, 97.9, 62.5 and 36.5 kD respectively by SDS-PAGE. Measured by isoeleetric focusing, their isoelectric points were 4.15, 4.24, 4.48 and 4.15 respectively. Four forms of inulinase exibited maximal inulinase activity between 55-60 degrees C with optimal pH 4.0-5.0. There were some difference in their thermal stability. The little the molecule of the component was, the stronger its thermal stability was. All of four components were exo-acting inulinases.
%K Aspergillus niger
%K Inulinases<br>黑曲霉
%K 菊粉酶
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=B1CA673B9B2517D5868016BAE2C5C025&yid=8CAA3A429E3EA654&vid=16D8618C6164A3ED&iid=0B39A22176CE99FB&sid=2B5DE8A23DCEED39&eid=F122871CC7EC92DC&journal_id=0001-6209&journal_name=微生物学报&referenced_num=8&reference_num=2