%0 Journal Article
%T PURIFICATION AND PROPERTIES OF ENDOGLUCANASES FROM ASPERGILIUS ACULEATUS SM-L22
脱墨用棘孢曲霉SM-L22纤维素酶系中内切酶的纯化及性质
%A G Chen
%A J Du
%A L Zhuang
%A P Gao
%A
陈冠军
%A 杜娟
%A 庄蕾
%A 高培基
%J 微生物学报
%D 2001
%I
%X The five endoglucanases(CMCase) components from Aspergillus aculeatus SM-L22 were separated and purified by exclusion chromatography and ion-exchange chromatography. Five components(EG II-1, EG II-2, EG III-1, EG III-2 and EG IV) had molecular weights of 38.7, 34.4, 31.4, 36.9 and 23.7 kD by SDS-PAGE, respectively, and IEF showed their pI were pH < 3.5, < 3.5, 4.9, 4.4 and 5.0, respectively. All of them have maximum reactive activities at pH 3.5-4.0; and the optimum temperatures were 55 degrees C, 60 degrees C, 60 degrees C-70 degrees C, 60 degrees C-70 degrees C and 60 degrees C, respectively. EG II-1 and EG II-2 can only act such morphological substrates as CMC or phosphated cellulose, but EG III-1, EG III-2 and EG IV can active xylan also. The activities of all components were stimulated by Fe2+ except EG IV, EG III-2 was activited mostly by Fe2+. The kinetics' showed that there were no relativies between the affectivity of cellulases and its Km.
%K Aspergillus aculeatus
%K Endoglucanases
%K Purification
%K Enzymatic properties
棘孢曲霉
%K 内切葡萄糖苷酶
%K 纤维素酶
%K 分离纯化
%K 酶学性质
%K 废纸脱墨
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=460BBC52255A7D6D&yid=14E7EF987E4155E6&vid=2001E0D53B7B80EC&iid=E158A972A605785F&sid=8F2250DA83AF77B8&eid=FE6B7E9BDCCDBAA6&journal_id=0001-6209&journal_name=微生物学报&referenced_num=10&reference_num=13