title: [Purification and properties of endoglucanases from Aspergillus aculeatus SM-L22].
abstract: 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.
authors.affiliation: State Key Laboratory of Microbial Technology, Shandong University, Jinan 250010, China.
authors.forename: G
authors.initials: G
authors.lastname: Chen
authors.forename: J
authors.initials: J
authors.lastname: Du
authors.forename: L
authors.initials: L
authors.lastname: Zhuang
authors.forename: P
authors.initials: P
authors.lastname: Gao
mesh_terms: D001230:Aspergillus / Q000737:chemistry / Q000201:enzymology*; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D005656:Fungal Proteins; D002480:Cellulase