title: [Purification and properties of alkaline cellulase from alkalophilic Bacillus N6-27].
abstract: The alkaline cellulase produced by alkalophilic Bacillus sp. N6-27 was purified to electrophoresis homogeneity by (NH4)2SO4 fractionation, Sepharose CL-4B hydrophobic interaction chromatography, Bio-gel P-150 chromatography. The molecular weight and pI determined by SDS-PAGE and by PAGE-IEF were 94,000 and 4.2, respectively. The optimum temperature and pH for the enzymatic catalysis were 55 degrees C and 8.5, respectively. The enzyme activity was stable under 50 degrees C and in the pH range of 6-11. The substrate was carboxymethylcellulose (CMC). The enzyme activity was strongly inhibited by Fe2+, Cu2+ and Hg2+.
authors.affiliation: Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080.
authors.forename: X
authors.initials: X
authors.lastname: Tian
authors.forename: X
authors.initials: X
authors.lastname: Wang
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D002480:Cellulase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight
chemical_list: D002480:Cellulase