Purification and characterization of a novel chitinase from Bacillus brevis

文献类型： 外文期刊

第一作者： Li, S

作者： Li, S;Zhao, ZA;Li, M;Gu, ZR;Bai, C;Huang, WD

作者机构：

关键词： endochitinase;Bacillus brevis;purification;dimer;disulfide bonds

期刊名称：ACTA BIOCHIMICA ET BIOPHYSICA SINICA （ 影响因子：3.848； 五年影响因子：3.67 ）

ISSN： 0582-9879

年卷期： 2002 年 34 卷 6 期

页码：

收录情况： SCI

摘要： An extracellular chitinase secreted by Bacillus brevis was purified to homogeneity by a combination of ammonium sulfate precipitation, Phenyl-Sepharose hydrophobic-interaction chromatography and DEAE anion-exchange chromatography. On SDS-polyacrylamide gel electrophoresis analysis, the purified enzyme showed a mass of 85 kD even in the presence of beta-mercaptoethanol, but shifted to 48 kD when heated in boiling water or treated with 8 mol/L urea at 50 degreesC for 10 min. The depolymerization of subunits was accompanied with the loss of chitinase activity, and removing denaturing factors by dialysis could restore the dimer structure and enzymatic activity. The enzyme had an isoelectric point of 5.5 and an optimal temperature of 60 degreesC, and was most active at pH 8.0. The enzymatic activity was stable at pH 6-10, and inhibited by Ag+. Ten N-terminal amino acids were determined to be AVSNSKIIGY, demonstrating that the purified enzyme was a novel one. The hydrolysis pattern of the purified enzyme indicated that the chitinase was an endochitinase. The extraordinary thermo-stability and high resistance to proteolysis provide the enzyme with a good prospect to be used as a new tool for biocontrol.

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