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|標題:||Fusion of Bacillus stearothermophilus leucine aminopeptidase II with the raw-starch-binding domain of Bacillus sp strain TS-23 alpha-amylase generates a chimeric enzyme with enhanced thermostability and catalytic activity||作者:||Hua, Y.W.
|關鍵字:||leucine aminopeptidase;Bacillus stearothermophilus;amylase;raw;starch-binding domain;Bacillus sp strain TS-23;thermostability;escherichia-coli;cyclodextrin glucanotransferase;expression;construction;glucoamylase;gene;purification;adsorption;proteins;cloning||Project:||Journal of Industrial Microbiology & Biotechnology||期刊/報告no：:||Journal of Industrial Microbiology & Biotechnology, Volume 31, Issue 6, Page(s) 273-277.||摘要:||
Bacillus stearothermophilus leucine aminopeptidase 11 (LAPII) was fused at its C-terminal end with the raw-starch-binding domain of Bacillus sp. strain TS-23 alpha-amylase. The chimeric enzyme (LAPsbd), with an apparent molecular mass of approximately 61 kDa, was overexpressed in IPTG-induced Escherichia coli cells and purified to homogeneity by nickel-chelate chromatography. The purified enzyme retained LAP activity and adsorbed raw starch. LAPsbd was stable at 70degreesC for 10 min, while the activity of wild-type enzyme was completely abolished under the same environmental condition. Compared with the wild-type enzyme, the twofold increase in the catalytic efficiency for LAPsbd was due to a 218% increase in the k(cat) value.
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