Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/70026
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.
Chi, M.C.
Lo, H.F.
Hsu, W.H.
Lin, L.L.
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.
URI: http://hdl.handle.net/11455/70026
ISSN: 1367-5435
DOI: 10.1007/s10295-004-0146-5
Appears in Collections:期刊論文

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