Construction of the bifunctional enzyme cellulase-β-glucosidase from the hyperthermophilic bacterium Thermotoga maritima
Construction of the bifunctional enzyme cellulase-β-glucosidase from the hyperthermophilic bacterium Thermotoga maritima
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DOI：
10.1007/s10529-007-9334-5
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发表时间：
2007-06-01
影响因子：
2.7
通讯作者：
Yun, Han-Dae
中科院分区：
文献类型：
--
作者：
Hong, Su-Young;Lee, Jin-Suk;Yun, Han-Dae
利用基因融合技术从极端嗜热菌Thermotoga maritima MSB 8中合成了一种人工合成的双功能酶-纤维素酶-β-葡萄糖苷酶。当bglB基因融合到cel 5C的下游时，融合蛋白表现出纤维素酶（Cel 5C）和β-葡萄糖苷酶（BglB）活性，但当cel 5C融合到bglB的下游时，融合蛋白不表现出纤维素酶（Cel 5C）和β-葡萄糖苷酶（BglB）活性。该双功能酶的比活力比纤维素酶或β-葡萄糖苷酶低70%。纯化了融合酶，分子量估计为114 kDa。该融合酶在pH8.0和70 ℃条件下酶活最高，酶活力最高，酶活最高，酶活力最低，酶活力最高，
An artificial bifunctional enzyme, cellulase-beta-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. The fusion protein exhibited both cellulase (Cel5C) and beta-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not when cel5C was fused to downstream of bglB. The specific activity of the bifunctional enzyme was 70% lower than that of cellulase or beta-glucosidase. The fusion enzyme was purified, and the MW was estimated as 114 kDa. The fusion enzyme displayed optimum cellulase activity at pH 8.0 and 70 degrees C over 30 min, and optimal beta-glucosidase activity at pH 7.0 and 80 degrees C over 30 min.