School of Food Science and Technology, Jiangnan University, Wuxi, China.
Biotechnol Lett. 2011 Nov;33(11):2193-9. doi: 10.1007/s10529-011-0676-7. Epub 2011 Jul 7.
A new fusion gene (Bgl-licMB), encoding β-1,3-1,4-glucanase both from Bacillus amyloliquefaciens (Bgl) and Clostridium thermocellum (licMB), was constructed via end-to-end fusion and expressed in Escherichia coli to improve hydrolytic activity and thermostability of β-1,3-1,4-glucanase. The results of enzymatic properties showed that the catalytic efficiency (K(cat)/K(m)) of the fusion enzyme for oat β-glucan was 2.7 and 20-fold higher than that of the parental Bgl and licMB, respectively, and that the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bgl and licMB were both less than 30%. These properties make this particular β-1,3-1,4-glucanase a good candidate for application in brewing and animal-feed industries.
构建了一个新的融合基因（Bgl-licMB），该基因通过末端融合的方式编码来自解淀粉芽孢杆菌（Bgl）和热纤梭菌（licMB）的β-1,3-1,4-葡聚糖酶，以提高β-1,3-1,4-葡聚糖酶的水解活性和热稳定性。酶学性质研究结果表明，融合酶对燕麦β-葡聚糖的催化效率（Kcat/Km）分别比亲本 Bgl 和 licMB 高 2.7 倍和 20 倍，融合酶在 80°C 孵育 30 min 后仍能保留超过 50%的活性，而 Bgl 和 licMB 的剩余活性均小于 30%。这些特性使这种特定的β-1,3-1,4-葡聚糖酶成为在酿造和动物饲料工业中应用的良好候选酶。
