Construction and characterization of a fusion β-1,3-1,4-glucanase to improve hydrolytic activity and thermostability.

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/K) 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. [ABSTRACT FROM AUTHOR]