title: Construction and characterization of a fusion β-1,3-1,4-glucanase to improve hydrolytic activity and thermostability.
abstract: 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.
authors: School of Food Science and Technology, Jiangnan University, Wuxi, China.
authors: Juntao
authors: J
authors: Sun
authors: Hongxin
authors: H
authors: Wang
authors: Wenping
authors: W
authors: Lv
authors: Chaoyang
authors: C
authors: Ma
authors: Zaixiang
authors: Z
authors: Lou
authors: Yixing
authors: Y
authors: Dai
mesh_terms: D018554:Avena / Q000737:chemistry; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D048013:Acetivibrio thermocellus / Q000201:enzymology* / Q000235:genetics; D044644:Endo-1,3(4)-beta-Glucanase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006358:Hot Temperature; D006868:Hydrolysis; D007700:Kinetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013997:Time Factors; D047071:beta-Glucans / Q000378:metabolism
chemical_list: D011993:Recombinant Fusion Proteins; D047071:beta-Glucans; D044644:Endo-1,3(4)-beta-Glucanase