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A Novel Thermostable GH3 ?-Glucosidase from Talaromyce leycettanus with Broad Substrate Specificity and Significant Soybean Isoflavone Glycosides-Hydrolyzing Capability.


ABSTRACT: A novel ?-glucosidase gene (Bgl3B) of glycoside hydrolase (GH) family 3 was cloned from the thermophilic fungus Talaromyce leycettanus JM12802 and successfully expressed in Pichia pastoris. The deduced Bgl3B contains 860 amino acid residues with a calculated molecular mass of 91.2 kDa. The purified recombinant Bgl3B exhibited maximum activities at pH 4.5 and 65°C and remained stable at temperatures up to 60°C and pH 3.0-9.0, respectively. The enzyme exhibited broad substrate specificities, showing ?-glucosidase, glucanase, cellobiase, xylanase, and isoflavone glycoside hydrolase activities, and its activities were stimulated by short-chain alcohols. The catalytic efficiencies of Bgl3B were 693 and 104/mM/s towards pNPG and cellobiose, respectively. Moreover, Bgl3B was highly effective in converting isoflavone glycosides to aglycones at 37°C within 10 min, with the hydrolysis rates of 95.1%, 76.0%, and 75.3% for daidzin, genistin, and glycitin, respectively. These superior properties make Bgl3B potential for applications in the food, animal feed, and biofuel industries.

SUBMITTER: Li X 

PROVIDER: S-EPMC6218797 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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A Novel Thermostable GH3 <i>β</i>-Glucosidase from <i>Talaromyce leycettanus</i> with Broad Substrate Specificity and Significant Soybean Isoflavone Glycosides-Hydrolyzing Capability.

Li Xinxin X   Xia Wei W   Bai Yingguo Y   Ma Rui R   Yang Hong H   Luo Huiying H   Shi Pengjun P  

BioMed research international 20181023


A novel <i>β</i>-glucosidase gene (<i>Bgl3B</i>) of glycoside hydrolase (GH) family 3 was cloned from the thermophilic fungus <i>Talaromyce leycettanus</i> JM12802 and successfully expressed in <i>Pichia pastoris</i>. The deduced Bgl3B contains 860 amino acid residues with a calculated molecular mass of 91.2 kDa. The purified recombinant Bgl3B exhibited maximum activities at pH 4.5 and 65°C and remained stable at temperatures up to 60°C and pH 3.0-9.0, respectively. The enzyme exhibited broad su  ...[more]

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