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- W2419364079 abstract "Abstract The fungus Humicola insolens is one of the most powerful decomposers of crystalline cellulose. However, studies on the β-glucosidases from this fungus remain insufficient, especially on glycosyl hydrolase family 3 enzymes. In the present study, we analyzed the functional diversity of three distant family 3 β-glucosidases from Humicola insolens strain Y1, which belonged to different evolutionary clades, by heterogeneous expression in Pichia pastoris strain GS115. The recombinant enzymes shared similar enzymatic properties including thermophilic and neutral optima (50–60 °C and pH 5.5–6.0) and high glucose tolerance, but differed in substrate specificities and kinetics. Hi Bgl3B was solely active towards aryl β-glucosides while Hi Bgl3A and Hi Bgl3C showed broad substrate specificities including both disaccharides and aryl β-glucosides. Of the three enzymes, Hi Bgl3C exhibited the highest specific activity (158.8 U/mg on p NPG and 56.4 U/mg on cellobiose) and catalytic efficiency and had the capacity to promote cellulose degradation. Substitutions of three key residues Ile48, Ile278 and Thr484 of Hi Bgl3B to the corresponding residues of Hi Bgl3A conferred the enzyme activity towards sophorose and vice versa. This study reveals the functional diversity of GH3 β-glucosidases as well as the key residues in recognizing +1 subsite of different substrates." @default.
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- W2419364079 date "2016-06-08" @default.
- W2419364079 modified "2023-10-16" @default.
- W2419364079 title "Functional diversity of family 3 β-glucosidases from thermophilic cellulolytic fungus Humicola insolens Y1" @default.
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- W2419364079 doi "https://doi.org/10.1038/srep27062" @default.
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