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- W1972377617 abstract "On the basis of the genomic sequence of Bacillus subtilis 168, two β-glucosidase genes ( bglH and yckE) from B. subtilis natto, which has been reported to have high isoflavone glucoside-hydrolyzing activity, were cloned and overexpressed in E. coli M15. The temperature for the optimal p-nitrophenyl-β- d-glucoside hydrolyzing activity of both enzymes was between 37 and 45 °C, but BglH had a higher thermal stability than YckE. Both showed high activity at pH 6.0, but YckE was stable over a wider pH range than BglH. Recombinant BglH was inhibited 73%, 63%, and 43% by 1.0 mM Cd 2+, Fe 2+, or Cu 2+, respectively, while other divalent metal ions resulted in 0–23% inhibition, whereas YckE was inhibited by less than 20% by any of the divalent metal ions we tested. Among the substrate we used, BglH showed the highest affinity for genistin and YckE showed the highest affinity for p-nitrophenyl-β- d-fructopyranoside. Both BglH and YckE hydrolyzed genistin and daidzin into their isoflavone aglycones, genistein and daidzein, but BglH was more efficient than YckE in isoflavone glucoside hydrolysis (20-fold higher k cat). Our results suggest that recombinant BglH may be applicable in the process of isoflavones deglycosylation." @default.
- W1972377617 created "2016-06-24" @default.
- W1972377617 creator A5008294938 @default.
- W1972377617 creator A5018498039 @default.
- W1972377617 date "2007-12-11" @default.
- W1972377617 modified "2023-10-16" @default.
- W1972377617 title "Cloning, Expression, and Characterization of Two β-Glucosidases from Isoflavone Glycoside-Hydrolyzing <i>Bacillus subtilis</i> natto" @default.
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- W1972377617 doi "https://doi.org/10.1021/jf072287q" @default.
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