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- W1974239564 abstract "ABSTRACTAn extracellular β-glucosidase (β-D-glucoside glucohydrolase, EC 3.2.1.21) produced by Aspergillus awamori K-1 was purified to electrophoretic homogeneity. The purified enzyme, which had a glycoprotein nature, was a monomer with a relative molecular mass of 116 kDa and pI= 5.8. The β-glucosidase was the most active against aryl-β-glucosides and cellobiose. In addition, the enzyme was able to catalyze the hydrolysis of β-1→2 and β-1 →6-linked diglucosides. The apparent Km and V values for p-nitrophenyl-β-D-gluco-pyranoside were calculated to be 0.8 mM and 5.29 μmol.min−1 respectively. Maximal β- glucosidase activity occurred at 60 °C and pH 5.0. This enzyme was competitively inhibited by β-D-glucose with K1 value of 13.15 mM." @default.
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- W1974239564 date "2002-01-01" @default.
- W1974239564 modified "2023-09-26" @default.
- W1974239564 title "Purification and Biochemical Characteristics of β-Glucosidase from Aspergillus Awamori K-1" @default.
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- W1974239564 doi "https://doi.org/10.1080/13102818.2002.10819160" @default.
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