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- W1977807009 abstract "An enzyme with α-l-rhamnosidase activity was purified by anion exchange chromatography from an Aspergillus niger commercial preparation. The α-l-rhamnosidase was shown to be N-glycosylated, and had a molecular mass of 85 kD on sodium dodecylsulfate-polyacrylamide gel electrophoresis of which approximately 12% was contributed by carbohydrate. The enzyme was optimally active at pH 4.5 and 65°C. When tested towards p-nitrophenyl-α-l-rhamnopyranoside it showed Km and Vmax values of 2.9 mM and 20.6 U mg−1, respectively whereas it was inhibited competitively by l-rhamnose (Ki 3.5 mM). Substrate specificity studies showed α-l-rhamnosidase to be active both on α-1,2 and α-1,6 linkages to β-d-glucose. Moreover, the enzyme was able to release l-rhamnose from geranyl-β-d-rutinoside and 2-phenylethyl-β-d-rutinoside." @default.
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- W1977807009 date "2006-01-17" @default.
- W1977807009 modified "2023-10-15" @default.
- W1977807009 title "Purification and characterization of an α-l-rhamnosidase from Aspergillus niger" @default.
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- W1977807009 doi "https://doi.org/10.1111/j.1574-6968.1997.tb12785.x" @default.
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