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Purification and characterization of an alpha-L-rhamnosidase from Aspergillus nidulans by P. Manzanares; M. Orejas; E. Ibanez; S. Valles; D. Ramon is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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An enzyme exhibiting alpha-L-rhamnosidase activity was purified by fractionating a culture filtrate of Aspergillus nidulans grown on L-rhamnose as the sole carbon source. The alpha-L-rhamnosidase was shown to be N-glycosylated and had a molecular mass of 102 kDa, of which approximately 7% was contributed by carbohydrate. The enzyme, optimally active at pH 4.5-6 and 60 degrees C, had an isoelectric point of 5. With rho-nitrophenyl-alpha-L-rhamnopyranoside as the substrate it showed Km and Vmax values of 0.27 mmol l-1 and 64.6 U mg-1, respectively. The enzyme was competitively inhibited by L-rhamnose (Ki 0.3 mmol l-1). Ca2+ (2 mmol l-1) stimulated the activity of the enzyme by 14%, whereas Mg2+ (2 mmol l-1) inhibited it by 63%. Substrate specificity studies showed the alpha-L-rhamnosidase to be active both on alpha-1,2 and alpha-1,6 linkages to beta-D-glucosides.

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Author

P. Manzanares; M. Orejas; E. Ibanez; S. Valles; D. Ramon

Publisher

Oxford University Press (OUP)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)