European Journal of Biochemistry 1992-10-15

Purification and properties of Aspergillus niger beta-glucosidase.

T Watanabe, T Sato, S Yoshioka, T Koshijima, M Kuwahara

Index: Eur. J. Biochem. 209 , 651, (1992)

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Abstract

Beta-glucosidase was purified from a crude cellulase preparation from Aspergillus niger by affinity chromatography on a methacrylamide-N-methylene-bis-methacrylamide copolymer bearing cellobiamine. The purified enzyme was a dimer with an isoelectric point of 4.0. The molecular mass of the enzyme was estimated to be 240 kDa by gel-permeation chromatography. The enzyme hydrolyzed specifically beta-glucosidic bonds and catalyzed transglucosylation of the beta-glucosyl group of cellobiose to yield 4-O-beta-gentiobiosylglucose in the presence of organic solvents or under neutral conditions.