Open AccessPurificication and properties of Aspergillus niger β‐glucosidase
Author(s) -
WATANABE Takashi,
SATO Toshie,
YOSHIOKA Shin,
KOSHIJIMA Tetsuo,
KUWAHARA Masaaki
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb17332.x
Subject(s) - methacrylamide , aspergillus niger , chemistry , gel permeation chromatography , cellobiose , isoelectric point , chromatography , hydrolysis , beta glucosidase , affinity chromatography , enzyme , cellulase , organic chemistry , biochemistry , acrylamide , polymer , monomer
β‐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 specificically β‐glucosidic bonds and catalyzed transglucosylation of the β‐glucosyl group of cellobiose to yield 4‐ O ‐β‐gentiobiosylglucose in the presence of organic solvents or under neutral conditions.