H. Hashimoto et al., TRANSGALACTOSYLATION CATALYZED BY ALPHA-GALACTOSIDASE FROM CANDIDA-GUILLIERMONDII H-404, Bioscience, biotechnology, and biochemistry, 59(4), 1995, pp. 619-623
The thermostable alpha-galactosidase from Candida guilliermondii H-404
synthesized self-transfer products in the absence of a suitable accep
tor. The main self-transfer product, using melibiose as a donor substr
ate, was ctosyl-(1,6)-O-alpha-D-galactosyl-(1,6)-D-glucose. This enzym
e had a wide acceptor specificity, D-Glucose, D-galactose, maltose, ma
ltitol, and 1,4-butandiol were the most effective accepters in the tra
nsgalactosylation catalyzed by this enzyme, The enzyme could also tran
sfer a-galactosyl residues to pentoses (L-arabinose, D-xylose, and D-r
ibose) and methyl pentoses (D-fucose and L-rhamnose), The main transfe
r products to lactose, maltose, and sucrose as accepters were identifi
ed as actosyl-(1,6)-O-beta-D-galactosyl-(1,4)-D-glucose, lactosyl-(1,6
)-O-alpha-D-glucosyl-(1,4)-D-glucose, and l-(1,6)-O-alpha-D-glucosyl-(
1,2)-beta-D-fructoside (raffinose), respectively.