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Transgalactosylation Catalyzed by α -Galactosidase from Candida guilliermondii H-404

1995; Oxford University Press; Volume: 59; Issue: 4 Linguagem: Inglês

10.1271/bbb.59.619

1347-6947

Hiroyuki Hashimoto, Chie Katayama, Masaru Goto, Tatsuyuki Okinaga, Sumio Kitahata,

Microbial Metabolites in Food Biotechnology

The thermostable alpha-galactosidase from Candida guilliermondii H-404 synthesized self-transfer products in the absence of a suitable acceptor. The main self-transfer product, using melibiose as a donor substrate, was O-alpha-D-galactosyl-(1,6)-O-alpha-D-galactosyl-(1,6)-D-glucose. This enzyme had a wide acceptor specificity. D-Glucose, D-galactose, maltose, maltitol, and 1,4-butandiol were the most effective acceptors in the transgalactosylation catalyzed by this enzyme. The enzyme could also transfer alpha-galactosyl residues to pentoses (L-arabinose, D-xylose, and D-ribose) and methyl pentoses (D-fucose and L-rhamnose). The main transfer products to lactose, maltose, and sucrose as acceptors were identified as O-alpha-D-galactosyl-(1,6)-O-beta-D-galactosyl-(1,4)-D-glucose, O-alpha-D-galactosyl-(1,6)-O-alpha-D-glucosyl-(1,4)-D-glucose, and O-alpha-D-galactosyl-(1,6)-O-alpha-D-glucosyl-(1,2)-beta-D-fructoside (raffinose), respectively.