Journal ArticleDOI
Transgalactosylation Catalyzed by α-Galactosidase from Candida guilliermondii H-404
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TLDR
The thermostable α-galactosidase from Candida guilliermondii H-404 synthesized self-transfer products in the absence of a suitable acceptor, which had a wide acceptor specificity.Abstract:
The thermostable α-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-α-D-galactosyl-(1,6)-O-α-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 α-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-α-D-galactosyl-(1,6)-O-β-D-galactosyl-(1,4)-D-glucose, O-α-D-galactosyl-(1,6)-O-α-D-glucosyl-(1,4)-D-glucose, and O-α-D-galactosyl-(1,6)-O-α-D-glucosyl-(1,2)-β-D-fructoside (raffinose), respectively.read more
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Journal ArticleDOI
Differentiation of green, white, black, Oolong, and Pu-erh teas according to their free amino acids content.
Ángela Alcázar,Oscar Ballesteros,J. M. Jurado,Fernando de Pablos,M. J. Martín,J L Vilches,Alberto Navalón +6 more
TL;DR: The amino acid contents were used as chemometric descriptors for classification purposes of different tea varieties and 100% success was obtained in the classification of green, black, Oolong, white, and Pu-erh teas.
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Three alpha-galactosidase genes of Trichoderma reesei cloned by expression in yeast.
TL;DR: The calculated molecular mass and the hydrolytic properties of AGLI indicate that it corresponds to the α-galactosidase previously purified from T. reesei, and the deduced amino acid sequences of A GLI and AGLIII showed similarity with the β-mannosidases of plant, animal, yeast and filamentous fungal origin.
Journal ArticleDOI
Cloning of the Gene Encoding a Novel Thermostable α-Galactosidase from Thermus brockianus ITI360
TL;DR: An α-galactosidase gene from Thermus brockianusITI360 was cloned, sequenced, and expressed in Escherichia coli, and the recombinant protein was purified and displayed high affinity for oligomeric substrates.
Journal ArticleDOI
Transglycosidase activity of Bifidobacterium adolescentis DSM 20083 alpha-galactosidase.
K.M.J. van Laere,R. Hartemink,Gerrit Beldman,Stuart M. Pitson,C. Dijkema,Henk A. Schols,Alphons G. J. Voragen +6 more
TL;DR: The enzyme was found to act with retention of configuration (α→α), releasing α-galactose from p-nitrophenyl galactoside, and probably operates with a double-displacement mechanism, and is consistent with the observed glycosyltransferase activity.
Journal ArticleDOI
Microbial production and biotechnological applications of α-galactosidase
TL;DR: This ubiquitous enzyme has been vastly commercialized and holds greater future prospects, including therapeutic advances in treatment of Fabry disease, blood group conversion and removal of α-gal type immunogenic epitopes in xenotransplantation.
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