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Oligosaccharide synthesis using a-glucosidases of different origin

Author

Listed:
  • Š. Malá

    (Institute of Chemical Technology - Department of Biochemistry and Microbiology, Prague, Czech Republic)

  • P. Karasová

    (Institute of Chemical Technology - Department of Biochemistry and Microbiology, Prague, Czech Republic)

  • M. Marková

    (Institute of Chemical Technology - Department of Biochemistry and Microbiology, Prague, Czech Republic)

  • B. Králová

    (Institute of Chemical Technology - Department of Biochemistry and Microbiology, Prague, Czech Republic)

Abstract

a-Glucosidase from Aspergillus awamori and intestinal a-glucosidase (saccharase-isomaltase complex) exhibited high transglycosylation activity and were able to synthesize tri- and tetrasaccharides during maltose hydrolysis. Both tested enzymes were also able to transfer the glucose residue to all tested monosaccharide acceptors (D-mannose, D-xylose, L-sorbose and D-galactose). Their transfer activity towards respective acceptors varied and their acceptor preference also depended on the origin of the enzyme. Out of the acceptors tested, both enzymes exhibited high transfer activity in xylose.

Suggested Citation

  • Š. Malá & P. Karasová & M. Marková & B. Králová, 2001. "Oligosaccharide synthesis using a-glucosidases of different origin," Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 19(2), pages 57-61.
    • Handle: RePEc:caa:jnlcjf:v:19:y:2001:i:2:id:6576-cjfs
    DOI: 10.17221/6576-CJFS
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