TY - JOUR
T1 - Cellulase-catalysed glycosylation reactions
T2 - Simple route towards a highly selective synthesis of oligosaccharides
AU - Karthaus, Olaf
AU - Shoda, Shin Ichiro
AU - Takano, Hiroshi
AU - Obata, Kei
AU - Kobayashi, Shiro
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1994
Y1 - 1994
N2 - Cellulase (EC 3.2.1.4) can be used for the enzyme-catalysed synthesis of oligosaccharides in a mixed buffer/organic solvent system. Besides glucopyranosides and cellooligosaccharides, non-glucosidic saccharides and modified glucoses as glycosyl acceptors also react with β-lactosyl fluoride as glycosyl donor. The reaction proceeds in a completely stereo- and regio-specific manner, giving rise to coupling products having β(1→4) glycosidic bonds exclusively. Based on these results, a model for the active site of cellulase (Trichoderma viride) and the orientation of the donor and acceptor therein is proposed.
AB - Cellulase (EC 3.2.1.4) can be used for the enzyme-catalysed synthesis of oligosaccharides in a mixed buffer/organic solvent system. Besides glucopyranosides and cellooligosaccharides, non-glucosidic saccharides and modified glucoses as glycosyl acceptors also react with β-lactosyl fluoride as glycosyl donor. The reaction proceeds in a completely stereo- and regio-specific manner, giving rise to coupling products having β(1→4) glycosidic bonds exclusively. Based on these results, a model for the active site of cellulase (Trichoderma viride) and the orientation of the donor and acceptor therein is proposed.
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U2 - 10.1039/p19940001851
DO - 10.1039/p19940001851
M3 - Article
AN - SCOPUS:11744326730
SP - 1851
EP - 1857
JO - Journal of the Chemical Society. Perkin Transactions 1
JF - Journal of the Chemical Society. Perkin Transactions 1
SN - 1470-4358
IS - 13
ER -