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EN
Dextransucrase catalyses the synthesis of a-D-glucopyranosyl homopolymers and oligomers from sucrose as a substrate. This paper is a review of reports on the mechanism of dextran and oligosaccharides synthesis. The presence of a low molecular acceptor dextran (3-20 kDa) or low molecular acceptor sugars in reaction mixtures enables obtaining of dextran with molecular weight in a range from 30 to 80 kDa or oligosaccharides with low d.p., which have gained increased nutritional interest (prebiotics). In these reactions, the hydrolytic enzyme, i.e. dextranase, may be involved together with dextransucrase instead of acceptors.
EN
An approach for enzymatic sythesis of oligosachcharides via transglycosylation with endo-beta-1,3-glucanase from Oerskovia xanthineolytica is described.Linear -beta-1,3-glucan (laminarin) was used as a donor of glycosyl residues, whereas nitrophenyl glycosides of different monosaccharides served as acceptors.The synthesis was performed in water-organic solvent environment with several combinations of donor/acceptor.Employing p-nitrophenyl-beta-D-xylopyranoside as an acceptor in the presence of 30% acetonitrile resulted in the production of six new glycosides shown by FAB MS to be di-, tri- and tetrasaccharides.This enzyme is therefore suitable for the synthesis of short-chain oligosaccharides.
EN
The review is focused on recent advances in the enzymatic synthesis of oligosaccharides by exoglycosidases. Reversed hydrolysis, transglycosylation and glycosidase-mediated coupling have been discussed. Relations between catalytic properties of the enzyme used, acceptor molecular structure and their effect on the synthesis results have been highlighted. The work contains 55 references the majority of which appeared after 1996.
EN
A key role of oligosaccharides in biological processes becoming more obvious every day. An increasing interest in this group of biomolecules is related to their broad spectrum of applications, i.e. in food, feed and pharmaceutical industries, in cosmetics and medicine. Efficient, full-scale processes that allow to produce different types of these oligomers are of graet importance. Biocatalysis is considered very attractive in comparison to the non specific, time-consuming and often environmental unfriendly chemical technologies of oligosaccharide production. Two groups of enzymes are involved in this process, transferases and glycosidase. This review describes oligosaccharide synthesis through the reactions of transfer, transglycosylation and reverse hydrolysis.
Biotechnologia
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2005
|
issue 2
103-124
EN
Enzyme ? mediated polymer synthesis in non-natural environments has significantly expanded in scope and impact over the past 10 years. This review focuses on a rapidly expanding research activity where in vitro enzyme catalysis is used for the synthesis of polyesters, polycarbonates, polyphenols, vinyl polymers, as well as natural and artificial oligosaccharides like cellulose, amylose, xylan, and chitin. The inclination to use enzymes for polymer synthesis has been fuelled by a desire to carry out these reactions in the absence of heavy metal-based catalysts, under mild conditions and with high selectivity. The aspects of this work that include enzyme-catalyzed step-growth polycondensation, chain-growth ring-opening polymerizations, oxidation polymerization and corresponding transesterification of macromolecular substrates are discussed. The polymerization utilizes mainly hydrolases and oxidoreductases as catalysts. Characteristic features of enzymatic polymerizations are also discussed.
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