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Enzymatic synthesis of manno‐ and heteromanno‐oligosaccharides using α‐mannosidases: A comparative study of linkage‐specific and non‐linkage‐specific enzymes
Author(s) -
Suwasono Sony,
Rastall Robert A.
Publication year - 1998
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199809)73:1<37::aid-jctb931>3.0.co;2-r
Subject(s) - cellobiose , chemistry , enzyme , oligosaccharide , mannose , stereochemistry , lactose , yield (engineering) , disaccharide , substrate (aquarium) , mannosidase , biochemistry , biology , cellulase , ecology , materials science , metallurgy
Two α‐mannosidase enzymes (EC 3.2.1.24) and an α‐1,2‐mannosidase enzyme (EC 3.2.1.113) were compared for their ability to synthesise hetero‐oligosaccharides by the equilibrium approach (condensation reaction). A panel of disaccharide acceptors was used and product yields and product spectra determined. Choice of enzyme had a significant influence on product yield, with yield being dependent on enzyme and substrate combination. Most of the enzyme/substrate combinations tested gave 1→6 linked manno‐oligosaccharides as the principal product. Mannose was linked to lactose, cellobiose and lactulose by both 1→3 and 1→6 linkages in ratios that depended upon the enzyme used. Homo‐oligosaccharide (mannotriose) formation was found in all but one of the enzyme/substrate combinations tested and, in the case of the α1,2‐mannosidase, the structure of the mannotrioses depended upon the acceptor used. Formation of hetero‐oligosaccharides over homo‐oligosaccharides could be favoured by use of low mannose: acceptor ratios. © 1998 Society of Chemical Industry