| Summary: | Abstract Background Oligosaccharide esters are attractive candidates for applications as surfactants, hydrogels and other materials, but direct enzymatic acylation is difficult with carbohydrates longer than disaccharides. Results A combination of one lipase-catalyzed step and one transglycosylation step catalyzed by a cyclodextrin glycosyl transferase (CGTase) was used to synthesize oligosaccharide esters. The conversion of glucose and maltose with vinyl propionate catalyzed by Candida antarctica lipase B (Novozym 435) in dioxane proceeded to full conversion to mixtures of mono and diesters. When ethyl acrylate was used as acyl donor, mono and diesters were formed, but full conversion was not reached. The CGTase catalyzed reactions between the glucose and maltose esters and α-cyclodextrin were carried out in water. In the initial phase, addition of the glucose residues of the cyclodextrin to the ester substrate occurred (coupling reaction), followed by disproportionation reactions yielding a range of oligosaccharide esters with varying chain length. The monoesters were efficient acceptors in the CGTase-catalyzed reactions, while the diesters were not converted to a significant extent. As a consequence, the glucose propionate which contained large amounts of diesters was converted to 40% conversion while the maltose propionate which contained mainly monoesters was converted to 86% conversion. Conclusions A two-step enzymatic process for preparation of oligosaccharide esters has been developed. Oligosaccharide propionates were produced in high yield with a total reaction time of 5 h. The double bond of the acrylate moiety reduced the reaction rate of the lipase catalyzed transesterification, but in both cases, the CGTase efficiently converted the monoesters to oligosaccharide esters.
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