Abstract
Abstract Alkyl derivatives of glucose, galactose and fructose were acylated by lipase-catalyzed transesterification with alkanoic esters. The best results were obtained with immobilized lipases of the Candida antarctica type. Primary alcohol functions were acylated first; followed by secondary ones depending on the structure of the glycoside. The water activity in the reaction medium had a striking effect on both the rate and the selectivity of the process. The size and orientation of the alkyl substituent and the structure of the acyl acceptor were also found to exert a profound influence on the course of the reaction.
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