Marian C. Steverink-de Zoete,Marcel F. M. Kneepkens,Pieter de Waard,Marjolein Woudenberg-van Oosterom,Ted M. Slaghek,K. F. Gotlieb
出处
期刊:Green Chemistry [Royal Society of Chemistry] 日期:1999-01-01卷期号:1 (3): 153-156被引量:10
标识
DOI:10.1039/a901381d
摘要
The lipase-catalyzed esterification of partially acetylated sucrose has been studied. It was shown that the chemical acetylation increased the reaction rate of the subsequent enzymatic acylation. Thus it was possible to perform the enzymatic acylation in the absence of solvents while underivatized sucrose did not react. From HMBC NMR spectroscopy, it was concluded that the main site of acylation was the 6-position of the fructose moiety.