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Acylation of glucose catalysed by lipases in supercritical carbon dioxide
Author(s) -
Tsitsimpikou C.,
Stamatis H.,
Sereti V.,
Daflos H.,
Kolisis F. N.
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(199804)71:4<309::aid-jctb859>3.0.co;2-l
Subject(s) - candida rugosa , candida antarctica , lipase , chemistry , acylation , mucor , rhizomucor miehei , lauric acid , triacylglycerol lipase , organic chemistry , chromatography , catalysis , enzyme , fatty acid , food science , penicillium
The acylation of glucose with lauric acid in a reaction catalysed by two Candida lipases and a Mucor miehei lipase in supercritical carbon dioxide (SCCO 2 ) was investigated. A linear dependence of the reaction rate on enzyme concentration was observed. Studies on the effect of temperature on enzyme activity showed that Candida antarctica lipase remains stable at temperatures as high as 70°C. Non‐immobilised Candida rugosa lipase was found to have a temperature optimum at 60°C. The acylation reaction rate depended on the initial water activity of both substrates and enzyme; the optimum was 0·75 for Candida antarctica lipase, 0·53 for Candida rugosa lipase, and between 0·3 and 0·5 for Mucor miehei lipase. Candida rugosa lipase was most active at a molar ratio of sugar: acyl donor of 1: 3, while the optimum ratio was found to increase to 1: 6 when the reaction was catalysed by Candida antarctica and Mucor miehei lipases. © 1998 SCI