Acylation of glucose catalysed by lipases in supercritical carbon dioxide

✍ Scribed by C. Tsitsimpikou; H. Stamatis; V. Sereti; H. Daflos; F. N. Kolisis

• Publisher: Wiley (John Wiley & Sons)
• Year: 1998
• Tongue: English
• Weight: 306 KB
• Volume: 71
• Category: Article
• ISSN: 0268-2575
• DOI: 10.1002/(sici)1097-4660(199804)71:4<309::aid-jctb859>3.0.co;2-l

✦ Synopsis

The acylation of glucose with lauric acid in a reaction catalysed by two Candida lipases and a Mucor miehei lipase in supercritical carbon dioxide was investigated. A linear dependence of the reaction rate on enzyme (SCCO 2 ) concentration was observed. Studies on the e †ect 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 0É75 for Candida antarctica lipase, 0É53 for Candida rugosa lipase, and between 0É3 and 0É5 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 (