Acylation of glucose catalysed by lipases in supercritical carbon dioxide

• Main Authors: Tsitsimpikou, C, Stamatis, H, Sereti, V, Daflos, H, Kolisis, FN
• Format: Article in Journal/Newspaper
• Language: English
• Published: JOHN WILEY & SONS LTD 1998
• Subjects: Glucose acylation; Lipase; Supercritical carbon dioxide; Biotechnology & Applied Microbiology; Chemistry; Multidisciplinary; Engineering; Chemical; carbon dioxide; glucose; lauric acid; triacylglycerol lipase; water; acylation; article; candida; catalyst; chemical reaction kinetics; enzyme activity; mucor; Candida antarctica; Candida rugosa; Mucor miehei; Catalysis; Catalyst activity; Composition effects; Enzymes; Organic acids; Organic solvents; Reaction kinetics; Thermal effects; Thermodynamic stability; Rugosa; Antarc*; Antarctica
• Online Access: http://dspace.lib.ntua.gr/handle/123456789/12560; https://doi.org/10.1002/(SICI)1097-4660(199804)71:4<309::AID-JCTB859>3.0.CO;2-L

The acylation of glucose with lauric acid in a reaction catalysed by two Candida lipases and a Mucor miehei lipase in supercritical carbon dioxide (SCCO2) 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 degrees C. Non-immobilised Candida rugosa lipase was found to have a temperature optimum at 60 degrees 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. (C) 1998 SCI.