Acylation of glucose catalysed by lipases in supercritical carbon dioxide
| Autor: | Haralambos Stamatis, Fragiskos N. Kolisis, H. Daflos, V. Sereti, Christina Tsitsimpikou |
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| Rok vydání: | 1998 |
| Předmět: |
General Chemical Engineering
Triacylglycerol lipase Inorganic Chemistry Acylation chemistry.chemical_compound supercritical carbon dioxide glucose acylation lipase Organic chemistry Lipase Waste Management and Disposal Chromatography Supercritical carbon dioxide biology Renewable Energy Sustainability and the Environment Chemistry Organic Chemistry biology.organism_classification Pollution Lauric acid Enzyme assay Candida rugosa Fuel Technology biology.protein Candida antarctica Biotechnology |
| Zdroj: | Journal of Chemical Technology & Biotechnology. 71:309-314 |
| ISSN: | 1097-4660 0268-2575 |
| DOI: | 10.1002/(sici)1097-4660(199804)71:4<309::aid-jctb859>3.0.co;2-l |
| Popis: | 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 70Β°C. Non-immobilised Candida rugosa lipase was found to have a temperature optimum at 60Β°C. The acylation reaction rate depended on the initial water activity of both substrates and enzyme; the optimum was 0Β·75 for Candida antarctica lipase, 0Β·53 for Candida rugosa lipase, and between 0Β·3 and 0Β·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. Β© 1998 SCI Journal of Chemical Technology & Biotechnology |
| Databáze: | OpenAIRE |
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