Studies of reaction parameters on synthesis of Citronellyl laurate ester via immobilized Candida rugosa lipase in organic media
| Autor: | Azlina Harun Kamaruddin, W. S. Long, N. Aziah Serri |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Acyclic Monoterpenes
Triacylglycerol lipase Bioengineering Amberlite Catalysis Fungal Proteins chemistry.chemical_compound Enzyme Stability Organic chemistry Computer Simulation Organic Chemicals Lipase Citronellol Chromatography biology Lauric Acids Esters General Medicine Enzymes Immobilized Lauric acid Candida rugosa Enzyme Activation Solvent Kinetics Models Chemical chemistry Monoterpenes biology.protein Laurates Biotechnology |
| Zdroj: | Bioprocess and Biosystems Engineering. 29:253-260 |
| ISSN: | 1615-7605 1615-7591 |
| DOI: | 10.1007/s00449-006-0074-z |
| Popis: | Immobilized Candida rugosa lipase was used for the synthesis of citronellyl laurate from citronellol and lauric acid. Screening of different types of support (Amberlite MB-1 and Celite) for immobilization of lipase and solvent (n-hexane, n-heptane, and iso-octane) and optimization of reaction conditions, such as catalyst loading, effect of substrates molar ratio and temperature, have been studied. The maximum enzyme activity was obtained at 310 K. The immobilized C. rugosa lipase onto Amberlite MB-1 support was found to be the best support with a conversion of 89% of citronellyl laurate ester in iso-octane compared to Celite 545. Deactivation of C. rugosa lipase at 313, 318 and 323 K were observed. Ordered bi bi mechanism with dead end complex of lauric acid was found to fit the initial rate data and the kinetic parameters were obtained by non-linear regression analysis. |
| Databáze: | OpenAIRE |
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