کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
18691 | 42735 | 2006 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Analysis of solvent-free ethyl oleate enzymatic synthesis at equilibrium conditions Analysis of solvent-free ethyl oleate enzymatic synthesis at equilibrium conditions](/preview/png/18691.png)
This work reports experimental equilibrium data for the esterification of pure oleic acid and a fatty acid mixture with ethanol, using an immobilized Candida antarctica B lipase as catalyst. Reactions are performed in a solvent-free system, containing a mixture of substrates and different amounts of distilled water. According to the initial amount of water and the extent of the reaction, one or two liquid phases are present. Therefore, when the equilibrium is achieved, the liquid–liquid and chemical reaction equilibria have to be simultaneously satisfied.Several reports dealing with enzymatic reactions performed in two-phase systems have found that the value of the reaction equilibrium constant calculated from overall experimental concentrations varies not only with temperature but also with substrate ratio and water content. Although this approach is a valuable way to explore equilibrium shifts in biphasic systems, it is limited to ideal systems with constant partition coefficients. The aim of this work is to consider the biphasic nature of the reactive mixture through a computational procedure that simultaneously takes into account liquid–liquid and reaction equilibria. This approach enables the determination of a classical temperature-dependent thermodynamic equilibrium constant, which accurately fits experimental equilibrium conversions over a wide range of operating conditions.
Journal: Enzyme and Microbial Technology - Volume 38, Issue 7, 2 May 2006, Pages 914–920