Evaluation of Activation Energy and Thermodynamic Properties of Enzyme-Catalysed Transesterification Reactions

DOI: 10.4236/aces.2012.21018   PDF   HTML     9,661 Downloads   18,130 Views   Citations


In this study, the activation energy and thermodynamic properties of immobilized enzyme catalysed transesterification reactions were evaluated based on the enzyme substrate transition theory. The activation energy for a enzyme catalysed biodiesel production system were found to be 4.25 (kcal/mole) for monoglyceride formation, 5.58(kcal/mole) for diglyceride formation and 5.50 (kcal/mole) for methyl ester formation respectively. The rate constants were found to be 3.2 × 1010(L/mol.sec) monoglyceride, 3.47 × 109 (L/mol.sec) for diglyceride and 3.93 × 109 (L/mol.sec) for methyl ester. Based on the present work and published literatures, the activation energy of enzyme-catalysed transesterification reactions were found to be lower than the chemical-catalysed and non-catalyzed transesterification reactions. The thermodynamic properties of immobilized enzyme-catalysed transesterification reaction were found to be Gibbs free energy (ΔG = –1.02 kcal/mol), enthalpy (ΔH = 544 cal/mol) and entropy (ΔS = 5.19 cal/Kmol).

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R. Pogaku, J. Raman and G. Ravikumar, "Evaluation of Activation Energy and Thermodynamic Properties of Enzyme-Catalysed Transesterification Reactions," Advances in Chemical Engineering and Science, Vol. 2 No. 1, 2012, pp. 150-154. doi: 10.4236/aces.2012.21018.

Conflicts of Interest

The authors declare no conflicts of interest.


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