A kinetic model for the enzyme‐catalyzed self‐epoxidation of oleic acid

This paper reports a kinetic model for the selfepoxidation of oleic acid with toluene as solvent and Novozym 435 (a commercially available preparation of immobilized Candida antarctica lipase) as catalyst at 30°C. The effects of various parameters on the conversion and rates of reaction were studied...

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Veröffentlicht in:	Journal of the American Oil Chemists' Society 2001-04, Vol.78 (4), p.347-351
Hauptverfasser:	Yadav, G. D., Manjula Devi, K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Applied sciences Biological and medical sciences Catalysis Chemical industry and chemicals Chemical kinetics enzyme deactivation Enzymes Enzymes and enzyme inhibitors Exact sciences and technology Fundamental and applied biological sciences. Psychology Hydrogen peroxide Hydrolases immobilized lipase Manufacturing and processing Mathematical models Oils and fats oleic acid Reaction kinetics self‐epoxidation Toluene
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Beschreibung
Zusammenfassung:	This paper reports a kinetic model for the selfepoxidation of oleic acid with toluene as solvent and Novozym 435 (a commercially available preparation of immobilized Candida antarctica lipase) as catalyst at 30°C. The effects of various parameters on the conversion and rates of reaction were studied. Both the initial rate and the progress curve data were used to fit an ordered bi‐bi model. At low temperatures, the rate of epoxidation was faster than the rate of deactivation of the enzyme by hydrogen peroxide.
ISSN:	0003-021X 1558-9331
DOI:	10.1007/s11746-001-0267-2