4.3 Article

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

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AMER OIL CHEMISTS SOC A O C S PRESS
DOI: 10.1007/s11746-001-0267-2

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chemical kinetics; enzyme deactivation; immobilized lipase; oleic acid; self-epoxidation

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This paper reports a kinetic model for the self epoxidation of oleic acid with toluene as solvent and Novozym 435 (a commercially available preparation of immobilized Candida antarctica lipase) as catalyst at 30 degreesC. 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.

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