Add time:08/27/2019         Source:sciencedirect.com

A kinetic study of 2-methyl butyric acid esterification reaction catalyzed by immobilized lipase (from Candida antarctica) has been made in a range of 62 – 78°C temperature. The kinetic characteristics observed in the chiral resolution of (±) 2-methyl butyric acid by esterification reaction with n-octanol were found to conform to an ordered bi-bi mechanism with competitive inhibition by reactants and products. According to the mechanism maximum reaction rate, Michaelis Menten constants and inhibition constants were determined. The results suggest that lipase should recognize the chirality of 2-methyl butyric acid molecule in the binding process to the active site of lipase. A good quality of fit was observed by fitting experimental rate data to the kinetic model.

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