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Lipase catalyzed transesterification of ethyl butyrate synthesis in n -hexane- a kinetic study.
Journal of Food Science and Technology 2017 August
Kinetics of lipase catalyzed transesterification of ethyl caprate and butyric acid was investigated. The objective of this work was to propose a reaction mechanism and develop a rate equation for the synthesis of ethyl butyrate by transesterification using surfactant coated lipase from Candida rugosa . The reaction rate could be described in terms of Michaelis-Menten equation with a Ping-Pong Bi-Bi mechanism and competitive inhibition by both the substrates. The values of kinetic parameters computed were Vmax = 2.861 μmol/min/mg; Km(acid) = 0.0746 M; Km(ester) = 0.125 M; Ki acid = 0.450 M. This study indicated a competitive enzyme inhibition by butyric acid during lipase catalyzed transesterification reaction. Experimental observations had clearly indicated that the substrates as well as product act as dead-end inhibitors.
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