The kinetics of the esterification of ethanol and hexanoic acid by immobilized lipase from Mucor miehei in heptane were investigated.The reaction follows Michaelis Menton kinetics as observed from the relationship of ...The kinetics of the esterification of ethanol and hexanoic acid by immobilized lipase from Mucor miehei in heptane were investigated.The reaction follows Michaelis Menton kinetics as observed from the relationship of initial rate of the reaction,both as a function of enzyme and of substrate concentration. The kinetics of reaction are suggested to agree with a Ping Pong Bi Bi mechanism.The substrate inhibition by excess of ethanol has been identified at its concentration of more than 0.2 mol/L.Under the condition of no significantly diffused inhibiton,kinetic parameters of the reaction have been measured.The Michaelis constants for hexanoic acid ( K m hexanoic acid)and for ethanol( K m ethanol) are 85.34 mmol/L and 33.59 mmol/L respectively.The maximum rate of the reaction ( V m) is 79.82 mmol/(min·g) The inhibitor constant of ethanol ( K i) is 89.1 mmol/L.展开更多
文摘The kinetics of the esterification of ethanol and hexanoic acid by immobilized lipase from Mucor miehei in heptane were investigated.The reaction follows Michaelis Menton kinetics as observed from the relationship of initial rate of the reaction,both as a function of enzyme and of substrate concentration. The kinetics of reaction are suggested to agree with a Ping Pong Bi Bi mechanism.The substrate inhibition by excess of ethanol has been identified at its concentration of more than 0.2 mol/L.Under the condition of no significantly diffused inhibiton,kinetic parameters of the reaction have been measured.The Michaelis constants for hexanoic acid ( K m hexanoic acid)and for ethanol( K m ethanol) are 85.34 mmol/L and 33.59 mmol/L respectively.The maximum rate of the reaction ( V m) is 79.82 mmol/(min·g) The inhibitor constant of ethanol ( K i) is 89.1 mmol/L.
