摘要
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.
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.
出处
《生物工程学报》
CAS
CSCD
北大核心
1999年第4期533-536,共4页
Chinese Journal of Biotechnology
基金
生物反应器工程国家重点实验室开放课题部分资助
关键词
固定化脂肪酶
动力学
酯化反应
底物抑制
Immobilized lipase, kinetics, esterification, substrate inhibition
