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Lipase‐catalyzed esterification of oleic acid and methanol in hexane—A kinetic study
Author(s) -
Ramamurthi Suresh,
McCurdy Alan R.
Publication year - 1994
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02542255
Subject(s) - methanol , chemistry , oleic acid , catalysis , lipase , kinetics , hexane , reaction rate , substrate (aquarium) , organic chemistry , reaction rate constant , chemical kinetics , enzyme kinetics , reaction mechanism , chromatography , enzyme , active site , biochemistry , physics , oceanography , quantum mechanics , geology
The kinetics of immobilized lipase‐catalyzed esterification of oleic acid and methanol in hexane 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. Inhibition by excess of methanol has been identified. The kinetic constants have been measured for the reaction in the absence of any significant external diffusional limitations. The kinetics of the enzymatic reaction are suggested to agree with a Ping‐Pong Bi Bi mechanism.