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Kinetic studies on immobilised lipase esterification of oleic acid and octanol
Author(s) -
Yong Yee Peng,
AlDuri Bushra
Publication year - 1996
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199603)65:3<239::aid-jctb433>3.0.co;2-h
Subject(s) - enzyme kinetics , lipase , oleic acid , chemistry , kinetics , rhizomucor miehei , substrate (aquarium) , octanol , chromatography , triacylglycerol lipase , organic chemistry , enzyme , active site , partition coefficient , biochemistry , biology , physics , quantum mechanics , ecology
The present work investigates the reaction kinetics of immobilised lipase esterification of oleic acid and octanol, in a solvent‐free system. Lipase from Rhizomucor miehei was immobilised on a hydrophobic support. The initial reaction rate was investigated as a function of octanol concentration and temperature, and the reaction kinetics were described in terms of the Michaelis–Menten mechanism. Evaluating K m , V max and k cat / K m as a function of temperature, it was found that K m was minimum and k cat / K m was maximum at 40°C while V max was maximum at 50°C. Furthermore, applying the Ping Pong Bi Bi mechanism yielded good results for this two‐substrate system.