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Kinetic study of the lipase‐catalyzed synthesis of triolein
Author(s) -
Lortie Robert,
Trani Michael,
Ergan Françoise
Publication year - 1993
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260411104
Subject(s) - triolein , lipase , chemistry , catalysis , triacylglycerol lipase , biochemistry , enzyme , chromatography , organic chemistry
The kinetics of the synthesis of triolein catalyzed by immobilized Mucor miehei lipase were studied. Equilibrium constants for the synthesis of mono‐, di‐, and triolein were calculated from the equilibrium compositions for different initial ratios of glycerol and oleic acid by means of multiresponse regression. The 1,3‐specific lipase can catalyze the synthesis of triolein because the ester enzymatically formed with the primary alcohol isomerizes, through acyl migration, to an ester on the secondary hydroxyl. The freed primary hydroxyl may then undergo further enzymatic conversion. The rates of isomerization depend on the concentration of oleic acid. © 1993 Wiley & Sons, Inc.