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Kinetics of enzymatic synthesis of isopropylidene glycerol esters by goat pregastric lipase
Author(s) -
Lai Douglas T.,
Hattori Norikatsu,
O’Connor Charmian J.
Publication year - 1999
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/s11746-999-0075-6
Subject(s) - caproic acid , chemistry , glycerol , lipase , enzyme , catalysis , reaction rate , partition coefficient , substrate (aquarium) , enzyme catalysis , michaelis–menten kinetics , biocatalysis , kinetics , organic chemistry , biochemistry , reaction mechanism , enzyme assay , oceanography , geology , physics , quantum mechanics
The goat pregastric lipase‐catalyzed esterification of isopropylidene glycerol with caproic acid, to form isopropylidene glycerol caproate, followed a ping pong bi bi mechanism incorporating an acyl‐enzyme intermediate. The maximum rate was estimated to be 96 µmol min −1 mg −1 in isooctane at 35°C, and the Michaelis‐Menten constants for isopropylidene glycerol and caproic acid were 0.23 and 0.32 M, respectively. The catalyzed rate also correlated well with the partition coefficient of caproic acid between the organic and aqueous phases. The results suggest that the desolvation energy of the substrate from the bulk medium to the active site of the enzyme dominates the reaction rate for the enzyme‐catalyzed reaction in organic media.