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A kinetic model for enzymatic reactions in reverse micellar systems involving water‐insoluble substrates and enzyme activators
Author(s) -
Hayashi Y,
Talukder MMR,
Takeyama T,
Wu JC,
Kawanishi T,
Shimizu N
Publication year - 2003
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/jctb.866
Subject(s) - lipase , chemistry , candida antarctica , michaelis–menten kinetics , micelle , hydrolysis , enzyme , hydrolase , glycerol , peg ratio , triacylglycerol lipase , enzyme catalysis , organic chemistry , enzyme assay , chromatography , finance , aqueous solution , economics
The activity of Chromobacterium viscosum lipase (glycerol‐ester hydrolase, EC 3.1.1.3) entrapped in AOT/isooctane reverse micelles was significantly increased by the addition of short chain polyethylene glycols (PEGs) or methoxypolyethylene glycols (MPEGs) for the hydrolysis of olive oil. To understand enzyme activity in the presence of PEG 400 or MPEG 550 molecules, a kinetic model was proposed. The validity of this model was verified by experimental data on the lipase‐catalyzed hydrolysis of olive oil in AOT/isooctane reverse micellar systems, in which PEG 400 or MPEG 550 had been added. The large value of the equilibrium constant ( k D ) for enzyme activation indicated that the affinity between C viscosum lipase and PEG 400 or MPEG 550 molecules was very strong. The Michaelis constant ( K m ) predicted by the proposed model explained enzymatic reactions more exactly than that by the previously published model. Copyright © 2003 Society of Chemical Industry