PMID: 2114098Jun 15, 1990Paper

The effect of substrate partitioning on the kinetics of enzymes acting in reverse micelles

The Biochemical Journal
R BruF García-Carmona

Abstract

A theoretical model for the expression of enzymic activity in reverse micelles previously developed [Bru. Sánchez-Ferrer & García-Carmona (1989) Biochem. J. 259, 355-361] was extended in the present work. The substrate concentration in each reverse-micelle phase (free water, bound water and surfactant apolar tails) and the organic solvent was expressed as a function of the total substrate concentration, taking into account its partition coefficients, that is, partitioning of the substrate in a multiphasic system. In each phase the enzyme expresses a catalytic constant and a Km. Thus the whole reaction rate is the addition of the particular rates expressed in each domain. This model was compared with that developed for a biphasic system [Levashov, Klyachko, Pantin, Khmelnitski & Martinek (1980) Bioorg. Khim. 6, 929-943] by fitting the experimental results obtained with mushroom tyrosinase (working on both 4-t-butylcatechol and 4-methylcatechol) to the two models. The parameters which characterize reverse micelles, omega 0 (water/surfactant molar ratio) and theta (fraction of water) were investigated. The omega 0 profile was shown to be hyperbolic for both substrates. Activity towards 4-t-butylcatechol decreases as theta increase...Continue Reading

Citations

Apr 17, 1998·Critical Reviews in Biochemistry and Molecular Biology·M Tuena de Gómez-Puyou, A Gómez-Puyou
Jul 1, 1991·European Journal of Biochemistry·R Bru, P Walde
Jun 5, 2012·Langmuir : the ACS Journal of Surfaces and Colloids·Yuri A Diaz FernandezJose M Fernandez Hechavarria
Aug 15, 1991·Biochemical and Biophysical Research Communications·Q Mao, P Walde
Dec 31, 2008·Langmuir : the ACS Journal of Surfaces and Colloids·M MoniruzzamanM Goto
May 1, 1994·Enzyme and Microbial Technology·A Sánchez-Ferrer, F García-Carmona

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