Theoretical models are developed here for enzymic activity in the presence of direct micellar aggregates. An approach similar to that of Bru et al. [Bru, Sánchez-Ferrer and Garcia-Carmona (1989) Biochem. J. 259, 355–361] for reverse micelles has been adopted. The system is considered to consist of three pseudo-phases: free water, bound water and surfactant tails. The substrate concentration in each pseudo-phase is related to the total substrate concentration in the reaction medium. In the absence of interactions between the enzyme and the micelles, the model predicts either monotonically increasing or monotonically decreasing trends in the calculated reaction rate as a function of surfactant concentration. With enzyme–micelle interactions included in the formulation (by introducing an equilibrium relation between the enzyme confined in the free water and in the bound water pseudo-phases, and by allowing for different catalytic behaviours for the two forms), the calculated reaction rate can exhibit a bell-shaped dependence on surfactant concentration. The effect of the partition of enzyme and substrate is described, as is that of enzyme efficiency in the various pseudo-phases.

Models for enzyme superactivity in aqueous solutions of surfactants

CANTARELLA, Maria
1999

Abstract

Theoretical models are developed here for enzymic activity in the presence of direct micellar aggregates. An approach similar to that of Bru et al. [Bru, Sánchez-Ferrer and Garcia-Carmona (1989) Biochem. J. 259, 355–361] for reverse micelles has been adopted. The system is considered to consist of three pseudo-phases: free water, bound water and surfactant tails. The substrate concentration in each pseudo-phase is related to the total substrate concentration in the reaction medium. In the absence of interactions between the enzyme and the micelles, the model predicts either monotonically increasing or monotonically decreasing trends in the calculated reaction rate as a function of surfactant concentration. With enzyme–micelle interactions included in the formulation (by introducing an equilibrium relation between the enzyme confined in the free water and in the bound water pseudo-phases, and by allowing for different catalytic behaviours for the two forms), the calculated reaction rate can exhibit a bell-shaped dependence on surfactant concentration. The effect of the partition of enzyme and substrate is described, as is that of enzyme efficiency in the various pseudo-phases.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/9296
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