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Enzyme and organic solvents: horse liver alcohol dehydrogenase in non-ionic microemulsion: stability and activity
1Laboratorie de Chimie Organique Biologique, UA no. 31, Institut de Chimie, Université Louis Pasteur, Strasbourg, France.
Abstract:
In a microemulsion made with Triton X-100, the stability of the enzymatic activity was higher than in ionic microemulsions. The stability increased with water content. The kinetic constants (Michaelis constant of NAD+ and maximum velocity) were close to those found in the previously studied microemulsions. The Michaelis constant of NAD+ expressed with respect to the buffer volume was higher than in water. The pH dependence of the kinetic constants in this microemulsion was determined. The activity determined by NAD+ reduction decreased with water content, whereas the redox activity determined via butanol oxidation coupled to retinal reduction was only slightly reduced.