Enzyme and organic solvents: horse liver alcohol dehydrogenase in non-ionic microemulsion: stability and activity.
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.
Lee
K M
KM
Laboratorie de Chimie Organique Biologique, UA no. 31, Institut de Chimie, Université Louis Pasteur, Strasbourg, France.
Biellmann
J F
JF
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000818:Animals; D004655:Emulsions; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D011092:Polyethylene Glycols; D012997:Solvents
D004655:Emulsions; D012997:Solvents; D009243:NAD; D011092:Polyethylene Glycols; D000426:Alcohol Dehydrogenase