Kinetics of ethanol oxidation catalyzed by yeast alcohol dehydrogenase in aqueous solutions of sodium dodecylsulfate.
A study has been made of the effect of sodium dodecylsufate (SDS) addition on the oxidation of ethanol catalyzed by yeast alcohol dehydrogenase. Experiments were performed at pH = 8.1 and SDS concentrations employed were below and above the surfactant critical micelle concentration (CMC). The double reciprocal plots obtained in the absence and in the presence of the surfactant were compatible with a sequential bi-bi ordered mechanism. In the presence of the surfactant the initial reaction rates were consistently lower than in pure buffer at all the surfactant concentrations considered (0.5-50 mM). This effect is mainly due to an increase in the dissociation constant of beta-NAD(+) which reaches its maximum value (7,100 +/- 1,700 microM) at the CMC. Above the CMC the effect of the surfactant is mainly due to an increase in the Michaels constants of the alcohol, with values of 41 +/- 1 mM for 15 mM SDS and 50 +/- 1 mM for 50 mM SDS. The catalytic rate constant was found to be practically independent of the presence of the surfactant in the range of concentrations considered (up to 50 mM).
Abuin
Elsa
E
Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Casilla 40-Correo 33, Santiago, Chile. eabuin@lauca.usach.cl
Lissi
Eduardo
E
León
Luis
L
D000426:Alcohol Dehydrogenase / Q000187:drug effects / Q000378:metabolism*; D000431:Ethanol / Q000378:metabolism*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*
D012967:Sodium Dodecyl Sulfate; D000431:Ethanol; D000426:Alcohol Dehydrogenase