Abstract
The kinetics of alcohol oxidation catalyzed by the enzyme horse liver alcohol dehydrogenase (HLADH) is studied in water/alcohol/C12E23 systems with a series of n-alcohols ranging from ethanol to I-decanol or with alpha,omega-alkandiols, namely, 1,5-pentanediol and 1,7-heptanediol. Essentially, the water-rich part of the ternary systems is examined, either without C12E23 or at several constant ...
Abstract
The kinetics of alcohol oxidation catalyzed by the enzyme horse liver alcohol dehydrogenase (HLADH) is studied in water/alcohol/C12E23 systems with a series of n-alcohols ranging from ethanol to I-decanol or with alpha,omega-alkandiols, namely, 1,5-pentanediol and 1,7-heptanediol. Essentially, the water-rich part of the ternary systems is examined, either without C12E23 or at several constant C12E23 concentrations above the cmc (1, 8, and 22 mass %). The substrate inhibition of the enzyme allows one to infer alcohol partition coefficients between the outer aqueous pseudophase and the surfactant aggregation pseudophase. In the case of short-chain n-alcohol (ethanol, I-propanol) and alkandiol (1,5-pentanediol) systems, the alcohol seems to remain in the aqueous pseudophase, whereas in the case of middle- and long-chain n-alcohol (1-butanol to 1-decanol) and alkandiol (1,7-heptandiol) systems, the alcohol participates in the structuration of the micelle.
Altmetric