Horse liver alcohol dehydrogenase as a probe for nano-structuring effects of alcohols in water/nonionic surfactant systems

C. Schirmer (1) , Yehan Liu (2) , D. Touraud (3) , A. Meziani (3) , S. Pulvin (3) , W. Kunz (3)

1 University of Regensburg
2 Peking University [Beijing]
3 GEC - Génie Enzymatique et Cellulaire

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 1-decanol or with ,-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, 1-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.

Domaines: Biochimie, Biologie Moléculaire

C. Schirmer, Yehan Liu, D. Touraud, A. Meziani, S. Pulvin, et al.. Horse liver alcohol dehydrogenase as a probe for nano-structuring effects of alcohols in water/nonionic surfactant systems. Journal of Physical Chemistry B, 2002, 106, pp.7414-7421. ⟨10.1021/jp014386r⟩. ⟨hal-00088754⟩