Schirmer, Christine and Liu, Y. and Touraud, D. and Meziani, A. and Pulvin, S. and Kunz, Werner (2002) Horse liver alcohol dehydrogenase as a probe for nanostructuring effects of alcohols in water/nonionic surfactant systems. JOURNAL OF PHYSICAL CHEMISTRY B, 106 (30). pp. 7414-7421. ISSN 1520-6106
Full text not available from this repository.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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PREPARING NONTOXIC MICROEMULSIONS; SODIUM DODECYL-SULFATE; ENZYMATIC-REACTIONS; AQUEOUS-SOLUTIONS; MICELLAR SYSTEMS; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry) > Prof. Dr. Werner Kunz |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Oct 2021 07:00 |
| Last Modified: | 12 Oct 2021 07:00 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40045 |
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