| Literature DB >> 18601257 |
A L Creagh1, J M Prausnitz, H W Blanch.
Abstract
Alcohol dehydrogenase (LADH) was studied in aqueous solutions of surfactants to determine its structural and catalytic characteristics. Fluorescence, circular dichroism (CD), and electron paramagnetic resonance (ERP) techniques were used to study structural changes to the enzyme. The activity of LADH in catalyzing the oxidation of ethanol was investigated. Short-chain alkyl sulfonates and sulfates did not deactivate LADH or alter its structure. Longer and branched alkyl sulfates and sulfonates, as well as a cationic surfactant (CTAB), affected both LADH activity and conformation.Entities:
Year: 1993 PMID: 18601257 DOI: 10.1002/bit.260410120
Source DB: PubMed Journal: Biotechnol Bioeng ISSN: 0006-3592 Impact factor: 4.530