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The effect of aqueous surfactant solutions on alcohol dehydrogenase (LADH)
Author(s) -
Creagh A. L.,
Prausnitz J. M.,
Blanch H. W.
Publication year - 1993
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260410120
Subject(s) - alcohol dehydrogenase , chemistry , circular dichroism , pulmonary surfactant , aqueous solution , alkyl , cationic polymerization , alcohol , adh1b , ethanol , organic chemistry , photochemistry , enzyme , stereochemistry , dehydrogenase , biochemistry , branched chain alpha keto acid dehydrogenase complex
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. © 1993 John Wiley & Sons, Inc.