Literature DB >> 18601257

The effect of aqueous surfactant solutions on alcohol dehydrogenase (LADH).

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


  1 in total

1.  Kinetics of ethanol oxidation catalyzed by yeast alcohol dehydrogenase in aqueous solutions of sodium dodecylsulfate.

Authors:  Elsa Abuin; Eduardo Lissi; Luis León
Journal:  Protein J       Date:  2008-06       Impact factor: 2.371

  1 in total

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