Authors: Erika Nahomy MarinoMarmolejo Antonio De LeónRodríguez Ana Paulina Barba de la Rosa Leticia Santos
Publish Date: 2008/12/05
Volume: 42, Issue: 1, Pages: 61-67
Abstract
Analysis of the Thermoplasma acidophilum DSM 1728 genome identified two putative alcohol dehydrogenase ADH open reading frames showing 504 identity against each other The corresponding genes Ta0841 and Ta1316 encode proteins of 336 and 328 amino acids with molecular masses of 3648 and 3601 kDa respectively The genes were expressed in Escherichia coli and the recombinant enzymes were functionally assessed for activity Throughout the study only Ta1316 ADH resulted active in the oxidative reaction in the pH range 2–8 optimal pH 50 and temperatures from 25 to 90°C optimal 75°C This ADH catalyzes the oxidation of several alcohols such as ethanol methanol 2propanol butanol and pentanol during the reduction of the cofactor NAD+ The highest activity was found in the presence of ethanol producing optically pure acetaldehyde The specific enzyme activity of the purified Ta1316 ADH with ethanol as a substrate in the optimal conditions was 6287 U/mg
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