Enzymatic reduction by alcohol dehydrogenase TA1316 from Thermoplasma acidophilum

Abstract

"In this work we present the NADH-dependent Ta1316 alcohol dehydrogenese (ADH) characterization for its reducingreaction in the presence of aldehydes, ketones and keto-esters. In the presence of 2 mM acetaldehyde, Ta1316 ADHshowed a remarkable thermal activity, displaying activity at temperatures up tp 90”C and low pH with a requirement ofZ+2to reach its maximum activity. In contrast to other characterized ADHs, Ta1316 ADH reduces methyl pyruvate, analpha-ketoester as its preferred substrate. We conclude that Ta1316 ADH’s principalfunction is the reduction of substratesand is potentially an enzyme that can be used in biotechnology, as erll as in industrial applications. "

"En este trabajo presentamos la caracterización de la actividad enzimática reductora de la enzima alcohol deshidrogenasa (ADH) Ta1316 dependiente de NADH en presencia de aldehídos, cetonas y ceto ́esteres. La ADH Ta1316 mostr ́o estabilidadt ́ermica notable con actividad m ́axima a temperatura de 90”C y pH ac ́ıdico en presencia del cofactor Zn+2y acetaldeh ́ıdo2 mM. En contraste con otras ADHs caracterizadas, Ta1316 es capaz de reducir metil-piruvato, un alfa-cetoéster como susustrato preferido. Concluimos que la función principal de la Ta1316 ADH es la reducción de sustratos y es una enzima que podría ser utilizada potencialmente en aplicaciones biotecnológicas e industriales."