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