ENZYMATIC REDUCTION BY ALCOHOL DEHYDROGENASE TA1316 FROM Thermoplasma acidophilum
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...
| Autores: | , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2017 |
| País: | México |
| Recursos: | Instituto Potosino de Investigación Científica y Tecnológica A.C. |
| Repositorio: | Redalyc-IPICYT |
| OAI Identifier: | oai:redalyc.org:62049878004 |
| Acesso em linha: | https://www.redalyc.org/articulo.oa?id=62049878004 |
| Access Level: | acceso abierto |
| Palavra-chave: | Ingeniería Ta1316 characterization reduction reaction Alcohol dehydrogenase Thermoplasma acidophilum |
| Resumo: | 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. |
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