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The enzyme can withstand elevated concentrations of organic solvents, such as acetone (up to 50% v\/v) and 2\u2010propanol (up to 80% v\/v). Thus, it is ideally suited for the preparative\u2010scale enantioselective oxidation of <jats:italic>sec<\/jats:italic>\u2010alcohol and the asymmetric reduction of ketones, using acetone and 2\u2010propanol, respectively, as cosubstrates for cofactor\u2010regeneration via a coupled\u2010substrate approach. The homodimeric protein was found to bear tightly bound zinc and displayed a molecular mass of 38 kDa per subunit as determined by SDS gel electrophoresis. The optimal temperature ranged from 30\u201350\u00b0C and the half\u2010life at 50\u00b0C was 35 h. In addition, excellent storage stability was found. The pH optimum for reduction is pH 6.5; pH 9.0 is preferred for oxidation. The enzyme followed a sequential reaction mechanism. The substrates are medium chain <jats:italic>sec<\/jats:italic>\u2010alcohols or (\u03c9\u20101)\u2010ketones; primary alcohols or aldehydes are not accepted. \u00a9 2004 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/bit.20004","type":"journal-article","created":{"date-parts":[[2004,3,4]],"date-time":"2004-03-04T03:00:41Z","timestamp":1078369241000},"page":"55-62","source":"Crossref","is-referenced-by-count":120,"title":["Purification and characterization of a chemotolerant alcohol dehydrogenase applicable to coupled redox 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