{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,8]],"date-time":"2025-12-08T22:11:50Z","timestamp":1765231910198,"version":"build-2065373602"},"reference-count":36,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2010,11,26]],"date-time":"2010-11-26T00:00:00Z","timestamp":1290729600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotech &amp;amp; Bioengineering"],"published-print":{"date-parts":[[2011,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Chiral 1\u2010(<jats:italic>o<\/jats:italic>\u2010chlorophenyl)\u2010ethanols are key intermediates in the synthesis of chemotherapeutic substances. Enantioselective reduction of <jats:italic>o<\/jats:italic>\u2010chloroacetophenone is a preferred method of production but well investigated chemo\u2010 and biocatalysts for this transformation are currently lacking. Based on the discovery that <jats:italic>Candida tenuis<\/jats:italic> xylose reductase converts <jats:italic>o<\/jats:italic>\u2010chloroacetophenone with useful specificity (<jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub>\/<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub>\u2009=\u2009340\u2009M<jats:sup>\u22121<\/jats:sup>\u2009s<jats:sup>\u22121<\/jats:sup>) and perfect <jats:italic>S<\/jats:italic>\u2010stereoselectivity, we developed whole\u2010cell catalysts from <jats:italic>Escherichia coli<\/jats:italic> and <jats:italic>Saccharomyces cerevisiae<\/jats:italic> co\u2010expressing recombinant reductase and a suitable system for recycling of NADH. <jats:italic>E. coli<\/jats:italic> surpassed <jats:italic>S. cerevisiae<\/jats:italic> sixfold concerning catalytic productivity (3\u2009mmol\/g dry cells\/h) and total turnover number (1.5\u2009mmol substrate\/g dry cells). <jats:italic>o<\/jats:italic>\u2010Chloroacetophenone was unexpectedly \u201ctoxic,\u201d and catalyst half\u2010life times of only 20\u2009min (<jats:italic>E. coli<\/jats:italic>) and 30\u2009min (<jats:italic>S. cerevisiae<\/jats:italic>) in the presence of 100\u2009mM substrate restricted the time of batch processing to maximally \u223c5\u2009h. Systematic reaction optimization was used to enhance the product yield (\u226460%) of <jats:italic>E. coli<\/jats:italic> catalyzed conversion of 100\u2009mM <jats:italic>o<\/jats:italic>\u2010chloroacetophenone which was clearly limited by catalyst instability. Supplementation of external NAD<jats:sup>+<\/jats:sup> (0.5\u2009mM) to cells permeabilized with polymyxin B sulfate (0.14\u2009mM) resulted in complete conversion providing 98\u2009mM <jats:italic>S<\/jats:italic>\u20101\u2010(<jats:italic>o<\/jats:italic>\u2010chlorophenyl)\u2010ethanol. The strategies considered for optimization of reduction rate should be generally useful, however, especially under process conditions that promote fast loss of catalyst activity. Biotechnol. Bioeng. 2011; 108:797\u2013803. \u00a9 2010 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/bit.23002","type":"journal-article","created":{"date-parts":[[2010,11,12]],"date-time":"2010-11-12T10:04:28Z","timestamp":1289556268000},"page":"797-803","source":"Crossref","is-referenced-by-count":22,"title":["Enzyme identification and development of a whole\u2010cell biotransformation for asymmetric reduction of 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