{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T16:42:42Z","timestamp":1772124162525,"version":"3.50.1"},"reference-count":28,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2013,5,13]],"date-time":"2013-05-13T00:00:00Z","timestamp":1368403200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotechnology Journal"],"published-print":{"date-parts":[[2013,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Generally, recombinant and native microorganisms can be employed as whole\u2010cell catalysts. The application of native hosts, however, shortens the process development time by avoiding multiple steps of strain construction. Herein, we studied the NAD(P)H\u2010dependent reduction of <jats:italic>o<\/jats:italic>\u2010chloroacetophenone by isolated xylose reductases and their native hosts <jats:italic>Candida tenuis<\/jats:italic> and <jats:italic>Pichia stipitis.<\/jats:italic> The natural hosts were benchmarked against <jats:italic>Escherichia coli<\/jats:italic> strains co\u2010expressing xylose reductase and a dehydrogenase for co\u2010enzyme recycling. Xylose\u2010grown cells of <jats:italic>C. tenuis<\/jats:italic> and <jats:italic>P. stipitis<\/jats:italic> displayed specific <jats:italic>o<\/jats:italic>\u2010chloroacetophenone reductase activities of 366 and 90 U g<jats:sub>CDW<\/jats:sub><jats:sup>\u20131<\/jats:sup>, respectively, in the cell\u2010free extracts. Fresh biomass was employed in batch reductions of 100 mM <jats:italic>o<\/jats:italic>\u2010chloroacetophenone using glucose as co\u2010substrate. Reaction stops at a product concentration of about 15 mM, which suggests sensitivity of the catalyst towards the formed product. In situ substrate supply and product removal by the addition of 40% hexane increased catalyst stability. Optimisation of the aqueous phase led to a (<jats:italic>S<\/jats:italic>)\u20101\u2010(2\u2010chlorophenyl)ethanol concentration of 71 mM (ee &gt;\u200999.9%) obtained with 44 g<jats:sub>CDW<\/jats:sub> L<jats:sup>\u20131<\/jats:sup> of <jats:italic>C. tenuis.<\/jats:italic> The final difference in productivities between native <jats:italic>C. tenuis<\/jats:italic> and recombinant <jats:italic>E. coli<\/jats:italic> was &lt;\u20091.7\u2010fold. The optically pure product is a required key intermediate in the synthesis of a new class of chemotherapeutic substances (polo\u2010like kinase 1 inhibitors).<\/jats:p>","DOI":"10.1002\/biot.201200322","type":"journal-article","created":{"date-parts":[[2013,4,16]],"date-time":"2013-04-16T04:56:40Z","timestamp":1366088200000},"page":"699-708","source":"Crossref","is-referenced-by-count":10,"title":["Harnessing <i>Candida tenuis<\/i> and <i>Pichia stipitis<\/i> in whole\u2010cell bioreductions of <i>o<\/i>\u2010chloroacetophenone: Stereoselectivity, cell activity, in situ substrate supply and product removal"],"prefix":"10.1002","volume":"8","author":[{"given":"Christoph","family":"Gruber","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stefan","family":"Krahulec","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bernd","family":"Nidetzky","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Regina","family":"Kratzer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2013,5,13]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.21980"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbpa.2007.01.685"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00253-003-1347-y"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00253-007-1005-x"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.fbp.2010.01.003"},{"key":"e_1_2_7_7_2","first-page":"4","article-title":"Biopharmaceutical processes: A glance into the 21st Century.","author":"Anicetti V.","year":"2009","journal-title":"Bioprocess Int."},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.E07-05-0517"},{"key":"e_1_2_7_9_2","doi-asserted-by":"crossref","unstructured":"Sato Y. Onozaki Y. Sugimoto T. Kurihara H. et al. Imidazopyridine derivatives as potent and selective Polo\u2010like kinase (PLK) inhibitors.Bioorg. Med. Chem. Lett.2009 19 4673\u20134678.","DOI":"10.1016\/j.bmcl.2009.06.084"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1186\/1475-2859-11-7"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.20737"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-4347(99)00380-1"},{"key":"e_1_2_7_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.biortech.2012.01.009"},{"key":"e_1_2_7_14_2","doi-asserted-by":"publisher","DOI":"10.1002\/mbo3.5"},{"key":"e_1_2_7_15_2","first-page":"326","article-title":"Nidetzky, B. 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