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The production of chiral alcohols from ketones can be carried out stereo selectively with alcohol dehydrogenases (ADHs). To establish a process for cost\u2010effective enzyme immobilization on solid phase for application in ketone reduction, we used an established enzyme pair consisting of ADH from <jats:italic>Rhodococcus erythropolis<\/jats:italic> and formate dehydrogenase (FDH) from <jats:italic>Candida boidinii<\/jats:italic> for NADH cofactor regeneration and co\u2010immobilized them on modified poly\u2010p\u2010hydroxybutyrate synthase (PhaC)\u2010inclusion bodies that were recombinantly produced in <jats:italic>Escherichia coli<\/jats:italic> cells. After separate production of genetically engineered and recombinantly produced enzymes and particles, cell lysates were combined and enzymes endowed with a Kcoil were captured on the surface of the Ecoil presenting particles due to coiled\u2010coil interaction. Enzyme\u2010loaded particles could be easily purified by centrifugation. Total conversion of 4'\u2010chloroacetophenone to (<jats:italic>S<\/jats:italic>)\u20104\u2010chloro\u2010\u03b1\u2010methylbenzyl alcohol could be accomplished using enzyme\u2010loaded particles, catalytic amounts of NAD<jats:sup>+<\/jats:sup> and formate as substrates for FDH. Chiral GC\u2010MS analysis revealed that immobilized ADH retained enantioselectivity with 99 % enantiomeric excess. In conclusion, this strategy may become a cost\u2010effective alternative to coupled reactions using purified enzymes.<\/jats:p>","DOI":"10.1002\/biot.201500495","type":"journal-article","created":{"date-parts":[[2016,2,22]],"date-time":"2016-02-22T10:48:56Z","timestamp":1456138136000},"page":"890-898","source":"Crossref","is-referenced-by-count":10,"title":["Coupled reactions on bioparticles: Stereoselective reduction with cofactor regeneration on PhaC inclusion bodies"],"prefix":"10.1002","volume":"11","author":[{"given":"Valerie","family":"Spieler","sequence":"first","affiliation":[{"name":"Institute for Organic Chemistry and Biochemistry, Technische Universit\u00e4t Darmstadt  Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernhard","family":"Valldorf","sequence":"additional","affiliation":[{"name":"Institute for Organic Chemistry and Biochemistry, Technische Universit\u00e4t Darmstadt  Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Franziska","family":"Maa\u00df","sequence":"additional","affiliation":[{"name":"Institute for Organic Chemistry and Biochemistry, Technische Universit\u00e4t Darmstadt  Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Kleinschek","sequence":"additional","affiliation":[{"name":"Chemistry and Biotechnology, Hochschule Darmstadt  Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan H.","family":"H\u00fcttenhain","sequence":"additional","affiliation":[{"name":"Chemistry and Biotechnology, Hochschule Darmstadt  Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harald","family":"Kolmar","sequence":"additional","affiliation":[{"name":"Institute for Organic Chemistry and Biochemistry, Technische Universit\u00e4t Darmstadt  Darmstadt Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,3,10]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/adsc.200700082"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1039\/c3cs35506c"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/bit.25136"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.35.070166.004301"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/9783527618262.ch6"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.00612-10"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi9530604"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.57.030502.091022"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1002\/anie.200301664"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-62703-550-7_2"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/btpr.606"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbiotec.2014.10.039"},{"key":"e_1_2_7_14_1","first-page":"380","article-title":"Cloning, sequence analysis, and heterologous expression of the gene encoding a (S)\u2010specific alcohol dehydrogenase from Rhodococcus erythropolis DSM 43297","volume":"62","author":"Abokitse K.","year":"2003","journal-title":"Appl. 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