{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T08:37:58Z","timestamp":1774600678235,"version":"3.50.1"},"reference-count":19,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2006,8,25]],"date-time":"2006-08-25T00:00:00Z","timestamp":1156464000000},"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; Bioengineering"],"published-print":{"date-parts":[[2006,12,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Lipase\u2010catalyzed kinetic resolution of racemates is a popular method for synthesis of chiral synthons. Most of these resolutions are reversible equilibrium limited reactions. For the first time, an extensive kinetic model is proposed for kinetic resolution reactions, which takes into account the full reversibility of the reaction, substrate inhibition by an acyl donor and an acyl acceptor as well as alternative substrate inhibition by each enantiomer. For this purpose, the reversible enantioselective transesterification of (R\/S)\u20101\u2010methoxy\u20102\u2010propanol with ethyl acetate catalyzed by <jats:italic>Candida antarctica<\/jats:italic> lipase B (CAL\u2010B) is investigated. The detailed model presented here is valid for a wide range of substrate and product concentrations. Following model discrimination and the application of Haldane equations to reduce the degree of freedom in parameter estimation, the 11 free parameters are successfully identified. All parameters are fitted to the complete data set simultaneously. Six types of independent initial rate studies provide a solid data basis for the model. The effect of changes in substrate and product concentration on reaction kinetics is discussed. The developed model is used for simulations to study the behavior of reaction kinetics in a fixed bed reactor. The typical plot of enantiomeric excess versus conversion of substrate and product is evaluated at various initial substrate mixtures. The model is validated by comparison with experimental results obtained with a fixed bed reactor, which is part of a fully automated state\u2010of\u2010the\u2010art miniplant. \u00a9 2006 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/bit.21034","type":"journal-article","created":{"date-parts":[[2006,8,25]],"date-time":"2006-08-25T22:46:31Z","timestamp":1156545991000},"page":"883-892","source":"Crossref","is-referenced-by-count":19,"title":["A kinetic study of lipase\u2010catalyzed reversible kinetic resolution involving verification at miniplant\u2010scale"],"prefix":"10.1002","volume":"95","author":[{"given":"W.R.","family":"Berendsen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Gendrot","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Freund","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Reuss","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,8,25]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.3109\/10242429809003198"},{"key":"e_1_2_1_3_1","volume-title":"Biochemical engineering fundamentals","author":"Bailey JE","year":"1986"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0957-4166(00)00465-1"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbiotec.2005.07.006"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bp060062e"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.memsci.2006.02.029"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0290(19990705)64:1<120::AID-BIT13>3.0.CO;2-A"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1002\/bit.10260"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.3109\/10242429308992098"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.46.070177.001555"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/bit.10580"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4838(95)00096-D"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1381-1177(99)00058-2"},{"key":"e_1_2_1_15_1","unstructured":"ResnickSM DonateFA FrankTC FoleyP.2003. Enzymatic resolution of propylene glycol alkyl (or aryl) ethers and ether acetates. World patent WO 03 083 126 A2."},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/0141-0229(92)90110-A"},{"key":"e_1_2_1_17_1","unstructured":"RotticciD.2000.Understanding and engineering the enantioselectivity ofCandida antarcticalipase B towards sec\u2010alcohols. Ph.D.\u2010Thesis. Stockholm. 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