{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T19:05:48Z","timestamp":1791918348000,"version":"4.3.4"},"reference-count":40,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2008,9,5]],"date-time":"2008-09-05T00:00:00Z","timestamp":1220572800000},"content-version":"vor","delay-in-days":978,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotechnology Progress"],"published-print":{"date-parts":[[2006,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A method is proposed for identification of kinetic parameters when diffusion of substrates is limiting in reactions catalyzed by immobilized enzymes. This method overcomes conventional sequential procedures, which assume immobilization does not affect the conformation of the enzyme and, thus, consider intrinsic and inherent kinetics to be the same. The coupled equations describing intraparticle mass transport are solved simultaneously using numerical methods and are used for direct estimation of kinetic parameters by fitting modeling results to time\u2010course measurements in a stirred tank reactor. While most traditional procedures were based on Michaelis\u2010Menten kinetics, the method presented here is applicable to more complex kinetic mechanisms involving multiple state variables, such as ping\u2010pong bi\u2010bi. The method is applied to the kinetic resolution of (<jats:italic>R<\/jats:italic>\/<jats:italic>S<\/jats:italic>)\u20101\u2010methoxy\u20102\u2010propanol with vinyl acetate catalyzed by <jats:italic>Candida antarctica<\/jats:italic> lipase B. A mathematical model is developed consisting of irreversible ping\u2010pong bi\u2010bi kinetics, including competitive inhibition of both enantiomers. The kinetic model, which fits to experimental data over a wide range of both substrates (5\u201395%) and temperatures (5\u201356 \u00b0C), is used for simulations to study typical behavior of immobilized enzyme systems.<\/jats:p>","DOI":"10.1021\/bp060062e","type":"journal-article","created":{"date-parts":[[2006,8,10]],"date-time":"2006-08-10T07:00:51Z","timestamp":1155193251000},"page":"1305-1312","source":"Crossref","is-referenced-by-count":43,"title":["Investigations of Reaction Kinetics for Immobilized Enzymes\u2014Identification of Parameters in the Presence of Diffusion Limitation"],"prefix":"10.1002","volume":"22","author":[{"given":"Wouter R.","family":"Berendsen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexei","family":"Lapin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Reuss","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,9,5]]},"reference":[{"key":"e_1_2_9_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/BA20020017"},{"key":"e_1_2_9_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.enzmictec.2003.07.001"},{"key":"e_1_2_9_4_2","doi-asserted-by":"publisher","DOI":"10.1385\/ABAB:91-93:1-9:739"},{"key":"e_1_2_9_5_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-4660(199603)65:3<239::AID-JCTB433>3.0.CO;2-H"},{"key":"e_1_2_9_6_2","doi-asserted-by":"publisher","DOI":"10.1042\/BA20030180"},{"key":"e_1_2_9_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(90)80537-S"},{"key":"e_1_2_9_8_2","volume-title":"Biochemical Engineering Fundamentals","author":"Bailey J. 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