Please use this identifier to cite or link to this item: http://dspace.unimap.edu.my:80/xmlui/handle/123456789/3386
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dc.contributor.authorXiu, Guo-Hua-
dc.contributor.authorJiang, Lei-
dc.contributor.authorLi, Ping-
dc.date.accessioned2008-12-01T05:11:26Z-
dc.date.available2008-12-01T05:11:26Z-
dc.date.issued2001-07-
dc.identifier.citationBiotechnology and Bioengineering, vol. 74, issue 1, 2001, pages 29-39en_US
dc.identifier.issn0006-3592-
dc.identifier.urihttp://dspace.unimap.edu.my/123456789/3386-
dc.description.abstractA mathematical model has been developed for immobilized enzyme-catalyzed kinetic resolution of racemate in a fixed-bed reactor in which the enzyme-catalyzed reaction (the irreversible uni-uni competitive Michaelis-Menten kinetics is chosen as an example) was coupled with intraparticle diffusion, external mass transfer, and axial dispersion. The effects of mass-transfer limitations, competitive inhibition of substrates, deactivation on the enzyme effective enantioselectivity, and the optical purity and yield of the desired product are examined quantitatively over a wide range of parameters using the orthogonal collocation method. For a first-order reaction, an analytical solution is derived from the mathematical model for slab-, cylindrical-, and spherical-enzyme supports. Based on the analytical solution for the steady-state resolution process, a new concise formulation is presented to predict quantitatively the masstransfer limitations on enzyme effective enantioselectivity and optical purity and yield of the desired product for a continuous steady-state kinetic resolution process in a fixed-bed reactor.en_US
dc.language.isoenen_US
dc.publisherJohn Wiley & Sons, Inc.en_US
dc.subjectImmobilized enzymes.en_US
dc.subjectMass transfer.en_US
dc.titleMass-transfer limitations for immobilized enzyme-catalyzed kinetic resolution of racemate in a fixed-bed reactoren_US
dc.typeArticleen_US
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