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dc.contributor.authorWang, Shi-Zhen
dc.contributor.author王世珍
dc.contributor.authorWu, Jian-Ping
dc.contributor.authorXu, Gang
dc.contributor.authorYang, Li-Rong
dc.date.accessioned2013-03-21T08:36:15Z
dc.date.available2013-03-21T08:36:15Z
dc.date.issued2012-06-15
dc.identifier.citationBIOCHEMICAL ENGINEERING JOURNAL,2012,65:57-62zh_CN
dc.identifier.issn1369-703X
dc.identifier.urihttp://dx.doi.org/10.1016/j.bej.2012.04.005
dc.identifier.uriWOS:000305300400009
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/15258
dc.description.abstractThe kinetics and thermodynamics of Candida antarctica lipase B-catalyzed remote asymmetric alcoholysis of the citalopram intermediate 3-[(acetyloxy)methyl]-4-[4-(dimethylamino)-1-(4-fluorophenyl)-1-hydroxybutyl]-benzonitrile (diol monoacetate) have been studied. A kinetic model based on the reversible ping-pong bi-bi mechanism with competitive enantiomer substrates was proposed. The product inhibition by each diol enantiomer and the substrate inhibition by isobutyl alcohol were also considered. The diffusion limitation was proven to be negligible. By reducing the degree of freedom in parameter estimation by model discrimination and Haldane equations, 14 free parameters were successfully identified. The model parameters were simulated by the Matlab program using time-concentration curves of different diol monoacetate concentrations; the simulated values fit the experimental values well, with an average relative error of 9.6%. The reaction activity and enantioselectivity of C. antarctica lipase B toward the tertiary alcohol were investigated by kinetic and thermodynamic analysis using simulated kinetic parameters. (c) 2012 Elsevier B.V. All rights reserved.zh_CN
dc.description.sponsorshipNational Natural Science Foundation of China [20936002]; Key Project of Chinese National Programs for Fundamental Research and Development [2011CB710800]; Hi-Tech Research and Development Program of China [2011AA02A209]zh_CN
dc.language.isoenzh_CN
dc.publisherELSEVIER SCIENCE SAzh_CN
dc.subjectDynamic modelingzh_CN
dc.subjectKinetic parameterszh_CN
dc.subjectLipasezh_CN
dc.subjectImmobilized enzymeszh_CN
dc.subjectTertiary alcoholzh_CN
dc.subjectAsymmetric alcoholysiszh_CN
dc.titleA kinetic and thermodynamic study of the lipase-catalyzed remote resolution of a chiral tertiary alcoholzh_CN
dc.typeArticlezh_CN


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