Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/108723
Type: Artigo de periódico
Title: Extending The Kinetic Solution Of The Classic Michaelis-menten Model Of Enzyme Action
Author: Bispo J.A.C.
Bonafe C.F.S.
de Souza V.B.
de Almeida e Silva J.B.
de Carvalho G.B.M.
Abstract: The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quantitative information on enzyme-catalyzed reactions under distinct conditions. The classic Michaelis-Menten model (Biochem Zeit 49:333, 1913) for enzyme kinetic has been widely used to determine important parameters involved in enzyme catalysis, particularly the Michaelis-Menten constant (K M) and the maximum velocity of reaction (V max). Subsequently, a detailed treatment of the mechanisms of enzyme catalysis was undertaken by Briggs-Haldane (Biochem J 19:338, 1925). These authors proposed the steady-state treatment, since its applicability was constrained to this condition. The present work describes an extending solution of the Michaelis-Menten model without the need for such a steady-state restriction. We provide the first analysis of all of the individual reaction constants calculated analytically. Using this approach, it is possible to accurately predict the results under new experimental conditions and to characterize and optimize industrial processes in the fields of chemical and food engineering, pharmaceuticals and biotechnology. © 2011 Springer Science+Business Media, LLC.
Editor: 
Rights: fechado
Identifier DOI: 10.1007/s10910-011-9869-5
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-80052259534&partnerID=40&md5=65fdad7c8a578b1257ffdde86437c0e0
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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