Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/348862
Type: Artigo
Title: Extending the kinetic solution of the classic Michaelis–Menten model of enzyme action
Author: Conceicao Bispo, Jose Ailton
Sampaio Bonafe, Carlos Francisco
de Souza, Volnei Brito
de Almeida e Silva, Joao Batista
Mafra de Carvalho, Giovani Brandao
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
Subject: Peroxidase
Country: Países Baixos
Editor: Springer
Rights: Fechado
Identifier DOI: 10.1007/s10910-011-9869-5
Address: https://link.springer.com/article/10.1007%2Fs10910-011-9869-5
Date Issue: 2011
Appears in Collections:IB - Artigos e Outros Documentos

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