Please use this identifier to cite or link to this item:
Author(s): Ana P. M. Tavares
Oscar Rodriguez
Eugénia A. Macedo
Title: Peroxidase biocatalysis in water-soluble ionic liquids: activity, kinetic and thermal stability
Issue Date: 2012
Abstract: The activity and stability of commercial peroxidase was investigated in the presence of five 1-alkyl-3-methylimidazolium-based ionic liquids (ILs) with either bromide or chloride anions: [C(x)mim][X]. The peroxidase activity and stability were better for the shorter alkyl chain lengths of the ILs and peroxidase was more stable in the presence of the bromide anion, rather than chloride. The thermal inactivation profile was studied from 45 to 60 degrees C in [C(4)mim][Cl] and [C(4)mim][Br]. The activation energy was also determined. Kinetic analysis of the enzyme in the presence of the [C(4)mim][Br] or control (buffer solution) showed that the K-M value increased 5-fold and Vm decreased 13-fold in the presence of the IL. The increase in K-M indicates that this IL can reduce the binding affinity between substrate and enzyme.
Subject: Ciências Tecnológicas, Ciências da engenharia e tecnologias
Technological sciences, Engineering and technology
Scientific areas: Ciências da engenharia e tecnologias
Engineering and technology
Related Information: info:eu-repo/grantAgreement/FCT - Fundação para a Ciência e Tecnologia/Programa de Financiamento Plurianual de Unidades de I&D/PEst-C/EQB/LA0020/2011/Projeto Estratégico-LA 20 - 2011-2012/LA 20
Document Type: Artigo em Revista Científica Internacional
Rights: restrictedAccess
Appears in Collections:FEUP - Artigo em Revista Científica Internacional

Files in This Item:
File Description SizeFormat 
  Restricted Access
707.29 kBAdobe PDF    Request a copy from the Author(s)

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.