Peroxidase biocatalysis in water-soluble ionic liquids: activity, kinetic and thermal stability

• Tipo: Artigo em Revista Científica Internacional
• Data: 2012

Autores

Ana P. M. Tavares (Autor) FEUP; Oscar Rodriguez (Autor) FEUP; Eugénia A. Macedo (Autor) FEUP

Revista

Título: Biocatalysis and Biotransformation

Vol. 30 Nº 4

Páginas: 417-425

ISSN: 1024-2422

Editora: Taylor & Francis

Indexação

ISI Web of Knowledge - 0 Citações

ISI Web of Science

Scopus - 4 Citações

Classificação Científica

FOS: Ciências da engenharia e tecnologias

CORDIS: Ciências Tecnológicas

Projetos Associados

LA 20 - Projeto Estratégico-LA 20 - 2011-2012

Outras Informações

ID Authenticus: P-002-74E

DOI: 10.3109/10242422.2012.715636

Abstract (EN): 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 9