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

• Type: Article in International Scientific Journal
• Date: 2012

Authors

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

Journal

Title: Biocatalysis and Biotransformation

Vol. 30 No. 4

Pages: 417-425

ISSN: 1024-2422

Publisher: Taylor & Francis

Indexing

ISI Web of Knowledge - 0 Citations

ISI Web of Science

Scopus - 4 Citations

Scientific classification

FOS: Engineering and technology

CORDIS: Technological sciences

Associated Projects

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

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9