Kinetic and Stability Study of the Peroxidase Inhibition in Ionic Liquids

• Type: Article in International Scientific Journal
• Date: 2009

Authors

Aristides P. Carneiro (Author) Other; Oscar Rodríguez (Author) FEUP; Fátima L. Mota (Author) FEUP; Ana P. M. Tavares (Author) FEUP; Eugénia A. Macedo (Author) FEUP

Journal

Title: Industrial & Engineering Chemistry Research

Vol. 48

Pages: 10810-10815

ISSN: 0888-5885

Publisher: American Chemical Society

Indexing

ISI Web of Knowledge - 8 Citations

ISI Web of Science

Scopus - 9 Citations

Scientific classification

FOS: Engineering and technology > Other engineering and technologies

Other information

Authenticus ID: P-003-DJV

DOI: 10.1021/ie9007612

Abstract (EN): The activity and stability of peroxidase in aqueous solutions of two ionic liquids (ILs) have been studied. The ILs selected were 1-ethyl-3-methylimidazolium 2-(2-methoxyethoxy) ethylsulfate, [emim][MDEGSO(4)], and 1-ethyl-3-methylimidazolium ethylsulfate, [emim][EtSO4]. Experiments were performed at room temperature using concentrations of ILs between 5 and 50% (v/v) and pH values in the range from 5 to 9. The initial activity of the enzyme in these ILs at optimized conditions (pH 7 and 5-10% IL) was similar or higher than that achieved with buffer solution. Kinetic studies showed that maximum reaction Velocity (V-max) decreased with increasing concentration of IL. The effect of [emim][EtSO4] concentration on the decrease of V-max was higher than that of [emim][MDEGSO(4)]. It was found that [emim][EtSO4] was a more potent inhibitor on peroxidase activity. The peroxidase studied was active in the ILs investigated, and the enzyme exhibited a higher stability in ILs at the optimized conditions. Kinetic studies showed that inhibition was a noncompetitive type in both ILs.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6