Stability and kinetic behavior of immobilized laccase from Myceliophthora thermophila in the presence of the ionic liquid 1-ethyl-3-methylimidazolium ethylsulfate

• Type: Article in International Scientific Journal
• Date: 2014

Authors

María Férnandez-Férnandez (Author) Other; Diego Moldes (Author) Other; Alberto Domínguez (Author) Other; M. Ángeles Sanromán (Author) Other; Ana Paula M. Tavares (Author) FEUP; Oscar Rodríguez (Author) FEUP; Eugénia A. Macedo (Author) FEUP

Journal

The Journal is awaiting validation by the Administrative Services.

Title: Biotechnol Progress - Biotechnology Progress

Vol. 30 No. 4

Pages: 790-796

ISSN: 8756-7938

Indexing

ISI Web of Knowledge - 6 Citations

ISI Web of Science

Scopus - 11 Citations

Scientific classification

CORDIS: Technological sciences

FOS: Engineering and technology

Associated Projects

LA 20 - PROJECTO ESTRATÉGICO - LA 20 - 2013-2014

Other information

Authenticus ID: P-009-Q3T

DOI: 10.1002/btpr.1910

Abstract (EN): The use of ionic liquids (ILs) as reaction media for enzymatic reactions has increased their potential because they can improve enzyme activity and stability. Kinetic and stability properties of immobilized commercial laccase from Myceliophthora thermophila in the water-soluble IL 1-ethyl-3-methylimidazolium ethylsulfate ([emim][EtSO4]) have been studied and compared with free laccase. Laccase immobilization was carried out by covalent binding on glyoxyl-agarose beads. The immobilization yield was 100%, and the activity was totally recovered. The Michaelis-Menten model fitted well to the kinetic data of enzymatic oxidation of a model substrate in the presence of the IL [emim][EtSO4]. When concentration of the IL was augmented, the values of V-max for free and immobilized laccases showed an increase and slight decrease, respectively. The laccase-glyoxyl-agarose derivative improved the laccase stability in comparison with the free laccase regarding the enzymatic inactivation in [emim][EtSO4]. The stability of both free and immobilized laccase was slightly affected by small amounts of IL (<50%). A high concentration of the IL (75%) produced a large inactivation of free laccase. However, immobilization prevented deactivation beyond 50%. Free and immobilized laccase showed a first-order thermal inactivation profile between 55 and 70 degrees C in the presence of the IL [emim][EtSO4]. Finally, thermal stability was scarcely affected by the presence of the IL. (C) 2014 American Institute of Chemical Engineers

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7