Studies of laccase from Trametes versicolor in aqueous solutions of several methylimidazolium ionic liquids

• Type: Article in International Scientific Journal
• Date: 2011

Authors

Alberto Domínguez (Author) FEUP; Oscar Rodríguez (Author) FEUP; Ana Paula M. Tavares (Author) FEUP; Eugénia A. Macedo (Author) FEUP; Mª Asunción Longo (Author) Other; Mª Ángeles Sanromán (Author) Other

Journal

Title: Bioresource Technology

Vol. 102 No. 16

Pages: 7494-7499

ISSN: 0960-8524

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 21 Citations

ISI Web of Science

Scopus - 29 Citations

Scientific classification

FOS: Engineering and technology

CORDIS: Technological sciences

Associated Projects

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

E-27/09 - Ionic Liquids as Solvents for Enzymatic Catalysis, Acção Integrada Luso-Espanhola

Other information

Authenticus ID: P-002-PBE

DOI: 10.1016/j.biortech.2011.05.063

Abstract (EN): Stability and kinetic behavior of laccase from Trametes versicolor in the presence of several ionic liquids from the methylimidazolium family have been investigated. In general laccase stability diminished as the size of the alkylic substitute in the methylimidazolium ring increased. Higher concentrations of ionic liquids caused more destabilization than lower ones. Thus, low concentrations of [C(2)mim(+)][EtSO(4)(-)] allowed maintaining enzymatic stability. [C(4)mim(+)][Cl(-)] appeared to have a stabilizing effect on laccase, as little activity decay was observed within three weeks. Kinetic studies indicated that both [C(2)mim(+)][EtSO(4)(-)] and [C(4)mim(+)][Cl(-)] inhibited laccase activity, although 10-fold more [C(2)mim(+)][EtSO(4)(-)] than [C(4)mim(+)][Cl(-)] was required to cause the same degree of inhibition. A kinetic model was developed to represent the experimental data.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6