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

• Tipo: Artigo em Revista Científica Internacional
• Data: 2011

Autores

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

Revista

Título: Bioresource Technology

Vol. 102 Nº 16

Páginas: 7494-7499

ISSN: 0960-8524

Editora: Elsevier

Indexação

ISI Web of Knowledge - 21 Citações

ISI Web of Science

Scopus - 29 Citações

Classificação Científica

FOS: Ciências da engenharia e tecnologias

CORDIS: Ciências Tecnológicas

Projetos Associados

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

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

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6