Abstract
Partitioning mediators into water-immiscible ionic liquids protects laccase from inactivation.
Highlights
Laccases (EC 1.10.3.2) catalyse cofactor-independent, one-electron oxidation of a wide range of substrates using dioxygen as the electron acceptor
In the presence of [C6mim][AOT], laccase retained 54, 35, 35 and 41% activity after 188 h in the presence of 4-hydroxybenzyl alcohol, phenothiazine and 2-hydroxybiphenyl and ABTS, respectively, whilst 30% activity was retained in the presence of [N1 8 8 8][Sac] and TEMPO
Control vials with the same mediator concentrations, but without ionic liquids, were incubated in the same way
Summary
Enhanced laccase stability through mediator partitioning into hydrophobic ionic liquids Lars Rehmann,a,b Ekaterina Ivanova,b H. TEMPO, 4-hydroxybenzyl alcohol, phenothiazine and 2-hydroxybiphenyl caused almost complete deactivation of laccase from Trametes versicolor within 24–140 h. A biphasic reaction system was developed to protect the laccase, by partitioning the mediator into water-immiscible ionic liquids. In the presence of [C6mim][AOT], laccase retained 54, 35, 35 and 41% activity after 188 h in the presence of 4-hydroxybenzyl alcohol, phenothiazine and 2-hydroxybiphenyl and ABTS, respectively, whilst 30% activity was retained in the presence of [N1 8 8 8][Sac] and TEMPO. The protection against deactivation by the mediators correlated strongly with the distribution coefficients of the mediators between ionic liquids and water
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