Enhanced laccase stability through mediator partitioning into hydrophobic ionic liquids
2014
Rehmann, Lars | Ivanova, Ekaterina | Gunaratne, H. Q Nimal | Seddon, Kenneth R. | Stephens, Gill
Laccase-mediator systems have numerous potential uses for green oxidations, but their practical use may be limited because the reactive, oxidised mediators deactivate the enzyme. TEMPO, 4-hydroxybenzyl alcohol, phenothiazine and 2-hydroxybiphenyl caused almost complete deactivation of laccase from Trametes versicolor within 24–140 h. By contrast, 18% activity was retained after 188 h in controls without mediator, and 15% in the presence of ABTS. 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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