Abstract
Thermal deactivation kinetics of horseradish peroxidase (HRP) were studied from 45 to 90 °C in phosphate buffer and 5–25% (v,w/v) 1-butyl-3-methylimidazolium tetrafluoroborate [BMIM][BF4] and 1-butyl-3-methylimidazolium chloride [BMIM][Cl]. HRP activity at 25 °C was not affected by the presence of ionic liquids up to 20% (v,w/v). Increasing the ionic liquids concentration up to 25% (v,w/v) changed the biphasic character of deactivation kinetics to an apparent single first-order step. The presence of 5–10% (v/v) [BMIM][BF4] significantly improved HRP thermal stability with lower activation energies for the deactivation second phase (83–87 kJ mol−1). After deactivation, enhanced activity regain of the enzyme, up to 70–80% of the initial activity, was found in 25% (v/v) [BMIM][BF4] and 10% (w/v) [BMIM][Cl] and correlated to prevalence of the deactivation first phase.
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Machado, M.F., Saraiva, J.M. Thermal Stability and Activity Regain of Horseradish Peroxidase in Aqueous Mixtures of Imidazolium-Based Ionic Liquids. Biotechnol Lett 27, 1233–1239 (2005). https://doi.org/10.1007/s10529-005-0023-y
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DOI: https://doi.org/10.1007/s10529-005-0023-y