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Journal of Colloid and Interface Science
Vol. 516, 2018, Pages: 466-475

Enzyme activity of horseradish peroxidase in surfactant-free microemulsions

Sebastian Krickl, Didier Touraud, Pierre Bauduin, Thomas Zinn, Werner Kunz

Institute of Physical and Theoretical Chemistry, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany.

Abstract

In the present contribution, we investigated the influence of the structuring of surfactant-free microemulsions (SFME) (water/1-propanol/limonene and water/tert-butanol/limonene) on the enzyme activity of horseradish peroxidase (HRP). To this purpose, the oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) with hydrogen peroxide was chosen as a model reaction. Enzymatic activities in SFMEs of varying compositions were investigated by UV–Vis spectroscopy and compared to the enzyme activity in pure buffer solution. Dynamic light, small-angle-X-ray scattering and conductivity measurements were performed in order to obtain structural information on the used SFMEs.

Findings presented in this study revealed that the ability of short-chain alcohols to form mesostructures (aqueous aggregates in oil) has a crucial effect on the enzyme activity in SFMEs. Mesoscale structuring with 1-propanol (NPA) was found to be more pronounced than for the more hydrophobic tert-butanol (TBA). It was concluded that the most pronounced mesoscale-structured SFMEs lead to the highest enzymatic activities.

Graphical abstract

Keywords: Microemulsion, Enzyme, Activity, Surfactant-free, Surfactantless, Detergentless, Horseradish peroxidase, ABTSHRP, Mesoscale structuring.

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