Zusammenfassung
The activity of the enzyme horse radish peroxidase (HRP) is studied in a series of reverse microemulsions composed of dodecane, aq. buffer, sodium dodecylsulfate (SDS) and alcs. of the homologous series 1-butanol to 1-octanol. The HRP catalyzed reaction is the oxidn. of a classical water sol. substrate, the 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) by hydrogen ...
Zusammenfassung
The activity of the enzyme horse radish peroxidase (HRP) is studied in a series of reverse microemulsions composed of dodecane, aq. buffer, sodium dodecylsulfate (SDS) and alcs. of the homologous series 1-butanol to 1-octanol. The HRP catalyzed reaction is the oxidn. of a classical water sol. substrate, the 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) by hydrogen peroxide. In parallel elec. cond. measurements are performed on the same solns. The structural changes in the microemulsions, as inferred by the cond. measurements, correlate remarkably well with the changes in the enzymic activities. In particular it is found that (a) the max. activity of the enzyme is always related to its optimum hydration and that this hydration can be related to the microemulsion structures, (b) the enzyme inhibition caused by the alcs. in microemulsions is a consequence of both the soly. of the alcs. in the buffer and the rigidity of the interfacial film. Consequently, it can be concluded that enzymic activity measurements are a valuable tool to study confined systems such as microemulsions and, in particular, the amt. of available hydration water. Enzymic activities can be finely tuned by small changes in microemulsion structures, probably in a predictive way.
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