Assays of Enzyme Activity

Most PQQ- and FAD-dependent dehydrogenases can be assayed using artificial electron acceptors such as potassium ferricyanide or phenazine methosulfate (PMS) [3]. In the case of potassium ferricyanide, enzyme activity can be assayed over a broad pH range, from highly acidic to highly alkaline conditions. On the other hand, enzyme activity measurement with PMS combined with dichlorophe-nol indophenol (DCIP) is invalid at acidic pH below 6 due to non-enzymatic decolorization of the electron acceptor used. Thus, the assay with PMS-DCIP is valid in the neutral to alkaline regions.

It is also worth noting that when enzymes containing a heme c component in the enzyme molecule or membrane fraction are used, the enzyme activities can be easily assayed with potassium ferricyanide. However, enzyme activity measurement with PMS-DCIP is invalid if the enzymes do not contain the heme c component after solubilization from the membrane.

6 | 1 Biooxidation with PQQ- and FAD-Dependent Dehydrogenases 1.3

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