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• W2047407002 abstract "The NADH-oxidase (NOX) from Lactococcus lactis was isolated from extracts of aerobically grown cells. It was purified by (NH4)2SO4 fractionation followed by ion exchange and affinity chromatographic steps. Spectra of the oxidized enzyme showed peaks with maxima at wavelengths of 274, 381 and 446 nm and FAD was identified as cofactor. The enzyme is apparently a dimer composed of two identical subunits of 53 kDa, each containing one molecule of non-covalently bound FAD. NOX showed optimum activity between pH 6.0 and 9.0 and was found to have a pI of 4.8. The lactococcal NOX uses dioxygen as the natural electron acceptor and forms water during the oxidation of NADH. The natural electron donor was β-NADH (Km=4.1 μm and Vmax=83.2 μmol min−1 mg−1) whereas α-NADH, α-NADPH or β-NADPH were not oxidized by the enzyme. Hydrogen peroxide, sulfhydryl reagents and quinine inactivated the enzyme activity. The oxidase described in this paper appears to possess kinetic characteristics potentially useful to redirect, in a food-grade manner, the carbon flux of lactococci." @default.
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• W2047407002 date "2001-01-01" @default.
• W2047407002 modified "2023-09-25" @default.
• W2047407002 title "Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis" @default.
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• W2047407002 doi "https://doi.org/10.1016/s0958-6946(01)00031-0" @default.
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