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- W2002946306 abstract "Abstract Alkaline p -nitrophenylphosphate phosphatase ( p NPPase) from the halophilic archaeon Halobacterium salinarum (previously halobium ) was solubilized in reversed micelles of cetyltrimethylammonium bromide (CTAB) in cyclohexane with 1-butanol as cosurfactant. The hydrolysis reaction appears to follow Michaelis–Menten kinetics. The dependency of the maximum reaction rate ( V max ) on the water content θ (% v/v) (or ω 0 value: molar ratio of water to surfactant concentrations) showed a bell-shaped curve for 0.3 M CTAB, but not for 0.2 M CTAB. The enzyme activity increased with the surfactant concentration at a constant ω 0 value (10.27). When the surfactant concentration was increased at a constant θ , the enzyme activity decreased. The enzyme was more stable in reversed micelles than in aqueous media." @default.
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- W2002946306 date "2000-11-01" @default.
- W2002946306 modified "2023-09-24" @default.
- W2002946306 title "Enzymatic activity of an extremely halophilic phosphatase from the Archaea Halobacterium salinarum in reversed micelles" @default.
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- W2002946306 doi "https://doi.org/10.1016/s1381-1177(00)00009-6" @default.
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