Browsing by Author "Maikokera, Raymond"

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    Surface Activity Interactions in Aqueous Solution of Anionic Surfactants with a Water Treatment Protein from Moringa oleifera Seeds
    (Scientific Research Publishing, 2015-02-11) Kwaambwa, Habauka M.; Maikokera, Raymond; Nermark, Fiona M.
    The interaction of anionic surfactants sodium dodecylbenzenesulphonate (SDBS) and sodium bis (2-ethyl-1-hexylsulfosuccinate) (AOT) with the water treatment protein extracted from Moringa oleifera seeds has been investigated by surface tension measurements. The results were compared with previously reported studies using surface tension and zeta potential measurements of the same protein with an anionic surfactant sodium dodecylsulphate. There is a strong electrostatic interaction between the protein and the surfactants characterized by a local maximum at intermediate surfactant concentration. This surfactant concentration depends on the protein concentration and corresponds to the surfactant concentration at the point of charge reversal (zeta potential = 0 mV). The number of surfactant molecules required to neutralize the positive charges on the protein was found to be 8 per protein molecule.
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    Surface Activity Interactions in Aqueous Solution of Anionic Surfactants with a Water Treatment Protein from Moringa oleifera Seeds
    (Scientific Research Publishing, 2015) Kwaambwa, Habauka M.; Maikokera, Raymond; Nermark, Fiona M.
    The interaction of anionic surfactants sodium dodecylbenzenesulphonate (SDBS) and sodium bis (2-ethyl-1-hexylsulfosuccinate) (AOT) with the water treatment protein extracted from Moringa oleifera seeds has been investigated by surface tension measurements. The results were compared with previously reported studies using surface tension and zeta potential measurements of the same protein with an anionic surfactant sodium dodecylsulphate. There is a strong electrostatic interaction between the protein and the surfactants characterized by a local maximum at intermediate surfactant concentration. This surfactant concentration depends on the protein concentration and corresponds to the surfactant concentration at the point of charge reversal (zeta potential = 0 mV). The number of surfactant molecules required to neutralize the positive charges on the protein was found to be 8 per protein molecule.