Interfacial properties and fluorescence of a coagulating protein extracted from Moringa oleifera seeds and its interaction with sodium dodecyl sulphate.

The surfactant behaviour of aqueous coagulating protein extracted from Moringa oleifera seeds has been investigated by surface tension measurements. The interaction of the coagulant protein with an anionic surfactant sodium dodecyl sulphate (SDS) has been monitored by surface tension and intrinsic protein fluorescence measurements. The extracted protein shows some weak surface activity at low concentrations. To achieve maximum surface activity (i.e. maximum reduction in surface tension of water), substantially higher concentrations of protein are required. The coagulant protein-SDS interaction scheme did not exhibit the behaviour of weakly interacting polymer-surfactant systems and the SDS interacts in a monomeric form with the protein. The association process of SDS with the coagulant protein is supported by protein fluorescence measurements. SDS has an effect on the fluorescence of the coagulant protein indicating that the local environment of tryptophan in the protein changes as SDS concentration below its critical micelle concentration is increased. These results have led us to the conclusions that: (1) the protein extracted from M. oleifera seeds has significant surfactant behaviour; (2) the coagulant protein interacts strongly with SDS and the protein might have specific binding sites for SDS; (3) there is formation of protein-SDS complex.