The interaction of hen egg-white lysozyme with sodium n-dodecyl sulfate (SDS) as an anionic surfactant was investigated by UV-vis spectrophotometry at different pHs at 25 degrees C using HCl/glycine and NaOH/glycine for acidic and basic pH ranges, respectively. Analysis of the spectral data using chemometric method gave the evidence for the existence of intermediate components during the cited interaction. Results also indicated a connection between turbidity of the protein solution upon interaction with SDS and distribution of our newly found intermediates. As intermediates are important in aggregation of proteins, beta-cyclodextrin was employed as an anti-aggregation agent and the results obtained for the lysozyme-SDS-beta-cyclodextrin ternary system were compared with those obtained in the absence of beta-cyclodextrin on distribution and mole fraction of intermediates with. It is also shown that as the distribution of intermediates broadens in a range of SDS concentrations, the turbidity and aggregation state of solution are reduced.
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