Study On The Interaction Between Alkyl Polyglucoside And Protein

Proteins/surfactants mixtures not only have wide applications in cosmetic, pharmaceutics, and food products, etc. but also can simulate biological systems, which expedites the penetration of biological technology into medicine and chemical industry field. So, the interest in interaction between protein and surfactant is very high for many years.To our knowledge, the interaction between protein and surfactant is mainly focus on the traditional surfactant such as SDS, Triton X-100, and CTAB, less attention has been paid to protein/APG surfactant. Alkyl Polyglycoside(APG) is a new non-ionic surfactant. APG is surface tension low, foam stability abound fine and smooth, decontamination choiceness, best compatibility performance. Moreover, APG of characteristic is blond to eyes and skin, fine consistent, innocuity, bio-degradation choiceness. APG is applied in many fields, such as food, medicine, detergent, cosmetics, pesticides and plastic. In this thesis, The interactions between Alkyl Polyglycoside(N-Octyl-β-D-glucopyranoside (OGP), Decyl-β-D-glucopyranoside(C10G),N-Dodecyl-β-D-glucopyranoside(C12G)) and protein have been investigated by fluorescence, ultraviolet spectroscopy and surface tension measurements.The surface tension curve of the surfactant solution can be modified by the addition of BSA, From the surface tension curve of the surfactant solution and surfactant /protein solution, we can see that the critical micelle concentration of surfactant in surfactant /protein solution is bigger than in surfactant solution. This is because that the concentration of surfactant monomer is decreased by the binding of surfactant molecules on the surface of protein. It was found that the presence of protein delays the surfactant aggregation by using the pyrene 1:3 ratio method. The reason is same with that of the surface tension change. The fluorescence intensity and ultraviolet absorption intensity of protein gradually decrease upon increasing the concentration of surfactant, and a blue shift of the max flurescence emission wavelength of protein was observed, this indicated that surfactant mainly interacts with Trp residues compared to Tyr residues. The results from synchronous fluorescence spectrum and I- quenching experiments also indicated that surfactant mainly interacts with Trp residues of hydrophobic loop. At the same time, we find that the binding of C10G is more effectively than C12G, and the OGP shows the least interaction with protein.