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|Title:||Adsorption of single component and binary mixtures of protein and surfactants at the oil-water interface||Authors:||Sudah, O.S.
|Keywords:||Dynamic interfacial tensions
Kinetics of adsorption
Surface waves diffraction
|Issue Date:||May-1999||Citation:||Sudah, O.S., Chen, G., Chiew, Y.C. (1999-05). Adsorption of single component and binary mixtures of protein and surfactants at the oil-water interface. Colloids and Surfaces B: Biointerfaces 13 (4) : 195-202. ScholarBank@NUS Repository. https://doi.org/10.1016/S0927-7765(99)00011-9||Abstract:||The dynamic interfacial tensions of non-ionic Triton X-100 surfactants, chicken-egg-white lysozyme proteins, and binary mixtures of Triton X-100-lysozyme at the dodecane-water interface were measured using a capillary wave technique. Consistent with results reported in the literature, the adsorption of Triton X-100 was found to be diffusion-controlled. The adsorption of lysozyme is well represented by a series of two first-order relaxation processes, which, respectively, had been identified in the literature as related to the adsorption/penetration of protein onto the interface and rearrangement/unfolding to its equilibrium in the interface. Our data show that the second process is the slower of the two. For Triton X-100-lysozyme binary mixtures, we found that the presence of nonionic Triton surfactants has little or no effect on the first process. In contrast, the Triton surfactants play a significant role in impeding the rearrangement/unfolding of the protein molecules in the interface. Copyright (C) 1999 Elsevier Science B.V.||Source Title:||Colloids and Surfaces B: Biointerfaces||URI:||http://scholarbank.nus.edu.sg/handle/10635/66432||ISSN:||09277765||DOI:||10.1016/S0927-7765(99)00011-9|
|Appears in Collections:||Staff Publications|
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