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|Title: ||Comparison of positional surfactant isomers for displacement of rubisco protein from the air-water interface|
|Authors: ||He, LZ|
|Issue Date: ||15-Aug-2011|
|Publisher: ||Academic Press INC Elsevier|
|Citation: ||He, L.Z., Onaizi, S.A., Dimitrijev-Dwyer, M., Malcolm, A.S., Shen, H.H., Dong, C.C., Holt, S.A., Thomas, R.K., Middelberg, A.P.J. (2011). Comparison of positional surfactant isomers for displacement of rubisco protein from the air-water interface. Journal of Colloid and Interface Science, 360(2), 617-622.|
|Abstract: ||Protein-surfactant interaction, which is a function of the protein and surfactant characteristics, is a common phenomenon in a wide range of industrial applications. In this work, we used rubisco, the most abundant protein in nature, as a model protein and sodium dodecylbenzenesulfonate (SDOBS), one of the most widely used commercial surfactants, with two positional isomers (SDOBS-2 and SDOBS-6), as a model surfactant. We first examined the surface tension and the mechanical properties of interfacial mixed rubisco-SDOBS films adsorbed at the air-water interface. The concentration of rubisco in solution was fixed at 0.1 mg mL(-1) while the SDOBS concentration varied from 0 to 150 mu M. Both the surface tension and the mechanical strength of the interfacial film decreased with increasing SDOBS concentration. Overall, the surface tension of a rubisco-SDOBS-6 mixture is lower than that of rubisco-SDOBS-2, while the mechanical strength of both systems is similar. Neutron reflection data suggest that rubisco protein is likely denatured at the interface. The populations of rubisco and SDOBS of the mixed systems at the interface were determined by combining non-deuterated and deuterated SDOBS to provide contrast variation. At a low surfactant concentration, SDOBS-6 has a stronger ability to displace rubisco from the air-water interface than SDOBS-2. However, when surfactant concentration reaches 50 mu M, SDOBS-2 has a higher population than SDOBS-6, with more rubisco displaced from the interface. The results presented in this work suggest that the extent of protein displacement from the air-water interface, and hence the nature of the protein-surfactant interactions at the interface, are strongly affected by the position of surfactant isomerisation, which might allow the design of formulations for efficient removal of protein stains.(C) 2011 Elsevier Inc. All rights reserved.|
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