Abstract
Ultrasonic velocities and densities of anionic surfactant, sodium dodecyl sulfate (SDS), in aqueous solutions of gelatin (0.25, 0.50, 1.00%w/v) have been measured over a wide temperature range (20–40 °C) at an interval of 2 °C by using DSA-5000. The data was used to calculate partial molar volume (Ф v ), adiabatic compressibility (β) and apparent molar compressibility (Ф k ) in order to explain protein–surfactant interactions. Viscosity measurements (viscous relaxation time and activation energy parameter) of SDS in aqueous solutions of gelatin were also carried out to support the explanation. A minimum observed in case of activation parameter in the concentration region 6–8 mmol kg − 1 of SDS supported the results obtained by other parameters indicating micellar solubilisation of the SDS in this region. The behaviour of both Ф k and Ф v data indicates that SDS binding to gelatin is non-cooperative at low surfactant concentration but becomes cooperative at higher concentration.
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