β-Lactoglobulin adsorption equilibrium at low- and high-energy surfaces Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/np193f48r

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  • Ellipsometry was used to study the effects of surface energetics and temperature on the equilibrium adsorptive behavior exhibited by β-lactoglobulin. β-Lactoglobulin isotherms at 25, 37, and 55°C were constructed for this purpose. The surfaces of acrylic, polycarbonate, polyester, glass, and #304 stainless steel were contacted with protein solutions of varying concentration, buffered at pH 6.7 with mono- and dibasic sodium phosphate. After three hours, the surfaces were mildly rinsed with deionized water and dried overnight. Optical properties of each film were ellipsometrically measured and the adsorbed mass was calculated as a function of film thickness and refractive index. Contact angle methods were used to measure the hydrophobicity exhibited by each of the five solid surfaces. However, interpretation of protein adsorption results based solely on solid surface hydrophobicity proved unworkable. For polymers (low-energy surfaces), the adsorbed mass of protein was explained with reference to the degree of extensibility of molecular structure. Glass (a high-energy surface) was observed to adsorb the greatest mass of β-lactoglobulin. Stainless steel was observed to adsorb the least mass of β-lactoglobulin and the plateau values of protein adsorption were found to be consistent with those reported elsewhere, and to lie within the range of adsorbed mass on metal surfaces in general. The temperature dependence of β-lactoglobulin adsorption could not be clearly quantified. Apparently, any differences in adsorbed mass were too small to be detected by the instrument. In any event, other investigators have not detected any significant difference in adsorbed mass as long as the temperature was below the denaturation temperature of the protein.
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