Interfacial properties of acidified skim milk.
The purpose of this study is to investigate the tension properties and dilatational viscoelastic modulus of various skim milk proteins (whole milk, EDTA-treated milk, beta-casein, and beta-lactoglobulin) at an oil/water interface at 20 degrees C. Measurements are performed using a dynamic drop tensiometer for 15,000 s. The aqueous bulk phase is a skim milk simulated ultrafiltrate containing 11 x 10(-3) g L(-1) milk protein. At pH 6.7, beta-casein appears as the best to decrease the interfacial tension, whereas beta-lactoglobulin leads to the highest interfacial viscoelastic modulus value. Whole milk was almost as surface-active as individual beta-casein in terms of the final (steady-state) lowering of the interfacial tension, but the rate of tension lowering was smaller. EDTA treatment improved the rate of tension lowering of whole milk. The acidification of milk, from previous measurements, would lead to the enhancement of surface activity. At t=15,000 s, the order of effectiveness is pH 4.3 > pH 5.3 = pH 5.6 > pH 6.7 whole milk, suggesting that pH 4.3 whole milk is the best surface active. As compared to pH 6.7 whole milk, the use of pH 5.3 and pH 5.6 milk as surface active would result in the use of milk containing more free beta-casein born of pH-dissociated casein micelles.
Cases
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Laboratoire IMSA-ENSBANA, Campus Montmuzard 1, esplanade Erasme, Dijon, France. eliane.cases@u-bourgogne.fr
Rampini
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Cayot
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D000143:Acids; D000818:Animals; D002364:Caseins; D004655:Emulsions; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins; D008892:Milk / Q000737:chemistry*; D008894:Milk Proteins / Q000737:chemistry*; D013500:Surface Tension
D000143:Acids; D002364:Caseins; D004655:Emulsions; D007782:Lactoglobulins; D008894:Milk Proteins