Abstract
Abstract Dispersions of commercial casein and whey protein and laboratory-prepared soybean protein were studied in mixed dispersants of water with various aliphatic alcohols, methanol, ethanol, n-propanol and 2-propanol. Supernatant and protein sediments were separated by centrifugation in two steps: 1800 rpm 10 min, followed by centrifugation of the supernatant at 50 000 rpm for 60 min (125 000×g). A gel-like protein sediment obtained at low alcohol concentration by high-g centrifugation increased in amounts as a function of the alcohol concentration until it progressively transformed, with higher alcohol concentrations, into an opaque flock (precipitate), sedimenting at 1800 rpm. It was concluded that the sediment obtained by ultracentrifugation was a protein of increased density which was produced by partial and progressive dehydration and alcohol binding. The conversion of the sediment into a flock or precipitate is discussed in terms of the hydrophilic-lipophilic balance of the protein and of the polar-nonpolar character of the dispersant.
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