Thermal stability of whey proteins studied by differential scanning calorimetry |
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Authors: | M. Paulsson P.-O. Hegg H.B. Castberg |
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Affiliation: | Dept. of Food Technology, University of Lund, P.O.Box 124, S-221 00 Lund, Sweden |
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Abstract: | The thermal stability of the bovine whey proteins.; β-lactoglobulin (β-1g), α-lactalbumin (α-1a) and serum albumin (BSA) was studied individually and in mixtures in the temperature range 25–140°C by differential scanning calorimetry. The thermal denaturation temperature (TD) and the transition enthalpies (ΔHapp) were determined at different pH-values (3.0–10.0) in simulated milk ultrafil-trate (SMUF).β-Lg was, except at pH 9.0 and 10.0, the most thermostable protein at all pH-values. At acidic pH-values BSA was the least thermostable. At alkaline pH-values, however, α-la had lower thermal stability than BSA. α-La exhibited double peak behaviour at acidic pH-values and ΔHapp was dependent on Ca-content. Mixtures of the proteins were studied at pH 4.0, 5.0 and 6.6. In general, when mixed, the proteins seemed to denaturate independently of each other. |
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