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Heat-induced Complex Formation between κ-Casein and α-Lactalbumin

It is considered that heat treatment affects the properties of milk such as heat-stability and chymosin clottability. The heat-induced interaction between κ-casein and α-lactalbumin was investigated under various conditions (buffer, pH, ionic strength, temperature). The results obtained, using Sephacryl S-300 gel filtration and sodium dodecylsulfate-polyacrylamide gel electrophoresis, indicated that a complex of the two proteins was formed in 35 m m phosphate buffer, pH 7.6, containing 0.4 m NaCl on heat treatment at 90°C for 30 min, while no complex was formed in 10m m imidazole–HCl buffer, pH 7.1, containing 70 m m KC1 with the same heat treatment. A κ-casein-α-lactalbumin complex was formed at high pH by heat treatment, and was dissociated in the presence of 2-mercaptoethanol. Under complex forming conditions, a change in the higher-order structure of α-lactalbumin was observed by ultraviolet absorption and fluorescence experiments. Though the participation of specific amino acid residues in the comple...