The major types of nondisulphide cross-linking which cause milk protein aggregation were investigated in milk, with and without lactose, heated at 95°C for up to 8 h. Compared with the milk containing no lactose, the milk containing lactose showed a smaller increase in pH, a larger increase in pH 4.6 soluble nitrogen, much smaller increase in lysinoalanine (LAL) and a much higher percentage of cross-linked proteins. It was concluded that cross-linking in milk products containing lactose occurs mainly via Maillard reaction products, and in milk products with no lactose, it occurs mainly via isopeptide linkages such as in LAL.

The optimum conditions for the production of coprecipitate from sheep milk were studied. The best percentage of calcium chloride added to milk was 0.2%, which resulted in a recovery of 97.5% of milk proteins. At low pH (4.5–5), the recovery of protein was low, but it increased at higher pH values (5.5–6.5); recovery was greatest at pH 6.5. The optimum heating temperature to obtain coprecipitate from sheep milk was 85–95°C. The functional properties of the sheep milk coprecipitate were studied. At pH values higher than 6, there were no differences between the solubility of sheep milk coprecipitate and sheep milk sodium caseinate, but the solubility of coprecipitate at pH values lower than 5 was relatively higher than those of the caseinate. At pH ≥6, the emulsion activity index (EAI) for emulsions of sheep milk coprecipitate and caseinate increased as pH increased; at all pH values, the EAI of the coprecipitate was higher than that of the caseinate. Sheep milk coprecipitate showed higher foaming ability and stability than sheep milk sodium caseinate.

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The effect of heat, transglutaminase and combination of heat and transglutaminase treatments on the solubility of films prepared from goat milk casein, goat milk whey proteins and whole goat milk proteins was investigated. Goat milk casein films were less soluble when treated with transglutaminase and combination of heat with transglutaminase compare with heat-treated caseins alone. Heat treatment was more effective at decreasing the solubility of whey protein films. SDS-PAGE patterns demonstrated that goat milk caseins were better cross-linked by transglutaminase, whereas whey proteins were better cross-linked by heat. The extent of cross-linking was further enhanced when a combination of heat and transglutaminase was used.