It has been shown that there is a time-dependent transfer of β-casein and the milk serine proteinase system from micelles to milk serum with change of temperature from 38 to 4 °C. It has been established that the γ-caseins can be formed by proteolytic degradation of β-casein. By a simple extraction technique, the very hydrophobic γ-casein fraction was separated from stored milks (26 and 4 °C) and estimated quantitatively. The results showed that the proteolytic degradation of β-casein is faster at 4 °C than at room temperature and this can be explained by the immobilization of enzyme and substrate at the micelle surface at higher temperatures (26 °C).

The results indicate that irreversible changes during cooling for short periods do not cause problems in milk processing, but the formation of γ-caseins and phosphopeptides may influence the technological properties of raw milk stored for more than 48 h.