Abstract

The effects of electron beam irradiation (EBI) at different doses (0, 2, 4, 6, 8, and 10 kGy) were investigated on the structural and functional properties of casein, including their interrelationship. A gradual reduction in the α-helix content of the secondary structure (as a stable structure) indicates that casein under EBI treatment mainly undergoes fragmentation and aggregation from a structural perspective. Furthermore, the hydrophobic group and tryptophan in the tertiary structure were exposed, which opened up the internal structure of the protein. In addition, a continuously increasing irradiation dose led to casein aggregation, as confirmed by electron microscopy. The structural changes affected its functional properties, such as solubility, emulsification, foaming, and rheological properties, all of which increased first and subsequently decreased. Finally, at irradiation doses of 4–6 kGy, casein was modified to exhibit optimal functional properties, which enhanced its food processing value and performance.

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