Abstract
Secalin (SCL), the prolamin fraction of rye protein, was chemically lipophilized using acylation reaction by treatment with different amounts of capric acid chloride (0, 2, 4, and 6 mmol/g) to enhance its functional properties. It was shown that SCL lipophilization increased the surface hydrophobicity and the hydrophobic interactions, leading to a reduction in protein solubility and water absorption capacity and to a greater oil absorption. In addition, SCL both emulsifying capacity and stability were improved when the protein was treated with low amount of capric acid chloride. Finally, the foaming capacity of SCL markedly increased after its treatment with increasing concentrations of the acylating agent, even though the foam of the modified protein was found to be more stable at the lower level of protein acylation. Technological application of lipophilized SCL as a protein additive in food preparations is suggested.