Abstract
The heat treatment required for the deactivation of enzymes was carried out on crop species such as oats. Stir-frying, a frequently employed method for enzyme inactivation to preserve their desirable shelf life, can result in diminished nutritional value and protein degeneration. The mechanism by which stir-frying affects the oat protein remains largely unknown. Therefore, this study aimed to investigate the physicochemical and functional properties of the extracted oat protein isolates (OPI) at different stir-frying durations (0, 10, 20, and 30 min) at a temperature of 230 °C. The findings of this study demonstrated that stir-frying led to a decrease in the content of amino acids (AA), potentially attributed to the involvement of certain amino acids in the Maillard reaction. As the time of stir-frying increased, the secondary structure of OPI underwent changes: specifically, β-turns transformed into β-sheets. The process of protein denaturation and redistribution of chemical bonds resulted in an increase in the disulfide bond content of OPI, leading to aggregation, large particle size, and reduced digestibility. However, the water retention properties, foaming properties, and emulsification properties of OPI showed improvement. These findings provide valuable insights for the controlled and precise processing of oats and highlight the potential of OPI as a functional food.