Physicochemical Properties and Metal Ion-Binding Capacity of Thermal-Induced Antarctic Krill Protein Aggregates under Different pH Conditions

Protein properties can be modified by thermal treatment at different pH values, resulting in the formation of protein aggregates with diverse morphologies and functionalities. This study investigated the morphology of aggregates of Antarctic krill protein (AKPS) formed by thermal treatment (90 °C, 15 min) at pH 2, 3, 4, and 6-12, characterized the different morphologies of AKPS, and determined the metal ion (Ca