Effects of Iron Saturations on the Physicochemical Properties and Potential Physiological Functions of Ovotransferrin: Based on Structure–Activity Relationship

Ovotransferrin (OVT) is a multifunctional protein related to lactoferrin (LF), sharing similar characteristics and considered a cost-effective alternative. Researchers were intrigued by the differences in iron saturation between native-LF and native-OVT, but whether iron saturation affected the cost-effectiveness of the ligand of OVT compared to LF was still uncertain. This study investigated the structure, physicochemical properties, and potential functions of an OVT with varying iron saturation levels, aiming to clarify the impact of iron saturation on an OVT. The findings showed that increased iron saturation altered the structure of an OVT, leading to changes in its physicochemical properties, such as larger particle size and better thermal stability. The findings from peptidomics indicated that iron saturation affects the resistance of OVT to digestion, resulting in the generation of peptides with distinct molecular weights and diverse potential functionalities. Overall, this study provided evidence to support that iron saturation was a limiting factor for the functional performance of the OVT.