Abstract
The integration of coffee into coconut milk and related beverages offers a potential strategy to enhance the digestibility of coconut protein. This study explored the molecular mechanisms by which phenolic acids, chlorogenic acid (CHA), ferulic acid (FA), and caffeic acid (CA), improved the digestibility of coconut 11S globulin (11S CG). The analyses demonstrated that phenolic acids primarily interacted with 11S CG through hydrogen bonding and hydrophobic interactions. Among these, CHA exhibited the strongest binding affinity, which was attributed to its greater number of polar functional groups and a larger hydrophobic region. Phenolic acids induced partial unfolding of the protein's secondary structure and dissociation of protein aggregates, resulting in the smallest particle size for 11S CG-CHA. These structural modifications enhanced the accessibility of digestive enzymes, leading to significantly higher degrees of digestibility and antioxidant activity. This research could provide valuable insights for the development of high-quality plant-based protein ingredients.