Abstract
This work attempts to investigate the inhibitory effect of L-lysine (Lys) on the thermal aggregation of coconut protein (CP). The results showed that under neutral conditions (pH = 7), temperature reduced the solubility and enhanced the thermally induced gel formation of CP. In addition, Lys reduced the fluorescence properties, particle size and increased the turbidity of CP, which had an inhibitory effect on heat induced gels. The results indicate that Lys plays an important role in inhibiting protein thermal aggregation by interacting with CP to create steric hindrance and increase protein electrostatic repulsion.