Molecular interaction between myofibrillar protein and beta-carotene during heating

Beta-carotene (β-C) is a natural phytochemical with good functions, but the strong hydrophobicity and acid-base instability limit its absorption in the intestine. A well-designed heat-induced myofibrillar protein (MP) transport system can improve the bioavailability of β-C, and temperature might have a significant impact on this process. This study utilized multispectral, surface plasmon resonance (SPR), and molecular dynamics simulation to investigate the effect of temperature on the interaction between β-C and MP. The results showed that the major interaction between β-C and MP switched from Van der Waals force to hydrophobic interaction at near 37 °C. The changes in the spatial structures of proteins and the thermal motion of molecules may be the main reasons for the transformation of intermolecular interaction. These results indicated that selecting the appropriate temperature is of great significance for designing the transport system of β-C.