Sequential changes in antioxidant activity and structure of curcumin-myofibrillar protein nanocomplex during in vitro digestion

This study aimed to investigate the in vitro digestion of curcumin-myofibrillar protein (MP) complexes characterized by antioxidant activity and structure changes. Curcumin-MP nanocomplexes were prepared by pH shifting (from 12 to 7) method and then digested in vitro. Results showed that the protein released by dissolved nitrogen and the scavenging rates of DPPH and ABTS free radicals were enhanced significantly by the formation of nanocomplex with curcumin. During simulated digestion, curcumin can reduce the alpha-helix of protein, along with red shifted and significantly decreased maximum fluorescence intensity. This structural difference may change the restriction sites of MP, resulting in substantial changes in the digested products composition and 11 unique peptides with potential bioactivity appearance in the digested products of curcuminMP complex. Our finding revealed the Curcumin-MP nanocomplexes has unique protein digestion fate which has potential application on functional enhanced food.

Automated summary

This study investigated the in vitro digestion of curcumin-myofibrillar protein (MP) complexes and found that the nanocomplexes significantly enhanced the release of protein and the scavenging of free radicals. Additionally, curcumin can alter the protein structure during digestion, leading to changes in the composition of the digested products.