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Sequential changes in antioxidant activity and structure of curcumin-myofibrillar protein nanocomplex during in vitro
Changling Wu1, Hualin Dong1, Peng Wang1
1Key Laboratory of Animal Products Processing, Ministry of Agriculture, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Jiangsu Synergetic Innovation Center of Meat Production and Processing, and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China.
Abstract:
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 α-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 curcumin-MP complex. Our finding revealed the Curcumin-MP nanocomplexes has unique protein digestion fate which has potential application on functional enhanced food.
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