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Exploring the polymorphism of foxtail millet proteins and the mechanisms of activity variations driven by varietal
Zeyu Peng1, Jia Cao1, Hongyue Zhao1
1College of Food Science, Northeast Agricultural University, Harbin 150030, China.
Abstract:
Foxtail millet proteins (FMPs), as highly nutritious ingredients, hold significant potential for applications in dietary supplements and functional foods. This study analyzed the structure, antioxidant activity, and amino acid (AA) composition of nine varieties of FMPs. It also explored the relationship between protein structure, AA composition, and antioxidant activity. Results indicated clear differences among FMP varieties. Structural features such as low α-helix content, high random coil content, pronounced red shifts in λ max, elevated UV absorption intensity, increased surface hydrophobicity (H0) (660.18-715.73), greater free sulfhydryl content (53.12-58.95 μmol/g), and subunit variation (higher proportions of low-molecular-weight subunits, <59 kDa) contributed to enhanced antioxidant activities in specific varieties (HZ3, JG21, and LG38). These were characterized by lower IC50 values for DPPH radical scavenging, ABTS radical scavenging, •OH radical scavenging, and Fe2+ chelation, as well as higher reducing power. Additionally, the AA composition showed that highly active FMPs (HZ3, JG21, and LG38) contained elevated levels of hydrophobic AAs (35.54-37.64 g/100 g protein), aromatic AAs (7.72-8.07 g/100 g protein), and negatively charged AAs (18.70-19.46 g/100 g protein). Correlation analysis further confirmed that the degree of unfolding in the higher-order structures varied among different FMP varieties, significantly influencing their antioxidant activity. In particular, a significant correlation was observed between H0 and multiple antioxidant indicators (P ≤ 0.05).
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