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<p>This study investigates the non-covalent complexation of decolorized highland barley protein (DHBP) with five structurally distinct polyphenols—gallic acid (GA), chlorogenic acid (CA), naringin (NA), salidroside (SA), and hesperidin (HE)—and its effects on protein conformation and antioxidant activity. Complexation with GA and CA induced significant aggregation and phase separation at higher concentrations, with particle size increasing from 154.4&#xa0;nm (native DHBP) to 2416.0&#xa0;nm and 4724.0&#xa0;nm, respectively. In contrast, complexes with NA, SA, and HE remained more stable. Polyphenol binding (except HE) increased surface hydrophobicity by up to 2.5-fold, indicating protein unfolding. Fluorescence quenching was observed for all polyphenols except SA, which uniquely exhibited a tyrosine emission peak. Secondary structure analysis revealed a shift from β-sheets to α-helices/turns upon complexation with GA, CA, NA, and SA, while HE induced partial unfolding with increased random coil content (from 31.86% to 36.70%). All DHBP-polyphenol complexes exhibited significantly enhanced antioxidant activity compared to native DHBP, with the DHBP-HE complex demonstrating consistent synergistic effects. These findings provide a structural basis for designing DHBP-polyphenol complexes as functional food ingredients with improved antioxidant properties.</p>

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Conformational and antioxidant activity changes in decolorized highland barley protein induced by polyphenol complexation

  • 期刊论文

  • 发表日期：

    2026年7月1日

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  • Bing Dang,
  • Muyan Ma,
  • Juan Li,
  • Wenju Zhou,
  • Pin Ma,
  • Chengjun Ji,
  • Yan Du,
  • Feng Liang,
  • Zhaoxin Tu,
  • Xijuan Yang

摘要

This study investigates the non-covalent complexation of decolorized highland barley protein (DHBP) with five structurally distinct polyphenols—gallic acid (GA), chlorogenic acid (CA), naringin (NA), salidroside (SA), and hesperidin (HE)—and its effects on protein conformation and antioxidant activity. Complexation with GA and CA induced significant aggregation and phase separation at higher concentrations, with particle size increasing from 154.4 nm (native DHBP) to 2416.0 nm and 4724.0 nm, respectively. In contrast, complexes with NA, SA, and HE remained more stable. Polyphenol binding (except HE) increased surface hydrophobicity by up to 2.5-fold, indicating protein unfolding. Fluorescence quenching was observed for all polyphenols except SA, which uniquely exhibited a tyrosine emission peak. Secondary structure analysis revealed a shift from β-sheets to α-helices/turns upon complexation with GA, CA, NA, and SA, while HE induced partial unfolding with increased random coil content (from 31.86% to 36.70%). All DHBP-polyphenol complexes exhibited significantly enhanced antioxidant activity compared to native DHBP, with the DHBP-HE complex demonstrating consistent synergistic effects. These findings provide a structural basis for designing DHBP-polyphenol complexes as functional food ingredients with improved antioxidant properties.