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<p>This study focuses on the controlled ball milling approach to achieve significant alterations in the structural and functional properties of dephenolized sunflower protein isolate. Electron microscopy revealed that the protein particles had irregular, disordered, and rough surfaces, and irregularities increased as the size of the particles decreased. The results demonstrated that after 8&#xa0;h of milling time, the particle size decreased from 23.91&#xa0;µm to 311.45&#xa0;nm. SDS-PAGE analysis revealed the appearance of new bands, but the subunit compositions and bands remained unchanged with increased grinding time. The X-ray diffraction crystallinity peak, observed at a 2<i>θ</i> value of 20°, remained unchanged while the crystallinity of ball-milled protein isolates was enhanced. However, FTIR analysis indicated a decrease in α-helices and β-sheets and an increase in β-turns and random coil structures, suggesting that the secondary structure of the protein isolates became more disordered and looser. Modifications in the microenvironment, secondary structure, and amino acid residues were too evident through intrinsic fluorescence. Additionally, the solubility of protein isolates improved significantly within treatment durations. Overall improvement in the different functional properties was observed. From the results obtained in this study, it can be concluded that mechanochemical reduction through ball milling is a powerful approach for synthesizing protein nanoparticles with desirable functional and structural properties for application in different food applications.</p>

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Ball Milling-Induced Structural and Functional Modifications in Dephenolized Sunflower Protein Isolates

  • 期刊论文

  • 发表日期：

    2026年3月23日

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  • Sadaf Dur,
  • Nisar Ahmad Mir,
  • Tariq Ahmad Ganaie

摘要

This study focuses on the controlled ball milling approach to achieve significant alterations in the structural and functional properties of dephenolized sunflower protein isolate. Electron microscopy revealed that the protein particles had irregular, disordered, and rough surfaces, and irregularities increased as the size of the particles decreased. The results demonstrated that after 8 h of milling time, the particle size decreased from 23.91 µm to 311.45 nm. SDS-PAGE analysis revealed the appearance of new bands, but the subunit compositions and bands remained unchanged with increased grinding time. The X-ray diffraction crystallinity peak, observed at a 2θ value of 20°, remained unchanged while the crystallinity of ball-milled protein isolates was enhanced. However, FTIR analysis indicated a decrease in α-helices and β-sheets and an increase in β-turns and random coil structures, suggesting that the secondary structure of the protein isolates became more disordered and looser. Modifications in the microenvironment, secondary structure, and amino acid residues were too evident through intrinsic fluorescence. Additionally, the solubility of protein isolates improved significantly within treatment durations. Overall improvement in the different functional properties was observed. From the results obtained in this study, it can be concluded that mechanochemical reduction through ball milling is a powerful approach for synthesizing protein nanoparticles with desirable functional and structural properties for application in different food applications.