Synergistic modification of sunflower seed protein by pH-cycling and ultrasound to improve its structural and functional properties
文献类型: 外文期刊
作者: Zhenyuan Li;Xuegang Huang;Jiaxin Guo;Yumeng Hu;Karim Gafurov;Jinchuang Zhang;Qiang Wang;Qin Guo
作者机构:
关键词: pH-cycling;Solubility;Structural modification;Sunflower seed protein;Ultrasound
期刊名称: Food Hydrocolloids
ISSN: 0268-005X
年卷期: 2025 年 172 卷
页码:
收录情况: SCIE(2025版) ; ; EI(2025版)
摘要: Sunflower seed protein (SPI) is a high-quality plant-based protein with balanced nutrition, low allergenicity, and excellent sustainability. However, its limited solubility hinders the full expression of its functional properties, thereby restricting its broader application in food processing. To address this issue, SPI was modified via a synergistic treatment combining pH-cycling and ultrasound in this study, and its modification mechanism and functional properties were comprehensively evaluated. The results indicate that the combined treatment induced protein structural aggregation-disaggregation-rearrangement, significantly enhancing SPI solubility to 81.27 %, representing a 58.14 % increase compared to unmodified protein. During modification, pH-cycling treatment converted SPI molecules into a molten globule state, while ultrasonic cavitation and shear forces effectively disrupted protein aggregates. This led to increased exposure of chromophores on side chains, enhanced fluorescence intensity, reduced particle size to 81.08 nm, and increased ζ-potential (−38.77 mV), thereby improving system stability. The modified SPI exhibited a higher enthalpy change (ΔH = 3.58 J/g), along with markedly improved functional characteristics: foaming capacity and foam stability increased by 2.29 times and 2.69 times, respectively; emulsifying activity and stability reached 6.23 m2/g and 88.72 %; and oil-holding capacity was enhanced to 5.52 g/g, representing 2.73 times increase. Overall, the synergistic pH-cycling and ultrasound modification proved highly effective in improving the solubility and functional performance of sunflower seed protein, offering promising potential for its application in advanced food systems.
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