Three physical modifications enhanced the binding interactions of Cyperus esculentus protein with proanthocyanidins and physicochemical properties of complexes: The contribution of non-covalent interactions.

• Tác giả: Caixia Li, Jing Li, Mengqing Li, Xuebo Liu, Yijie Shi, Lijun Sun, Yutang Wang
• Ngôn ngữ: eng
• Thông tin xuất bản: England : Food chemistry , 2025
• Bộ sưu tập: NCBI
• ID: 708214

Tóm tắt

 This study investigated non-covalent interactions between unmodified/modified (ball-milling, BMP
  high pressure homogenization, HPHP
  cold plasma, CPP) Cyperus esculentus protein (CEP) and proanthocyanidins (PA and PB2) to evaluate structure, functionalities and potential in emulsions. The PA and PB2 addition significantly increased the turbidity and ζ-potential of CEP samples, as confirmed by aggregations observed via atomic force microscopy, validating the formation of protein-proanthocyanidin complexes. Fluorescence quenching and isothermal titration calorimetry revealed that procyanidins caused CEP sample static quenching, with CEP-proanthocyanidins binding affinity order as CPP >
  HPHP>
 BMP >
  CEP. The CEP-proanthocyanidins involve non-covalent interactions, driven by hydrogen bonding and electrostatic interactions, without altering CEP sample spectral bands and secondary structures, but enhancing thermal stabilities, antioxidant activities, and emulsifying properties. Then, the CPP-PA stabilized emulsion droplet size decreased with aqueous phase pH increasing, contrary to ζ-potential values. Conclusively, these findings illustrated that the modified CEP-proanthocyanidin complexes as a promising strategy for addressing these challenges and stabilizing emulsion.