Food Hydrocolloids, Год журнала: 2025, Номер unknown, С. 111510 - 111510
Опубликована: Апрель 1, 2025
Язык: Английский
Food Hydrocolloids, Год журнала: 2025, Номер unknown, С. 111510 - 111510
Опубликована: Апрель 1, 2025
Язык: Английский
Foods, Год журнала: 2025, Номер 14(7), С. 1204 - 1204
Опубликована: Март 29, 2025
The application of walnut protein isolate (WPI) and polyphenols is usually limited by low solubility. To solve the above problem, impact alkaline treatment method ultrasound-assisted on structural functional properties protein–polyphenol covalent complexes (WPI–(–)-epigallocatechin-3-gallate (EGCG), UWPI–EGCG, respectively) was explored. Fourier transform infrared spectroscopy fluorescence indicated that binding EGCG to WPI altered secondary tertiary structures increased its random coil content. In addition, UWPI–EGCG samples had lowest particle size (153.67 nm), largest absolute zeta potential value (25.4 mV), highest polyphenol (53.37 ± 0.33 mg/g protein). Meanwhile, WPI–EGCG also possessed excellent solubility emulsification properties. These findings provide a promising approach for in applications such as foods.
Язык: Английский
Процитировано
0Food Hydrocolloids, Год журнала: 2025, Номер unknown, С. 111510 - 111510
Опубликована: Апрель 1, 2025
Язык: Английский
Процитировано
0