Nuclei-induced formation of amyloid fibrils in whey protein: Effects of enzyme hydrolysis on the ability of nuclei to induce fibril formation.
Food Chem
; 410: 135433, 2023 Jun 01.
Article
en En
| MEDLINE
| ID: mdl-36640658
Homogeneous and secondary nuclei (HN and SN) are aggregates formed at different stages of whey protein isolate (WPI) self-assembly. More fibrils can form when HN/SN are added as nuclei than when WPI self-assembles. We evaluated the effect of hydrolysis treatment on fibril-induction ability of nuclei derived from WPI, and investigated the relationship between induction ability and nuclear structure. Hydrolyzed SN-induced 9.47% more WPI fibrils than unhydrolyzed SN-induced. Infrared spectroscopy, X-ray diffraction analysis, and atomic force microscopy were used to examine the structural changes in hydrolyzed nuclei and the fibrils induced using these nuclei. We concluded that hydrolysis treatment led to a looser inter-ß-sheet packaging in nuclei by increasing the inter-ß-sheet distance. The inter-ß-sheet distance of cross-ß structure was a key determinant of fibril-induction ability of nuclei, which could be enhanced when inter-ß-sheet structure was moderately loose. This research may provide a theoretical basis for the mechanism of nuclei-induced WPI fibrillation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Amiloide
Idioma:
En
Revista:
Food Chem
Año:
2023
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Reino Unido