Self-assembly and aggregation behavior of temperature-controlled modified glycinin and d-galactose colloidal particles.
Food Chem
; 441: 138323, 2024 May 30.
Article
en En
| MEDLINE
| ID: mdl-38199105
ABSTRACT
The molecular structure and morphologies of complex colloidal particles with modified glycine (S-11S) and d-galactose were studied by multispectral, microscopic imaging and chromatographic techniques at different temperatures, and the self-assembly and aggregation mechanisms were determined. Overall, high-temperature-treated S-11S and d-galactose associate at cysteine and phenylalanine sites and self-assemble into colloidal particles of greater stability than glycinin and S-11S via ionic and disulfide bonds. The structure and subunit content of composite colloidal particles were changed. Assessing the sub-microstructure reveals that temperature can regulate the directional aggregation of complex colloidal particles. The elasticity of the complex colloidal particles is maximum enhanced at 95â¯â as confirmed by the rheological. Thus, the heat-treated aggregation of the soy protein and its complex was evaluated to provide a new theoretical basis for the application of soy protein in gels and other areas and contribute to the design of new soy protein products.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Soja
/
Globulinas
Idioma:
En
Revista:
Food Chem
Año:
2024
Tipo del documento:
Article
País de afiliación:
China