Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility.
Curr Res Struct Biol
; 7: 100135, 2024.
Article
em En
| MEDLINE
| ID: mdl-38516624
ABSTRACT
Plant-based proteins are often associated with a range of health benefits. Most research primarily investigates pea and soy proteins, while lentil proteins received minimal attention. This study evaluates the effect of protein complexation (using the pH-shifting technique) coupled with trehalose conjugation on lentil and whey proteins. The protein structures after the modification were analysed using spectroscopic methods:
Fourier-transform infrared, ultraviolet spectra, and fluorescence spectra. The amide group I, conformation protein, and tertiary structure of the trehalose-conjugated lentil-whey protein complexes (T-LWPs) showed significant changes (P < 0.05). Moreover, the surface properties (surface hydrophobicity and charges) of T-LWPs were significantly modified (P < 0.05), from 457 to 324 a.u and from 36 to -40 mV, respectively. Due to these modifications on the protein structures, the protein digestibility (80-86%) and water solubility (90-94.5%) of T-LWPs increased significantly (P < 0.05) with the increase in the trehalose concentration, from 0 (control) to 5% (w/w), respectively. This study suggested that coupling protein complexation and trehalose conjugation can enhance the overall properties of lentil-based protein complexes. With this enhancement, more opportunities in the utilisation of lentils are to be expected.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
Curr Res Struct Biol
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Malásia