Changes in the structure and functional properties of soybean isolate protein: Effects of different modification methods.
Functional properties
Modification method
Soybean protein isolate
Structure
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
30 Jan 2024
30 Jan 2024
Historique:
received:
06
12
2022
revised:
12
08
2023
accepted:
17
08
2023
medline:
18
9
2023
pubmed:
1
9
2023
entrez:
31
8
2023
Statut:
ppublish
Résumé
Soybean protein isolate (SPI) is an important plant protein in food processing; however, its spherical structure prevents the exposure of its hydrophobic residues and affects its functional properties. In this study, we elucidate the effects of deamidation, phosphorylation, and glycosylation on the structure (Fourier-transform infrared spectroscopy, circular dichroism, fluorescence, and scanning electron microscopy) and functional properties (solubility, emulsifying activity index (EAI), and emulsifying stability index (ESI)) of SPI. The zeta potentials of the deamidated, phosphorylated, and glycosylated (DSPI, PSPI, and MSPI, respectively) samples decreased significantly (p < 0.05) relative to those of SPI. The functional properties of the modified SPI samples were improved, with MSPI-2 showing the best solubility (86.73 ± 0.34%), EAI (118.89 ± 0.73 m
Identifiants
pubmed: 37651782
pii: S0308-8146(23)01832-0
doi: 10.1016/j.foodchem.2023.137214
pii:
doi:
Substances chimiques
Soybean Proteins
0
Plant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
137214Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.