Effect of succinylation-assisted glycosylation on the structural characteristics, emulsifying, and gel properties of walnut glutenin

• Published in: Food chemistry 2024-07, Vol.446, p.138856-138856, Article 138856
• Main Authors: Wang, Yuanli, Tao, Liang, Wang, Zilin, Wang, Yue, Lin, Xinyue, Dai, Jiahe, Shi, Chongying, Dai, Tianyi, Sheng, Jun, Tian, Yang
• Format: Article
• Language: English
• Subjects: Glutens - chemistry; Glycosylation; Juglans - chemistry; Nuts - chemistry; Physicochemical properties; Sodium alginate; Structural characterization; Succinylation; Walnut glutenin
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2024.138856

[Display omitted] •GLU-SA and GLU-SA-ALG were prepared.•Succinylation reduced particle size and improved the solubility of GLU.•GLU-SA-ALG improved the order and flexibility of GLU structure.•GLU-SA-ALG expanded the application range of GLU in food protein processing. In this study, we examined the effects of various sodium alginate (ALG) concentrations (0.2%-0.8%) on the functional and physicochemical characteristics of succinylated walnut glutenin (GLU-SA). The results showed that acylation decreased the particle size and zeta potential of walnut glutenin (GLU) by 122- and 0.27-fold, respectively. In addition, the protein structure unfolded, providing conditions for glycosylation. After GLU-SA was combined with ALG, the surface hydrophobicity decreased and the net negative charge and disulfide bond content increased. The protein structure was analyzed by FTIR, Endogenous fluorescence spectroscopy, and SEM, and ALG prompted GLU-SA cross-linking to form a stable three-dimensional network structure. The results indicated that dual modification improved the functional properties of the complex, especially its potential protein gel and emulsifying properties. This research provide theoretical support and a technical reference for expanding the application of GLU in the processing of protein and oil products.