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Cited by 37Proteins in Food SystemsPolysaccharides Composition and ApplicationsHydrogels: synthesis, properties, applications

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Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

Cheng, Xiaoyi, Li, Wenkang, Peng, Ruiqi, Chen, Yan, Mu, Sixian, Cui, Lifan, Liu, Zhengqin, Wang, Huan, Xu, Jing, Jiang, Lianzhou·2024·Journal of Agricultural and Food Chemistry
DOI 10.1021/acs.jafc.4c02232
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Abstract

The objective of this work was to investigate the effect of succinylation treatment on the physicochemical properties of black bean proteins (BBPI), and the relationship mechanism between BBPI structure and gel properties was further analyzed. The results demonstrated that the covalent formation of higher-molecular-weight complexes with BBPI could be achieved by succinic anhydride (SA). With the addition of SA at 10% (v/v), the acylation of proteins amounted to 92.53 ± 1.10%, at which point there was a minimized particle size of the system (300.90 ± 9.57 nm). Meanwhile, the protein structure was stretched with an irregular curl content of 34.30% and the greatest processable flexibility (0.381 ± 0.004). The dense three-dimensional mesh structure of the hydrogel as revealed by scanning electron microscopy was the fundamental prerequisite for the ability to resist external extrusion. The thermally induced hydrogels of acylated proteins with 10% (v/v) addition of SA showed excellent gel elastic behavior (1.44 ± 0.002 nm) and support capacity. Correlation analysis showed that the hydrogel strength and stability of hydrogels were closely related to the changes in protein conformation. This study provides theoretical guidance for the discovery of flexible proteins and their application in hydrogels.

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  • Succinylation of black soybean protein increased the stretching and irregular coiling of protein polypeptide chains after acylation, enhancing intermolecular interactions during gelation.

    “As shown in Figure 7, Cheng et al. (2024) investigated the effects of succinylation on the gelling properties of black soybean protein, indicating that the increased stretching and irregular coiling of the protein polypeptide chains after acylation enhanced intermolecular interactions during gelation.”

    From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Cheng et al. (2024)

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Metadata

Authors
Cheng, X., Li, W., Peng, R., Chen, Y., Mu, S., Cui, L., Liu, Z., Wang, H., Xu, J., & Jiang, L.
Affiliations
Northeast Agricultural University (CN)
Corresponding author
  • Wang, Huan
  • Xu, Jing
ORCID
Venue
Journal of Agricultural and Food Chemistry
Publisher
American Chemical Society (ACS)
Published
2024-07-08
Volume
72
Issue
28
Pages
15920-15932
ISSN
  • 0021-8561 (ISSN-L)
  • 1520-5118
DOI
10.1021/acs.jafc.4c02232
OpenAlex
W4400426005
Cited by
37
References
2
Citations by year
2026: 18 · 2025: 18 · 2024: 1
FWCI
6.24
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Journal of Agricultural and Food Chemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Northeast Agricultural University (X202310224142)
  • Key Research and Development Program of Heilongjiang (GA21B001)
  • National Natural Science Foundation of China (31901605)
  • College Student SIPT Innovation Training Program of Heilongjiang Province (S202310224106)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
  • Physical Sciences › Materials Science › Biomaterials › Hydrogels: synthesis, properties, applications
Keywords
succinylation, succinic anhydride, protein hydrogels, protein conformation, hydrogel microstructure, gel mechanical properties, protein acylation, hydrogel stability, flexible proteins, particle size
MeSH terms
Acylation, Gels, Plant Proteins, Protein Conformation, Succinic Anhydrides, Hydrogels, Phaseolus, Protein Stability

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