Cited by 26Proteins in Food SystemsPolysaccharides Composition and ApplicationsFood composition and properties

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Modulation of acid-induced pea protein gels by gellan gum and glucono-δ-lactone: Rheological and microstructural insights

Abstract

This study investigated the effect of gellan gum (GG) and glucono-δ-lactone (GDL) on the acid-induced gel properties of pea protein isolate (PPI) pretreated with media milling. The inclusion of GG substantially enhanced the gel hardness of PPI gel from 18.69 g to 792.47 g though slightly reduced its water holding capacity (WHC). Rheological analysis showed that GG increased storage modulus (G') and decreased damping factor of gels in the small amplitude oscillatory shear region and transformed its strain thinning behavior into weak strain overshoot behavior in the large amplitude oscillatory shear region. SEM revealed that GG transformed the microstructure of gel from a uniform particle aggregate structure to a chain-like architecture composed of filaments with small protein particles attached. Turbidity and zeta potential analysis showed that GG promoted the transformation of PPI from a soluble polymer system to an insoluble coagulant during acidification. When GG content was relatively high (0.2 %-0.3 %), high GDL content increased the electrostatic interaction between PPI and GG molecules, causing their rapid aggregation into a dense irregular aggregate structure, further enhancing gel strength and WHC. Overall, GG and GDL can offer the opportunity to modulate the microstructure and gel properties of acid-induced PPI gels, presenting potential for diversifying food gel design strategies through PPI-GG hybrid systems.

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Crossref · 10.1016/j.foodres.2024.114988

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  • Acid-induced gelation lowers pH, bringing proteins closer to their isoelectric point, leading to partial unfolding and aggregation, ultimately forming a gel.

    “Acid-induced gelation lowers the pH values, bringing proteins closer to their isoelectric point, leading to partial unfolding and aggregation, ultimately forming a gel (Galante et al. 2020;Xia et al. 2022;Li, Dai, et al. 2024).”

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

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Metadata

Authors
Li, C., Dai, T., Jiang, D., Zhang, G., Deng, L., Li, T., Liang, R., Dai, H., Fu, A., Liu, C., & Chen, J.
Affiliations
Nanchang University (CN)
Corresponding author
Chen, Jun
Venue
Food Research International
Publisher
Elsevier BV
Published
2024-11
Volume
195
Pages
114988
ISSN
0963-9969 (ISSN-L)
OpenAlex
W4401862728
Cited by
26
References
1
Citations by year
2026: 16 · 2025: 8 · 2024: 2
FWCI
5.57
Type
journal article
Language
en
Open access
closed
Locations
  • Food Research International (publishedVersion)
  • PubMed (publishedVersion)
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
  • Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
Keywords
pea protein isolate, gellan gum, glucono-δ-lactone, acid-induced gelation, protein gels, gel hardness, water holding capacity, gel microstructure, rheology, coagulation, electrostatic interactions, media milling
MeSH terms
Pea Proteins, Gels, Gluconates, Hydrogen-Ion Concentration, Lactones, Polysaccharides, Bacterial, Rheology

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