Various factors affecting the gel properties of surimi: A review
Open accessAbstract
As an important aquatic prepared food, surimi products are favored by consumers due to their unique viscoelastic properties and high nutritional value. Gel properties are the main indicators to measure the quality of surimi products. The gelation of surimi mainly involves intramolecular (conformational change) and intermolecular (chemical force) changes. Factors such as processing treatments, raw fish species and exogenous additives affect surimi protein structure, chemical forces and endogenous enzyme activities, which further affect the gel properties of surimi products. This review focuses on the mechanism of surimi heat‐induced gel, mainly including protein chain expansion and aggregation through various chemical forces to form a three‐dimensional network structure. In addition, the mechanism and application of different factors on the gel properties of surimi were also discussed, providing a reference for the selection of fish species, the control of heating conditions in the gel process of surimi products, the selection of additives and other measures to improve the gel performance.
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Several research studies have reported contradictory conclusions regarding the dominant molecular interaction and their roles in protein gels.
“Several research studies have reported contradictory conclusions regarding the dominant molecular interaction and their roles in protein gels.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Xie et al. 2024
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Tan, Y., Sun, P., Zhang, X., Zhang, H., Man, H., & Li, D. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110462 · Cited by 43 · see citing works
Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion
Dong, X., Wang, Y., Chen, X. D., & Selomulya, C. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70424 · Cited by 17 · see citing works
“For example, one review suggests that disulfide bond is the primary molecular force in surimi protein gels that determines gel strength (Xie et al. 2024 ).”
- Authors
- Xie, D., Tang, Y., & Dong, G.
- Affiliations
- Nanchang University (CN)
- Shenzhen University (CN)
- Corresponding author
- Xie, Dongfei
- Tang, Yu
- ORCID
- Venue
- Journal of Texture Studies
- Publisher
- Wiley
- Published
- 2024-06
- Volume
- 55
- Issue
- 3
- Pages
- e12847-e12847
- ISSN
- 0022-4901 (ISSN-L)
- 1745-4603
- OpenAlex
- W4400052223
- Cited by
- 39
- References
- 0
- Citations by year
- 2026: 17 · 2025: 18 · 2024: 4
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Texture Studies (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- surimi, gel properties, heat-induced gelation, fish protein, protein conformation, intermolecular interactions, protein aggregation, protein network structure, exogenous additives, endogenous enzymes, viscoelasticity
- MeSH terms
- Animals, Fish Products, Fishes, Food Handling, Gels, Hot Temperature, Humans, Nutritive Value, Viscosity, Fish Proteins
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