Improvement of gel properties of low-salt shrimp (Litopenaeus vannamei) surimi by sodium alginate: Effect of mannuronic acid/guluronic acid ratios
Abstract
The impact of different mannuronic acid (M)/guluronic acid (G) ratios (2:1, 1:1, and 1:2) in sodium alginate (SA) on the gel properties of low-salt whiteleg shrimp surimi was investigated, and the corresponding mechanism was elucidated in this study. The results showed that all three types of SA (M-block dominant, M/G balanced, and G-block dominant) could improve the texture characteristics of low-salt shrimp surimi gel (SSG), strongly modulated by the M/G ratio. As the G content of the SA increased, the gel strength, hardness, and storage modulus of low-salt SSG were significantly enhanced (P < 0.05). After adding SA at the M/G ratio of 1:2, the highest water holding capacity (86.13 %) and the lowest cooking loss (1.16 %) were observed in the low-salt SSG. These phenomena could be attributed to the structural differences between the M unit (with an equatorial C5 carboxyl group, flexible) and the G unit (with an axial C5 carboxyl group, rigid) of SA. SA with high G content had a superior ability to construct a rigid network, which restricted protein mobility, increased the probability of protein-protein interactions, and thereby promoted protein cross-linking and disulfide bond formation. Meanwhile, the protein conformation in the low-salt SSG changed from α-helix to β-sheet after adding SA. These effects collectively contributed to forming a dense gel network, leading to better texture and water retention capacity of low-salt SSG. In conclusion, the M and G components of SA play crucial roles in establishing the protein-polysaccharide network, which is essential for developing high-quality low-salt SSG.
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Increased disulfide bonds consistently correlate with higher gel strength, G′/G′′ and water holding capacity, whereas reduced disulfide bond formation typically results in a weaker gel matrix.
“The increased disulfide bonds consistently correlate with higher gel strength, G′/G″ and water holding capacity (WHC), whereas the reduced disulfide bond formation typically results to a weaker gel matrix (M. Liu, Shan, et al. 2023; Teng et al. 2024; Song et al. 2025).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Song et al. 2025
Disulfide bonds exhibit a strong positive association with gel mechanical properties.
“Notably, disulfide bonds exhibit a strong positive association with gel mechanical properties.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Song et al. 2025
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- Authors
- Song, H.-L., Wang, Y.-Q., Zhang, Q., Liu, Y., Zhang, L.-D., Yan, J.-N., Lai, B., Wang, C., & Wu, H.-T.
- Affiliations
- Dalian Polytechnic University (CN)
- Corresponding author
- Wang, Ce
- Wu, Hai-Tao
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2025-11
- Volume
- 330
- Issue
- Pt 1
- Pages
- 148037
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W4414830283
- Cited by
- 13
- References
- 64
- Citations by year
- 2026: 11 · 2025: 2
- FWCI
- 6.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- International Journal of Biological Macromolecules (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (U22A20538, 32402148)
- 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
- sodium alginate, gel properties, gel strength, water holding capacity, cooking loss, protein cross-linking, disulfide bond formation, protein conformation, Litopenaeus vannamei, texture
- MeSH terms
- Alginates, Animals, Gels, Hexuronic Acids, Water, Penaeidae
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