Effect of curdlan on the gel properties and interactions of whey protein isolate gels
Abstract
This study investigated the influence of curdlan on the gel properties of whey protein isolate (WPI). Results demonstrated that curdlan significantly improved the water-holding capacity, gel strength and rheological properties of the WPI gels. Moreover, it promoted the unfolding of the molecular structures of WPI, which was manifested by the transition from α-helix to β-sheet, an increase in free sulfhydryl content and a decrease in surface hydrophobicity. Furthermore, 4 % curdlan promoted the formation of WPI with uniform and compact elastic gel network structures, primarily attributed to disulphide bonds, hydrogen bonds and hydrophobic interactions. However, when the addition of curdlan exceeds 4 %, excessive entanglement of curdlan chains and steric hindrance effects hinder the unfolding and folding of protein structures, weaken their interaction, result in a loose network structure and affect the gel properties. In conclusion, this study demonstrates that curdlan can effectively improve the gelling properties of WPI, suggesting its potential application in low-calorie gel-based dairy products.
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Compared to the group without chitosan, the emulsion gels with chitosan had higher β-carotene bioaccessibility, which may be because the promotion of lipid digestion by chitosan facilitated the release of β-carotene and its subsequent incorporation into mixed micelles-an essential step for intestinal absorption.
“Compared to the group without chitosan, the emulsion gels with chitosan had higher β‐carotene bioaccessibility, which may because the promotion of lipid digestion by chitosan facilitated the release of β‐carotene and its subsequent incorporation into mixed micelles‐an essential step for intestinal absorption”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Y. Hu, Wang, et al. 2024
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Liu, M., Shan, S., Gao, X., Shi, Y., & Lu, W. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124344 · Cited by 115 · see citing works
Xu, Y., Liang, X., Kong, B., Sun, F., Xia, X., Zhang, H., Liu, Q., & Cao, C. (2024) · Food Research International · doi:10.1016/j.foodres.2024.114115 · Cited by 45 · see citing works
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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
- Authors
- Hu, W., Xu, X., Wang, X., Ma, T., Li, Y., Qin, X., Wei, J., & Chen, S.
- Affiliations
- Guangxi University (CN)
- Foshan University (CN)
- Corresponding author
- Chen, Shan
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2024-10
- Volume
- 277
- Issue
- Pt 3
- Pages
- 134161
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W4400943728
- Cited by
- 61
- References
- 2
- Citations by year
- 2026: 23 · 2025: 33 · 2024: 5
- FWCI
- 11.93
- 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 (32260561)
- 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
- curdlan, whey protein isolate, protein gels, water holding capacity, gel strength, rheological properties, protein secondary structure, disulfide bonds, hydrogen bonding, hydrophobic interactions, gel network structure, steric hindrance
- MeSH terms
- Whey Proteins, Gels, Hydrogen Bonding, Rheology, Water, beta-Glucans, Hydrophobic and Hydrophilic Interactions
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