Mechanistic study on in vitro disintegration and proteolysis of whey protein isolate gels: Effect of the strength of sodium ions
Abstract
In this study, the influence of the strength of sodium ions on the mechanical properties, microstructure and proteolysis of whey protein isolate (WPI) gels during in vitro gastrointestinal digestion was investigated. The results showed that heat treatment of 15% (w/v) WPI solutions in the presence of 0–0.1 M NaCl resulted in fine-stranded gels with a smaller coarseness length scale, while the presence of higher salt concentrations (0.15–0.5 M) induced coarse-stranded gels with larger particle sizes of the protein aggregates. The elastic shear modulus was found to increase with increasing NaCl concentration, followed by a reduction under higher ionic strength. During in vitro gastrointestinal digestion, the kinetics of disintegration of all the gels were dominated by a surface erosion mechanism. The half disintegration time (t₁/₂) significantly increased from 136.2 min to 416.0 min with the increase of NaCl concentration from 0 to 0.5 M, respectively. The coarse-stranded gels were more resistant to digestion with less mass loss and a lower rate and extent of proteolysis throughout the in vitro digestion than the fine-stranded gels. This could be attributed to the limited swelling and more severe protein aggregation found in the coarser gels with more compact structures, which would retard the accessibility of acids and enzymes during digestion. The present work has provided mechanistic insights into the microstructural changes induced by sodium salts on disintegration and proteolysis of WPI gels during in vitro digestion. This is meaningful for future designing protein-based structured food products with designated digestion rates for targeted dietary demands.
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The coarse chain structure of whey protein gel with severe protein aggregation exhibited limited swelling/moisture absorption and delayed gel breakdown during digestion, significantly inhibiting protein digestion.
“The coarse chain structure of whey protein gel with severe protein aggregation exhibited limited swelling/moisture absorption and delayed gel breakdown during digestion, significantly inhibiting the digestion of protein”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as X. Dong et al. 2022
With increase of NaCl (0-0.5 M), the microstructure of WPI gels transformed from fine-strand structure to coarse-strand structure.
“With the increase of NaCl (0–0.5 M), the microstructure of WPI gels transformed from fine‐strand structure to coarse‐strand structure.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as X. Dong et al. 2022
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- Authors
- Dong, X., Wu, P., Cong, H., & Chen, X. D.
- Affiliations
- Xiamen University (CN)
- Soochow University (CN)
- Corresponding author
- Wu, Peng
- Chen, Xiao Dong
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2022-11
- Volume
- 132
- Pages
- 107862
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W4281733608
- Cited by
- 33
- References
- 47
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 5 · 2023: 5 · 2022: 1
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Hydrocolloids (publishedVersion)
- Funders
- National Natural Science Foundation of China (22078212)
- Natural Science Research of Jiangsu Higher Education Institutions of China (19KJD550001)
- 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
- whey protein isolate, protein gels, sodium chloride, ionic strength, gel microstructure, proteolysis, in vitro digestion, surface erosion, protein aggregation, elastic shear modulus, heat treatment (food and biological processing), digestion rate
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