Digestion of food proteins: the role of pepsin
Open accessAbstract
The nutritive value of a protein is determined not only by its amino acid composition, but also by its digestibility in the gastrointestinal tract. The interaction between proteins and pepsin in the gastric stage is the first step and plays an important role in protein hydrolysis. Moreover, it affects the amino acid release rates and the allergenicity of the proteins. The interaction between pepsin and proteins from different food sources is highly dependent on the protein species, composition, processing treatment, and the presence of other food components. Coagulation of milk proteins under gastric conditions to form a coagulum is a unique behavior that affects gastric emptying and further hydrolysis of proteins. The processing treatment of proteins, either from milk or other sources, may change their structure, interactions with pepsin, and allergenicity. For example, the heat treatment of milk proteins results in the formation of a looser curd in the gastric phase and facilitates protein digestion by pepsin. Heated meat proteins undergo denaturation and conformational changes that enhance the rate of pepsin digestion. This review provides new ideas for the design of food products containing high protein concentrations that optimize nutrition while facilitating low allergenicity for consumers.
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Digestive characteristics of protein gels significantly influence the release of nutrients and delivery of bioactive ingredients.
“Digestive characteristics of protein gels significantly influence the release of nutrients and delivery of bioactive ingredients (M. Yang, Yang, et al. 2025).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Yang, Yang, et al. 2025
Plant-animal protein composite gels have gathered significant interest in development of high-protein food products, owing to potential to combine functional advantages of both protein sources.
“Plant–animal protein composite gels have gathered significant interest in the development of high‐protein food products, owning to their potential to combine the functional advantages of both protein sources (M. Li, Zhou, et al. 2025; M. Yang, Yang, et al. 2025).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Yang, Yang, et al. 2025
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- Authors
- Yang, M., Yang, Z., Everett, D. W., Gilbert, E. P., Singh, H., & Ye, A.
- Affiliations
- Riddet Institute (NZ)
- University of Hawaiʻi at Mānoa (US)
- Australian Nuclear Science and Technology Organisation (AU)
- Corresponding author
- Ye, Aiqian
- Venue
- Critical Reviews in Food Science and Nutrition
- Publisher
- Informa UK Limited
- Published
- 2025-01-21
- Volume
- 65
- Issue
- 30
- Pages
- 6919-6940
- ISSN
- 1040-8398 (ISSN-L)
- 1549-7852
- OpenAlex
- W4406666594
- Cited by
- 65
- References
- 269
- Citations by year
- 2026: 41 · 2025: 24
- FWCI
- 5.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Critical Reviews in Food Science and Nutrition (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- The Australian Nuclear Science and Technology Organisation Institutional Repository (The Australian Nuclear Science and Technology Organisation) (submittedVersion, cc-by-nc-nd)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
- Keywords
- pepsin, proteolysis, gastric phase, protein digestibility, protein allergenicity, amino acid release, protein processing
- MeSH terms
- Meat Proteins, Amino Acids, Animals, Dietary Proteins, Digestion, Food Handling, Food Hypersensitivity, Humans, Hydrolysis, Milk Proteins, Nutritive Value, Pepsin A
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