Digestion of food proteins: the role of pepsin

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dc.contributor.authorYang, MXen_AU
dc.contributor.authorYang, Zen_AU
dc.contributor.authorEverett, DWen_AU
dc.contributor.authorGilbert, EPen_AU
dc.contributor.authorSingh, Hen_AU
dc.contributor.authorYe, AQen_AU
dc.date.accessioned2025-03-06T04:04:41Zen_AU
dc.date.available2025-03-06T04:04:41Zen_AU
dc.date.issued2025-01-21en_AU
dc.date.statistics2025-02-26en_AU
dc.description.abstractThe 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. © 2025 The Author(s). Published with license by Taylor & Francis Group, LLC. This is an open access article distributed under the terms of the Creative Commons attribution-nonCommercial-noderivatives license.en_AU
dc.description.sponsorshipThe authors would like to acknowledge the New Zealand Milks Mean More (NZ3M) program and the Riddet Institute Centre of Research Excellence, Tertiary Education Commission, New Zealand for financial support. Mengxiao Yang thanks the Australian Institute of Nuclear Science and Engineering (AINSE) for a Postgraduate Research Award.en_AU
dc.format.mediumPrint-Electronicen_AU
dc.identifier.citationYang, M., Yang, Z., Everett, D. W., Gilbert, E. P., Singh, H., & Ye, A. (2025). Digestion of food proteins: the role of pepsin. Critical Reviews in Food Science and Nutrition, 1-22. doi:10.1080/10408398.2025.2453096en_AU
dc.identifier.issn1040-8398en_AU
dc.identifier.issn1549-7852en_AU
dc.identifier.issueahead-of-printen_AU
dc.identifier.journaltitleCritical Reviews in Food Science and Nutritionen_AU
dc.identifier.pagination1-22en_AU
dc.identifier.urihttps://doi.org/10.1080/10408398.2025.2453096en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/16020en_AU
dc.identifier.volumeahead-of-printen_AU
dc.languageEnglishen_AU
dc.language.isoenen_AU
dc.publisherTaylor & Francisen_AU
dc.subjectFooden_AU
dc.subjectProteinsen_AU
dc.subjectPepsinen_AU
dc.subjectDigestionen_AU
dc.subjectNutritionen_AU
dc.subjectAmino acidsen_AU
dc.subjectHydrolysisen_AU
dc.subjectAmino acidsen_AU
dc.subjectGastrointestinal tracten_AU
dc.titleDigestion of food proteins: the role of pepsinen_AU
dc.typeJournal Articleen_AU
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