Intragastric restructuring dictates the digestive kinetics of heat-set milk protein gels of contrasting textures

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dc.citation.volume195
dc.contributor.authorLi S
dc.contributor.authorMungure T
dc.contributor.authorYe A
dc.contributor.authorLoveday SM
dc.contributor.authorEllis A
dc.contributor.authorWeeks M
dc.contributor.authorSingh H
dc.coverage.spatialCanada
dc.date.accessioned2024-10-02T20:36:30Z
dc.date.available2024-10-02T20:36:30Z
dc.date.issued2024-11
dc.description.abstractThe gelation of milk proteins can be achieved by various means, enabling the development of diverse products. In this study, heat-set milk protein gels (15 % protein) of diverse textures were made by pH modulation and two gels were selected for dynamic in vitro gastric digestion: a spoonable soft gel (SG, pH 6.55' G' of ∼100 Pa) and a sliceable firm gel (FG, pH 5.65; G' of ∼7000 Pa). The two gels displayed markedly different structural changes and digestion kinetics during gastric digestion. The SG underwent substantial structural compaction during the first 120 min of gastric digestion into a denser and firmer gastric chyme (26.3 % crude protein, G* of ∼8500 Pa) than the chyme of the FG (15.7 % crude protein, G* of ∼3000 Pa). These contrasting intragastric structural changes of the gels reversed their original textural differences, which led to slower digestion and gastric emptying of proteins from the SG compared with the FG. The different intragastric pH profiles during the digestion of the two gels likely played a key role by modulating the proteolytic activity and specificity (to κ-casein) of pepsin. Preferential early cleavage of κ-casein in SG stimulated coagulation and compaction of solid chyme, whereas rapid hydrolysis of αS- and β-caseins in the FG weakened coagulation. This study provided new insights into controlling the structural development of dairy-based foods during gastric digestion and modulating digestion kinetics.
dc.description.confidentialfalse
dc.edition.editionNovember 2024
dc.format.pagination114944-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/39277222
dc.identifier.citationLi S, Mungure T, Ye A, Loveday SM, Ellis A, Weeks M, Singh H. (2024). Intragastric restructuring dictates the digestive kinetics of heat-set milk protein gels of contrasting textures.. Food Res Int. 195. (pp. 114944-).
dc.identifier.doi10.1016/j.foodres.2024.114944
dc.identifier.eissn1873-7145
dc.identifier.elements-typejournal-article
dc.identifier.issn0963-9969
dc.identifier.number114944
dc.identifier.piiS0963-9969(24)01014-7
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/71577
dc.languageeng
dc.publisherElsevier
dc.publisher.urihttps://www.sciencedirect.com/science/article/pii/S0963996924010147
dc.relation.isPartOfFood Res Int
dc.rights(c) The author/sen
dc.rights.licenseCC BYen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectFood structure
dc.subjectGastric restructuring
dc.subjectIn vitro digestion
dc.subjectMilk protein gels
dc.subjectProtein digestion
dc.subjectGels
dc.subjectDigestion
dc.subjectHydrogen-Ion Concentration
dc.subjectKinetics
dc.subjectMilk Proteins
dc.subjectHot Temperature
dc.subjectGastric Emptying
dc.subjectCaseins
dc.subjectPepsin A
dc.subjectAnimals
dc.subjectFood Handling
dc.subjectProteolysis
dc.titleIntragastric restructuring dictates the digestive kinetics of heat-set milk protein gels of contrasting textures
dc.typeJournal article
pubs.elements-id491329
pubs.organisational-groupOther
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