Effect of ingestion temperature on the pepsin-induced coagulation and the in vitro gastric digestion behavior of milk

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dc.contributor.authorYang, MXen_AU
dc.contributor.authorYe, AQen_AU
dc.contributor.authorYang, Zen_AU
dc.contributor.authorEverett, DWen_AU
dc.contributor.authorGilbert, EPen_AU
dc.contributor.authorSingh, Hen_AU
dc.date.accessioned2023-06-29T06:17:43Zen_AU
dc.date.available2023-06-29T06:17:43Zen_AU
dc.date.issued2023-05en_AU
dc.date.statistics2023-03-10en_AU
dc.description.abstractPepsin-induced protein coagulation occurs in the gastric environment when the milk pH is above the isoelectric point of casein proteins. In this study, the effect of milk temperature (4–48 °C) on the hydrolysis of κ-casein by pepsin and the consequent protein coagulation was studied at pH 6.0 for 120 min. Quantitative determination of the released para-κ-casein showed that both the κ-casein hydrolysis reaction rate constant and the pepsin denaturation rate constant increased with an increase in temperature. The temperature coefficient (Q10) of the specific hydrolysis of κ-casein was calculated to be ∼1.95. The coagulation process was investigated by the evolution of the storage modulus (Gʹ). At higher temperature, the milk coagulated faster but had a lower firming rate and Gʹmax with larger aggregates and voids were observed. The digestion behavior of the milk ingested at 4 °C, 37 °C, or 50 °C was investigated for 240 min in a human gastric simulator, in which the milk temperature increased or decreased to 37 °C (body temperature) over ∼ 60 min. The coagulation of the 4 °C milk was slower than for the 37 °C and 50 °C milk. The curd obtained from the 4 °C milk had a looser and softer structure with a significantly higher moisture content at the initial stage of digestion (20 min) which, in turn, facilitated the breakdown and hydrolysis of the caseins by pepsin. During the digestion, the curd structure became more cohesive, along with a decrease in moisture content. The knowledge gained from this study provides insight into the effect of temperature on the kinetics of pepsin-induced milk coagulation and the consequent digestion behavior. © The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/bync- nd/4.0/).en_AU
dc.description.sponsorshipThis study was funded by the New Zealand Milks Mean More (NZ3M) program and the Riddet Institute Centre of Research Excellence, Tertiary Education Commission, New Zealand. The author Mengxiao Yang thanks the Australian Institute of Nuclear Science and Engineering (AINSE) for a Post Graduate Research Award. We would like to acknowledge the support of Michael Agnew (AgResearch Limited, New Zealand) for helping with the RP-phase HPLC and Claire Woodhall (Havelock North, New Zealand) for proofreading the manuscript.en_AU
dc.identifier.articlenumber108550en_AU
dc.identifier.citationYang, M., Ye, A., Yang, Z., Everett, D. W., Gilbert, E. P., & Singh, H. (2023). Effect of ingestion temperature on the pepsin-induced coagulation and the in vitro gastric digestion behavior of milk. Food Hydrocolloids, 139, 108550. doi:10.1016/j.foodhyd.2023.108550en_AU
dc.identifier.issn0268-005Xen_AU
dc.identifier.journaltitleFood Hydrocolloidsen_AU
dc.identifier.urihttps://doi.org/10.1016/j.foodhyd.2023.108550en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15071en_AU
dc.identifier.volume139en_AU
dc.language.isoenen_AU
dc.publisherElsevier B. V.en_AU
dc.relation.urihttps://doi.org/10.1016/j.foodhyd.2023.108550en_AU
dc.subjectTemperature rangeen_AU
dc.subjectPepsinen_AU
dc.subjectHydrolysisen_AU
dc.subjectMilken_AU
dc.subjectCoagulantsen_AU
dc.subjectDigestionen_AU
dc.subjectCaseinen_AU
dc.subjectKineticsen_AU
dc.titleEffect of ingestion temperature on the pepsin-induced coagulation and the in vitro gastric digestion behavior of milken_AU
dc.typeJournal Articleen_AU
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