Gastric colloidal behaviour of milk protein as a tool for manipulating nutrient digestion in dairy products and protein emulsions

Ye, Aiqian

doi:10.1016/j.foodhyd.2021.106599

Cited by 53 publications

(26 citation statements)

References 132 publications

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“…Milk undergoes significant changes in its physicochemical and microstructural properties during gastric digestion (Mulet-Cabero et al, 2020a;Roy et al, 2020a;Ye et al, 2020). It has been suggested that such changes have an effect on the gastric emptying rates of different nutrients (such as proteins and fats) (Mulet-Cabero et al, 2020a;Huppertz and Chia, 2021;Ye, 2021), which may influence their subsequent rates of absorption in the small intestine (Montoya et al, 2018). Our previous in vitro studies on understanding the dynamic gastric digestion of the milk from different species (cow, goat, and sheep) have shown that all milks separate into a semi-solid curd (caseins) and a liquid (soluble nutrients such as whey) in a human gastric simulator.…”

Section: Introductionmentioning

confidence: 99%

Structural changes in milk from different species during gastric digestion in piglets

Roy

Moughan

et al. 2022

Journal of Dairy Science

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This study investigated the structural and physicochemical changes that occur in milk, a naturally designed complex structured emulsion, during gastric digestion using the bottle-fed piglet as an animal model. The gastric digestions of cow, goat, and sheep milk were compared in male piglets euthanized at different postfeeding times to collect the stomach chyme. The cow and noncow milks separated into curd (aggregated caseins) and liquid (mostly soluble whey) phases in the piglet's stomach. For milk from all the species, the curd remained longer in the stomach because of its slow disintegration, whereas the liquid phase emptied readily. The majority of the fat globules were found to be entrapped within the protein network of the curd. The rate of release of fat globules was strongly dependent on the breakdown of the surrounding protein network of the curd. The consistency of the gastric curds changed as digestion progressed, with goat and sheep milk curds having relatively softer curd consistency and less fused protein networks, especially toward the end of digestion. This might have led to the lower protein and fat retention in the goat and sheep milk curds and relatively faster gastric emptying of these nutrients from goat and sheep milk in comparison to cow milk. This in vivo study provided new and enhanced understanding of the mechanisms of the gastric digestion of milk from different species. It may have implications for developing bioinspired structures for the controlled digestion and delivery of nutrients.

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Section: Introductionmentioning

confidence: 99%

Structural changes in milk from different species during gastric digestion in piglets

Roy

Moughan

et al. 2022

Journal of Dairy Science

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“…As a result, numerous studies are focusing on employing lipid-based nanosystems to encapsulate curcumin, particularly nanoemulsions, to overcome these constraints (16)(17)(18). However, in the nanoemulsionbased milk formulation, the physicochemical interactions of nanoemulsion with milk proteins during processing and digestion within the gastrointestinal tract play an important role in the bioavailability of fortified bioactive compound (19).…”

Section: Introductionmentioning

confidence: 99%

Impact of Recombined Milk Systems on Gastrointestinal Fate of Curcumin Nanoemulsion

Qazi

Acevedo-Fani

et al. 2022

Front. Nutr.

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Milk powder is an important ingredient in various foods and pediatric formulations. The textural and digestion properties of the formulations depend on the preheat treatment of the milk powder during manufacture. Thus, it is interesting to know how these modifications can influence on the release of fortified bioactive compounds during digestion with a milk matrix. In this study, a curcumin nanoemulsion was incorporated into milks reconstituted from low-heat, medium-heat and high-heat skim milk powders (SMPs) and the milks were subjected to semi dynamic in vitro digestion. All the recombined milk systems formed a curd under gastric conditions, which reduced the gastric emptying of protein and curcumin-loaded oil droplets. Because of the formation of heat-induced casein/whey protein complexes, the open fragmented curd formed by the high-heat-treated reconstituted powder resulted in higher protein and oil droplets emptying to the intestine and higher curcumin bioaccessibility. This study provides useful information for how protein ingredients can govern the fate of added health-promoting compounds during digestion.

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“…It is well known that κ-CN on the surface of the casein micelles provides steric and electrostatic stabilization (Payens, 1979). The action of pepsin on the casein micelles involves 3 distinct phases (Huppertz and Chia, 2021): (1) specific hydrolysis of the Phe 105 -Met 106 bond of κ-CN by pepsin at pH >5 yielding the C-terminal glycosylated caseinomacropeptide and para-κ-CN; (2) aggregation of casein micelles by hydrophobic association together with ionic electrostatic effects (Horne and Lucey, 2014), which occurs when a minimum amount of the caseinomacropeptide has been removed (a critical degree of hydrolysis); and (3) progressive proteolysis where both caseins and whey proteins are hydrolyzed into peptides at pH <4 (Ye, 2021).…”

Section: Introductionmentioning

confidence: 99%

Kinetics of pepsin-induced hydrolysis and the coagulation of milk proteins

Yang

et al. 2022

Journal of Dairy Science

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Hydrolysis-induced coagulation of casein micelles by pepsin occurs during the digestion of milk. In this study, the effect of pH (6.7-5.3) and pepsin concentration (0.110-2.75 U/mL) on the hydrolysis of κ-casein and the coagulation of the casein micelles in bovine skim milk was investigated at 37°C using reverse-phase HPLC, oscillatory rheology, and confocal laser scanning microscopy. The hydrolysis of κ-casein followed a combined kinetic model of first-order hydrolysis and putative pepsin denaturation. The hydrolysis rate increased with increasing pepsin concentration at a given pH, was pH dependent, and reached a maximum at pH ~6.0. Both the increase in pepsin concentration and decrease in pH resulted in a shorter coagulation time. The extent of κ-casein hydrolysis required for coagulation was independent of the pepsin concentration at a given pH and, because of the lower electrostatic repulsion between para-casein micelles at lower pH, decreased markedly from ~73% to ~33% when pH decreased from 6.3 to 5.3. In addition, the rheological properties and the microstructures of the coagulum were markedly affected by the pH and the pepsin concentration. The knowledge obtained from this study provides further understanding on the mechanism of milk coagulation, occurring at the initial stage of transiting into gastric conditions with high pH and low pepsin concentration.

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Gastric colloidal behaviour of milk protein as a tool for manipulating nutrient digestion in dairy products and protein emulsions

Cited by 53 publications

References 132 publications

Structural changes in milk from different species during gastric digestion in piglets

Structural changes in milk from different species during gastric digestion in piglets

Impact of Recombined Milk Systems on Gastrointestinal Fate of Curcumin Nanoemulsion

Kinetics of pepsin-induced hydrolysis and the coagulation of milk proteins

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