Formation of a structured clot during the gastric digestion of milk: Impact on the rate of protein hydrolysis

Ye, Aiqian; Cui, Jian; Dalgleish, Douglas G.; Singh, Harjinder

doi:10.1016/j.foodhyd.2015.07.023

Cited by 127 publications

(82 citation statements)

References 41 publications

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“…These bands are attributable to the chymotrypsin (molecular mass of 25 kDa) and trypsin (molecular mass of 23.5 kDa) that were added in the intestinal digestion stage. Our results regarding the rate of the gastrointestinal breakdown of the caseins are in line with our previous studies [15,20,24] and with the literature [37,38]. To test the influence of loaded PTX or TQD on the digestibility of rCM, both PTX-rCM and TQD-rCM (6:1 and 4:1 drug:CN molar ratio, respectively) breakdown during simulated digestion was studied using SDS-PAGE.…”

Section: Protein Degradation By In Vitro Simulated Digestionsupporting

confidence: 89%

Re-assembled Casein Micelles for Oral Delivery of Chemotherapeutic Combinations to Overcome Multidrug Resistance in Gastric Cancer

2018

J Mol Clin Med.

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Multidrug resistance (MDR) mediated by ATP-dependent efflux transporters continues to be a dominant obstacle towards curative cancer therapy. We have previously demonstrated the ability of β-casein micelles (β-CM) to orally deliver a combination of individually encapsulated hydrophobic cargo of drugs and chemosensitizers designed to overcome MDR in gastric cancer. Herein we investigated the potential of reassembled casein micelles (rCM) to serve as a target-activated delivery platform comprising a synergistic duo of a chemotherapeutic drug (paclitaxel) and a P-glycoprotein-specific transport inhibitor (tariquidar). The high binding affinity of paclitaxel and tariquidar to rCM was demonstrated by spectrofluorometry. Furthermore, solubilization of the drugs and suppression of crystal growth was shown by light microscopy and dynamic light scattering. A remarkable antitumor activity and complete MDR reversal were demonstrated in the in vitro cytotoxicity assay against MDR human gastric carcinoma cells overexpressing P-glycoprotein. The structure and cytotoxic activity of drug-loaded rCM were completely retained after freeze-drying and reconstitution as in β-CM. Hence, our findings highlight the great potential of casein-based nanovehicles as efficient platforms for oral delivery and local target-activated release of synergistic hydrophobic drug combinations to treat gastric cancer, and overcome of cancer chemoresistance, and for the possible treatment of non-malignant gastric disorders.

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Section: Protein Degradation By In Vitro Simulated Digestionsupporting

confidence: 89%

Re-assembled Casein Micelles for Oral Delivery of Chemotherapeutic Combinations to Overcome Multidrug Resistance in Gastric Cancer

2018

J Mol Clin Med.

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“…Both may result in a slower digestion of caseins compared to whey proteins. 33,34 In line with this, Picariello et al 35 reported that traces of β-lactoglobulin and α-lactalbumin survive simulated gastrointestinal digestion; however, they stated that there is a high degree of protein hydrolysis based on the protein sequence recovery. It has thus repeatedly been observed in both animal and in vitro studies that the number of whey protein-derived peptides is lower than the number of casein-derived peptides.…”

Section: Peptide Formation and Average Peptide Lengthmentioning

confidence: 88%

Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release

et al. 2020

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“…The protein hydrolysis sites of pepsin are different from those of the intestinal proteases (mainly trypsin and chymotrypsin). Pepsin acts preferentially on κ-casein on the casein micelles, leading to the coagulation of the casein fraction of milk proteins under acidic conditions, whereas the whey protein fraction remains soluble ( 107 ). Thus, the early role played by the stomach in milk digestion is an essential step in regulating the rate of digestion of the milk proteins in the gastrointestinal tract ( 108 ).…”

Section: Milk Digestionmentioning

confidence: 99%

“…Not only protein composition and (or) casein micelle structure, but also different processing temperature and time combinations may induce differences in the curd structure in the stomach, which may influence the rate of delivery of proteins to the small intestine and their subsequent absorption. For instance, Ye et al ( 107 ) studied the dynamic gastric digestion behavior of raw and heated (90°C for 20 min) cattle skim milk using an HGS. The HGS is a dynamic stomach model that is capable of simulating the stomach contraction forces and the flow of gastric fluids that occur in vivo ( 144 ).…”

Section: Milk Digestionmentioning

confidence: 99%

Composition, Structure, and Digestive Dynamics of Milk From Different Species—A Review

et al. 2020

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Background: The traditional dairy-cattle-based industry is becoming increasingly diversified with milk and milk products from non-cattle dairy species. The interest in non-cattle milks has increased because there have been several anecdotal reports about the nutritional benefits of these milks and reports both of individuals tolerating and digesting some non-cattle milks better than cattle milk and of certain characteristics that non-cattle milks are thought to share in common with human milk. Thus, non-cattle milks are considered to have potential applications in infant, children, and elderly nutrition for the development of specialized products with better nutritional profiles. However, there is very little scientific information and understanding about the digestion behavior of non-cattle milks. Scope and Approach: The general properties of some non-cattle milks, in comparison with human and cattle milks, particularly focusing on their protein profile, fat composition, hypoallergenic potential, and digestibility, are reviewed. The coagulation behaviors of different milks in the stomach and their impact on the rates of protein and fat digestion are reviewed in detail. Key findings and Conclusions: Milk from different species vary in composition, structure, and physicochemical properties. This may be a key factor in their different digestion behaviors. The curds formed in the stomach during the gastric digestion of some non-cattle milks are considered to be relatively softer than those formed from cattle milk, which is thought to contribute to the degree to which non-cattle milks can be easily digested or tolerated. The rates of protein and fat delivery to the small intestine are likely to be a function of the macro- and micro-structure of the curd formed in the stomach, which in turn is affected by factors such as casein composition, fat globule and casein micelle size distribution, and protein-to-fat ratio. However, as no information on the coagulation behavior of non-cattle milks in the human stomach is available, in-depth scientific studies are needed in order to understand the impact of compositional and structural differences on the digestive dynamics of milk from different species.

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Formation of a structured clot during the gastric digestion of milk: Impact on the rate of protein hydrolysis

Cited by 127 publications

References 41 publications

Re-assembled Casein Micelles for Oral Delivery of Chemotherapeutic Combinations to Overcome Multidrug Resistance in Gastric Cancer

Re-assembled Casein Micelles for Oral Delivery of Chemotherapeutic Combinations to Overcome Multidrug Resistance in Gastric Cancer

Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release

Composition, Structure, and Digestive Dynamics of Milk From Different Species—A Review

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