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Digestion of food proteins: the role of pepsin.
(Taylor and Francis Group, 2025-01-21) Yang M; Yang Z; Everett DW; Gilbert EP; Singh H; Ye A
The 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.
Study Protocol for a Randomized Controlled Trial Investigating the Effects of the Daily Consumption of Ruminant Milk on Digestive Comfort and Nutrition in Older Women: The YUMMI Study.
(MDPI (Basel, Switzerland), 2024-12-06) Ong SP; Miller JC; McNabb WC; Gearry RB; Ware LM; Mullaney JA; Fraser K; Hort J; Bayer SB; Frampton CMA; Roy NC; Miranda JM
BACKGROUND: Age-related changes can lead to dietary insufficiency in older adults. The inclusion of high-quality, nutrient-dense foods such as ruminant milks can significantly improve health outcomes. However, many older adults worldwide do not meet daily milk intake recommendations because of digestive discomfort and health concerns. Ovine and caprine milks are increasingly popular for their perceived digestive and nutritional benefits. While preclinical studies suggest differences in milk digestion, human studies investigating acute postprandial responses remain inconclusive, and the impacts of sustained milk consumption remain uncertain. OBJECTIVES: Hence, we present a randomized controlled trial investigating how the sustained consumption of bovine, caprine, or ovine milk influences digestion, nutrition, and metabolism in older women. METHODS: A total of 165 healthy older women were randomized to receive bovine, caprine, or ovine milk, or no milk, twice daily for 12 weeks. The primary outcome is the impact of milk consumption on digestive comfort assessed via the Gastrointestinal Syndrome Rating Scale (GSRS). Secondary outcomes include changes in nutrient intake, plasma amino acid and lipid appearance, bowel habits, the gut microbiota, cardiometabolic health, physical function, physical activity, sleep, mood, sensory perception, and emotional response. CONCLUSIONS: The findings could inform dietary recommendations for older women and facilitate the development of targeted functional food products.
Requirement of digestible calcium at different dietary concentrations of digestible phosphorus for broiler chickens 3. Broiler finishers (d 25 to 35 post-hatch)
(y Elsevier Inc (USA), on behalf of Poultry Science Association Inc, 2023-04) David LS; Abdollahi MR; Bedford MR; Ravindran V
An experiment was conducted to determine the digestible calcium (Ca) and digestible phosphorous (P) requirements of 25 to 35-day-old broiler chickens. Fifteen corn-soybean meal-based diets containing 2.0, 2.5, 3.0, 3.5, and 4.0 g/kg standardized ileal digestible (SID) Ca and 2.5, 3.5, and 4.5 g/kg SID P were fed to broilers from d 25 to 35 post-hatch. Each experimental diet was randomly allocated to 6 replicate cages (8 birds per cage). Body weight and feed intake were recorded, and the feed conversion ratio was calculated. On d 35, birds were euthanized to collect the ileal digesta, tibia, and carcass for the determination of ileal Ca, and P digestibility, concentrations of ash, Ca, and P in tibia and the retention of Ca and P in the carcass. Titanium dioxide (5.0 g/kg) was included in all diets as an indigestible indicator for the ileal digestibility measurement. Feed intake and total excreta output were measured during the last 4 d of the experimental period for the measurement of apparent total tract retention of Ca and P. Fixed effects of the experiment were dietary concentrations of SID Ca and SID P and their interaction. If the interaction or main effects were significant (P < 0.05), the parameter estimates for second-order response surface model (RSM) were determined using General Linear Model procedure of SAS. The maximum response was not predicted for most of the parameters (including growth performance and tibia) as the Ca effect was linear which indicated that the highest level of Ca employed in the study may have not been high enough. The requirement of dietary SID Ca for maximization of these parameters, therefore, depends on the dietary SID P concentration when the dietary SID Ca is within 2.0 to 4.0 g/kg. However, based on the factorial analysis, the highest weight gain was observed at 3.5 g/kg SID P and 3.5 g/kg SID Ca concentrations. Tibia ash was higher in birds fed 4.5 g/kg SID P and was unaffected by dietary SID Ca concentrations. However, based on overall findings, a combination of 3.5 g/kg SID P and 3.0-3.5 g/kg SID Ca may be recommended for the optimum tibia ash. The recommended SID Ca requirements (at 3.5 g/kg SID P) for weight gain (3.5 g/kg or 6.4 g/kg total Ca) and tibia ash (3.0-3.5 g/kg or 5.5-6.4 g/kg total Ca) are lower than the current Ca recommendations (7.8 g/kg total Ca equivalent to 4.25 g/kg SID Ca; Ross, 2019) for broiler finishers, suggesting possible excess of Ca in diets formulated based on the current recommendation.
The impact of heating and drying on protease activities of ruminant milk before and after in vitro infant digestion
(Elsevier Ltd, 2023-12-15) Leite JAS; Montoya CA; Loveday SM; Mullaney JA; Loo TS; McNabb WC; Roy NC
This study investigated the effect of heating (63°C/30 min or 75°C/15 s) and drying (spray-drying or freeze-drying) on plasmin, cathepsin D, and elastase activities in bovine, ovine, and caprine milk, compared to non-dried raw milk counterparts. Protease activities and protein hydrolysis were assessed before and after in vitro infant digestion with or without gastric and pancreatic enzymes. At 75°C/15 s, plasmin activity in caprine and ovine milk decreased (69-75%, p<0.05), while cathepsin D activity in spray-dried bovine milk heated increased (2.8-fold, p<0.05). Plasmin and cathepsin D activities increased (<1.2-fold, p<0.05) after in vitro digestion with pancreatin, regardless of milk species. Endogenous milk enzymes hydrolyzed more proteins than gastric enzymes during gastric digestion and contributed to small intestinal digestion. In summary, milk proteases remained active after processing with effects dependent on the species of milk, and they contributed to in vitro protein hydrolysis in the stomach and small intestine.
The kinetics of amino acid disappearance in the small intestine is related to the extent of amino acids absorbed in growing pigs
(Cambridge University Press on behalf of The Nutrition Society, 2024-03-14) Montoya CA; van Bemmel M; Kreutz K; Hodgkinson SM; Stroebinger N; Moughan PJ
This study evaluated the importance of a correction for amino acids (AA) released into the hindgut on a measure of AA absorption kinetics and tested whether AA absorption kinetics are related to the extent of AA absorption using the growing pig as a model for humans. Thirty-six nine-week-old pigs (22·3 kg) received a diet containing whey protein as the sole protein source for 8 d. Pigs received their last meal containing the indigestible marker titanium dioxide before being euthanised at 1, 2, 3, 4, 6 and 12 h post-feeding. The entire content of each gastrointestinal tract (GIT) region was collected to determine AA released into the hindgut, and the kinetics and extent of AA absorption (uncorrected and corrected for AA entering the hindgut). Amounts of AA released into the hindgut increased over time (e.g. 33 and 180 mg of Glu for 4 and 6 h post-feeding). The corrected apparent amount of each AA absorbed from the GIT lumen after 4 h post-feeding was generally lower (P ≤ 0·05) than the uncorrected counterpart. Differences in both the kinetics and extent of AA absorption were observed across AA. For example, the time to reach half of the apparent AA absorption (T50) was 1·5 and 3·4 h for Met and Arg, respectively, whereas their extent of apparent absorption was 93 and 73 %. Negative correlations between parameters related to kinetics and the extent of apparent absorption were observed (e.g. for T50 r = -0·81; P < 0·001). The kinetics of AA absorption is related to the extent of AA absorption.
A proposed framework to establish in vitro-in vivo relationships using gastric digestion models for food research
(The Royal Society of Chemistry, 2024-10-21) Nadia J; Roy D; Montoya CA; Singh H; Acevedo-Fani A; Bornhorst GM
In vitro digestion methods have been utilized in food research to reduce in vivo studies. Although previous studies have related in vitro and in vivo data, there is no consensus on how to establish an in vitro-in vivo relationship (IVIVR) for food digestion. A framework that serves as a tool to evaluate the utility and limitations of in vitro approaches in simulating in vivo processes is proposed to develop IVIVRs for food digestion, with a focus on the gastric phase as the main location of food structural breakdown during digestion. The IVIVR consists of three quantitative levels (A, B, and C) and a qualitative level (D), which relate gastric digestion kinetic data on a point-to-point basis, parameters derived from gastric digestion kinetic data, in vitro gastric digestion parameters with in vivo absorption or appearance parameters, and in vitro and in vivo trends, respectively. Level A, B, and C IVIVRs can be used to statistically determine the agreement between in vitro and in vivo data. Level A and B IVIVRs can be utilized further evaluate the accuracy of the in vitro approach to mimic in vivo processes. To exemplify the utilization of this framework, case studies are provided using previously published static and dynamic gastric in vitro digestion data and in vivo animal study data. Future food digestion studies designed to establish IVIVRs should be conducted to refine and improve the current framework, and to improve in vitro digestion approaches to better mimic in vivo phenomena.
The impact of heat-set milk protein gel textures modified by pH on circulating amino acid appearance and gastric function in healthy female adults: a randomised controlled trial.
(Royal Society of Chemistry, 2024-05-21) Milan AM; Menting GGA; Barnett MPG; Liu Y; McNabb WC; Roy NC; Hutchings SC; Mungure T; Weeks M; Li S; Hort J; Calder S; O'Grady G; Mithen RF
Modification of dairy proteins during processing impacts structural assemblies, influencing textural and nutritional properties of dairy products, and release and availability of amino acids during digestion. By modifying only pH, acid heat-set bovine dairy gels with divergent textural properties were developed to alter protein digestion. In vitro assay confirmed faster digestion of protein from a firm gel (pH 5.65) versus a soft gel (pH 6.55). We hypothesised that firm gel (FIRM-G; pH 5.6) would result in greater indispensable amino acid (IAA) appearance in circulation over 5 h and corresponding differences in gastric myoelectrical activity relative to soft gel (SOFT-G; pH 6.2). In a randomised, single-blind cross-over trial, healthy females (n = 20) consumed 150 g of each gel; plasma amino acid appearance was assessed over 5 hours. Iso-nitrogenous, iso-caloric gels were prepared from identical mixtures of bovine milk and whey protein concentrates; providing 17.7 g (FIRM-G) and 18.9 g (SOFT-G) of protein per serving. Secondary outcomes included gastric myoelectrical activity measured by body surface gastric mapping, glycaemic, triglyceridaemic, and subjective appetite and digestive responses. Overall plasma IAA (area under the curve) did not differ between gels. However, plasma IAA concentrations were higher, and increased more rapidly over time after SOFT-G compared with FIRM-G (1455 ± 53 versus 1350 ± 62 μmol L-1 at 30 min, p = 0.024). Similarly, total, branched-chain and dispensable amino acids were higher at 30 min with SOFT-G than FIRM-G (total: 3939 ± 97 versus 3702 ± 127 μmol L-1, p = 0.014; branched-chain: 677 ± 30 versus 619 ± 34 μmol L-1, p = 0.047; dispensable: 2334 ± 53 versus 2210 ± 76 μmol L-1, p = 0.032). All other measured parameters were similar between gels. Peak postprandial aminoacidaemia was higher and faster following ingestion of SOFT-G. Customised plasma amino acid appearance from dairy is achievable by altering gel coagulum structure using pH during processing and may have minimal influence on related postprandial responses, with implications for targeting food design for optimal health. The Clinical Trial Registry number is ACTRN12622001418763 (https://www.anzctr.org.au) registered November 7, 2022.
Ileal Digestibility of Nitrogen and Amino Acids in Human Milk and an Infant Formula as Determined in Neonatal Minipiglets
(Elsevier Inc. on behalf of American Society for Nutrition, 2023-04) Charton E; Henry G; Cahu A; Le Gouar Y; Dahirel P; Moughan PJ; Montoya CA; Bellanger A; Dupont D; Le Huërou-Luron I; Deglaire A
BACKGROUND: Infant formula (IF) has to provide at least the same amount of amino acids (AAs) as human milk (HM). AA digestibility in HM and IF was not studied extensively, with no data available for tryptophan digestibility. OBJECTIVES: The present study aimed to measure the true ileal digestibility (TID) of total nitrogen and AAs in HM and IF to estimate AA bioavailability using Yucatan mini-piglets as an infant model. METHODS: Twenty-four 19-day-old piglets (males and females) received either HM or IF for 6 days or a protein-free diet for 3 days, with cobalt-EDTA as an indigestible marker. Diets were fed hourly over 6 h before euthanasia and digesta collection. Total N, AA, and marker contents in diets and digesta were measured to determine the TID. Unidimensional statistical analyses were conducted. RESULTS: Dietary N content was not different between HM and IF, while true protein was lower in HM (-4 g/L) due to a 7-fold higher non-protein N content in HM. The TID of total N was lower (P < 0.001) for HM (91.3 ± 1.24%) than for IF (98.0 ± 0.810%), while the TID of amino acid nitrogen (AAN) was not different (average of 97.4 ± 0.655%, P = 0.272). HM and IF had similar (P > 0.05) TID for most of the AAs including tryptophan (96.7 ± 0.950%, P = 0.079), except for some AAs (lysine, phenylalanine, threonine, valine, alanine, proline, and serine), with small significant difference (P < 0.05). The first limiting AA was the aromatic AAs, and the digestible indispensable AA score (DIAAS) was higher for HM (DIAASHM = 101) than for IF (DIAASIF = 83). CONCLUSION: HM, compared to IF, had a lower TID for total N only, whereas the TID of AAN and most AAs, including Trp, was high and similar. A larger proportion of non-protein N is transferred to the microbiota with HM, which is of physiological relevance, although this fraction is poorly considered for IF manufacturing.
Presence of Unabsorbed Free Amino Acids at the End of the Small Intestine Indicates the Potential for an Increase in Amino Acid Uptake in Humans and Pigs
(Elsevier Inc on behalf of American Society for Nutrition, 2023-03) van der Wielen N; de Vries S; Gerrits WJ; Lammers-Jannink K; Moughan PJ; Mensink M; Hendriks W
BACKGROUND: Unabsorbed free amino acids (AAs) at the end of the small intestine result in a potential preventable nutritional loss. OBJECTIVES: This study aimed to quantify free AAs in terminal ileal digesta of both humans and pigs to investigate its relevance for the nutritional value of food proteins. METHODS: Two studies with three diets were performed: a human study-ileal digesta from eight adult ileostomates were collected over 9 h after ingestion of a single meal unsupplemented or supplemented with 30 g zein or whey; pig study-12 cannulated pigs were fed for 7 d with a diet containing whey or zein or no-protein diet, and ileal digesta were collected on the last 2 d. Digesta were analyzed for total and 13 free AAs. True ileal digestibility (TID) of AAs was compared with and without free AAs. RESULTS: All terminal ileal digesta samples contained free AAs. The TID of AAs in whey was 97% ± 2.4% (mean ± SD) in human ileostomates and 97% ± 1.9% in growing pigs. If the analyzed free AAs would have been absorbed, TID of whey would increase by 0.4%-units in humans and 0.1%-units in pigs. The TID of AAs in zein was 70% ± 16.4% in humans and 77% ± 20.6% in pigs and would increase by 2.3%-units and 3.5%-units, respectively, if the analyzed free AAs would have been fully absorbed. The largest difference was observed for threonine from zein: if free threonine was absorbed, the TID would increase by 6.6%-units in both species (P < 0.05). CONCLUSIONS: Free AAs are present at the end of the small intestine and can potentially have a nutritionally relevant effect for poorly digestible protein sources, whereas the effect is negligible for highly digestible protein sources. This result provides insight into the room for improvement of a protein's nutritional value if all free AAs are to be absorbed. J Nutr 2023;xx:xx-xx. This trial was registered at clinicaltrials.gov as NCT04207372.
In vitro digestibility of dietary proteins and in vitro DIAAS analytical workflow based on the INFOGEST static protocol and its validation with in vivo data
(Elsevier Ltd, 2023-03-15) Sousa R; Recio I; Heimo D; Dubois S; Moughan PJ; Hodgkinson SM; Portmann R; Egger L
The FAO recommends the digestible indispensable amino acid score (DIAAS) to determine protein quality in foods, preferably tested in vivo. Here, the INFOGESTin vitrodigestion protocol was applied and supplemented with an analytical workflow allowing the assessment of protein digestibility and DIAAS calculation. The protocol was applied to selected samples WPI, zein, collagen, black beans, pigeon peas, All-Bran®, and peanuts. The total protein digestibility, digestibility of individual amino acids (AA), and DIAAS values were established and compared with in vivo data for the same substrates. Total protein digestibility (total Nitrogen, r = 0.7, P < 0.05; primary amines (OPA), r = 0.6, P < 0.02; total AA, r = 0.6, P < 0.02) and digestibility of individual AA (r = 0.6, P < 0.0001) were in good agreement, between in vitro and in vivo, with a mean difference of 1.2 %. In vitro DIAAS was highly correlated with DIAAS obtained from in vivo true ileal digestibility values (r = 0.96, R2 = 0.89, P < 0.0001) with a mean difference of 0.1 %.

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