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Food Research International (Ottawa,... Jan 2019In this work, the effects of maturation time and simulated gastrointestinal digestion on the molecular and peptide profiles of "Bresaola Valtellina" were assessed...
In this work, the effects of maturation time and simulated gastrointestinal digestion on the molecular and peptide profiles of "Bresaola Valtellina" were assessed through the foodomics approach, in this case food proteomics and peptidomics combined to other analytical and biological assays, aiming at depicting a holistic food quality. Human digestion of this Italian cured meat product was simulated using an in vitro static protocol and the degree of proteolysis and the in vitro bioactivity of the soluble free compounds in the digestates were evaluated by biochemical assays, e.g. SDS-PAGE, size exclusion HPLC, HPLC/MS, H NMR, enzymatic and antioxidant activities. The obtained results demonstrated that in vitro gastrointestinal digestion contributed to a considerable release of myofibrillar proteins by the muscle tissue. Data from SDS-PAGE, peptidomic and size exclusion HPLC assays showed that the in vitro digestion largely degraded proteins of muscle tissue to peptides smaller than 250 Da. The released peptides were likely responsible for the inhibitory activity on amylolytic enzymes and for the antioxidant properties elicited by the gastric digestates of Bresaola. Overall, the results demonstrated the negligible role of ripening in making meat proteins more bioaccessible, whereas they confirmed the highly in vitro digestibility of meat proteins from Bresaola. This study represents a new approach merging proteomics and foodomics to evaluate the effect of ripening and in vitro digestion on the bioactivity and bioaccessibility of proteins and peptides of meat products.
Topics: Antioxidants; Chromatography, High Pressure Liquid; Digestion; Electrophoresis, Polyacrylamide Gel; Food Analysis; Food Quality; Gastrointestinal Tract; Humans; Italy; Mass Spectrometry; Meat Products; Peptides; Proteins; Proteolysis; Proteomics
PubMed: 30599953
DOI: 10.1016/j.foodres.2018.11.021 -
Journal of Colloid and Interface Science Jul 2021This study aimed to understand the structural devolution of 10% w/w rennet-induced (RG) and transglutaminase-induced acid (TG) gels in HO and DO under in vitro gastric...
This study aimed to understand the structural devolution of 10% w/w rennet-induced (RG) and transglutaminase-induced acid (TG) gels in HO and DO under in vitro gastric conditions with and without pepsin. The real-time devolution of structure at a nano- (e.g. colloidal calcium phosphate (CCP) and micelle) and micro- (gel network) level was determined using ultra-small (USANS) and small-angle neutron scattering (SANS) with electron microscopy. Results demonstrate that gel firmness or elasticity determines disintegration behaviour during simulated mastication and consequently the particle size entering the stomach. Shear of mixing in the stomach, pH, and enzyme activity will also affect the digestion process. Our results suggest that shear of mixing primarily results in erosion at the particle surface and governs gel disintegration behaviour during the early stages of digestion. Pepsin diffusivity, and hence action, occur more readily in the latter stages of gastric digestion via access to the particle interior. This occurs via the progressively larger pores of the looser gel network and channels created within the larger, less dense casein micelles of the RG gels. Gel firmness and brittleness were greater in the DO samples compared to HO, facilitating gel disintegration. Despite the higher strength and elasticity of RG compared to TG, the protein network strands of the RG gels become more compact when exposed to the acidic gastric environment with comparatively larger pores observed through SEM imaging. This led to a higher degree of digestibility in RG gels compared to TG gels. This is the first study to examine casein gel structure during simulated gastric digestion using scattering and highlights the benefits of neutron scattering to monitor structural changes during digestion at multiple length scales.
Topics: Caseins; Digestion; Gels; Neutrons; Scattering, Small Angle; Stomach
PubMed: 33780761
DOI: 10.1016/j.jcis.2021.03.087 -
Journal of Animal Science Jan 2021Energy values and amino acid (AA) digestibility of dried yeast (DY) and soybean meal (SBM) were determined in 2 experiments with growing pigs. Experiment 1 was conducted...
Energy values and amino acid (AA) digestibility of dried yeast (DY) and soybean meal (SBM) were determined in 2 experiments with growing pigs. Experiment 1 was conducted to determine the digestible energy (DE) and metabolizable energy (ME) in DY and SBM. Thirty barrows with a mean initial body weight (BW) of 20.6 kg (SD = 1.04) were assigned to 5 dietary treatments in a randomized complete block design with period and BW as blocking factors. A reference diet was prepared with corn, canola meal, and soybean oil as energy-contributing ingredients. Four additional diets were prepared by adding 5% and 10% DY or SBM at the expense of energy-contributing ingredients in the reference diet. The ratio of corn, canola meal, and soybean oil was kept consistent across the experimental diets. Each experimental period consisted of 5-d adaptation and 5-d quantitative collection of feces and urine. Test ingredient-associated DE or ME intake (kcal/d) was regressed against test ingredient intake [kg dry matter (DM)/d] to estimate the DE or ME in test ingredients as the slope of linear regression model. The DE in DY was estimated at 3,933 kcal/kg DM, which was not different from the estimated DE in SBM at 4,020 kcal/kg DM. Similarly, there was no difference between DY and SBM in the estimated ME (3,431 and 3,756 kcal/kg DM, respectively). Experiment 2 was conducted to determine the standardized ileal digestibility (SID) of AA in DY and SBM. Twenty-one barrows with a mean initial BW of 20.0 kg (SD = 1.31) were surgically fitted with T-cannulas at the distal ileum and assigned to 3 dietary treatments in a randomized complete block design with BW as a blocking factor. Two semi-purified diets containing DY or SBM as the sole nitrogen source and one nitrogen-free diet (NFD) were prepared. The NFD was used to estimate the basal ileal endogenous losses of CP and AA. Pigs were fed the 3 diets for 5 d as adaptation, followed by 2 d of feeding with ileal digesta collection. The SID of AA, except Gly and Pro, in DY was less (P < 0.05) than in SBM. The SID of indispensable AA in DY ranged from 64.1% for Thr to 85.2% for Arg, and those in SBM ranged from 83.9% for Thr to 91.8% for Arg. In conclusion, energy values of DY are not different from those of SBM, whereas AA in DY is less digestible than in SBM. The estimated DE and ME as well as the SID of AA in DY and SBM can be used in diet formulation for growing pigs using these ingredients.
Topics: Amino Acids; Animal Feed; Animal Nutritional Physiological Phenomena; Animals; Diet; Digestion; Energy Metabolism; Ileum; Glycine max; Swine; Yeast, Dried
PubMed: 33515467
DOI: 10.1093/jas/skaa385 -
Poultry Science Nov 2020This study was aimed to investigate whether 1-deoxynojirimycin (DNJ) affects the digestion system of young geese and assess whether mulberry leaf, which contains this...
This study was aimed to investigate whether 1-deoxynojirimycin (DNJ) affects the digestion system of young geese and assess whether mulberry leaf, which contains this substance, has disadvantages that compromise its value as poultry feed. One hundred and twenty-eight 12-day-old male Wanxi white geese were randomly assigned into 4 treatment groups. The control group was fed an ordinary diet without DNJ. The other groups namely L-DNJ, M-DNJ, and H-DNJ had their basic diets supplemented with 0.05 mg/g, 0.1 mg/g, and 0.15 mg/g DNJ, respectively. The geese were fed for 6 wk, and the apparent digestibility test was conducted in the last week. Intestinal parameters, digestive organs, and enzymes were determined. 16S rRNA gene sequencing was conducted for cecal flora composition. The results revealed that DNJ decreased body and liver weight and increased feed conversion ratio in comparison with the control (P < 0.05); however, it did not influence the weight and length of the intestine or the pancreas weight. The utilization of organic matter, metabolizable energy, ether extract, acid detergent fiber, and calcium in feed were reduced in the M-DNJ and L-DNJ groups compared with those in the control (P < 0.05); however, the utilization of crude protein was increased in all DNJ-treated groups (P < 0.01). In the H-DNJ group, the usage of soluble phosphorus was also increased (P < 0.05). High-dose DNJ increased the activity of trypsin in the pancreas but reduced those of amylase (P < 0.05) and lipase (P > 0.05) in the pancreas and duodenum. The intestinal villi were short, even impaired, in DNJ-treated groups. High-throughput sequencing data revealed that DNJ supplement reduced the α-diversity indices of the cecal microbiota. The principal component analysis further suggested a difference in community structure between the DNJ treatment groups and control. High-dose DNJ increased the relative abundance of Bacteroides, Escherichia-Shigella, and Butyricicoccus but reduced that of unclassified Ruminococcaceae compared with the control (P < 0.05). In conclusion, changes in the digestive system caused by DNJ seriously affected the metabolism of nutrients in geese and reduced their growth performance. Attention should be paid to the adverse effects of DNJ when using mulberry leaves as poultry feed.
Topics: 1-Deoxynojirimycin; Animals; Bacteria; Digestion; Gastrointestinal Microbiome; Geese; Male; Morus; Plant Leaves; RNA, Ribosomal, 16S; Random Allocation
PubMed: 33142503
DOI: 10.1016/j.psj.2020.07.048 -
Advances in Nutrition (Bethesda, Md.) Aug 2022The recent Food and Agricultural Organization/World Health Organization/United Nations University expert consultations on protein requirements and quality have... (Review)
Review
The recent Food and Agricultural Organization/World Health Organization/United Nations University expert consultations on protein requirements and quality have emphasized the need for the new Digestible Indispensable Amino Acid Score (DIAAS), as a measure of protein quality. This requires human measurements of the true ileal digestibility of individual indispensable amino acids (IAAs) until the end of the small intestine. Digestibility is measured using standard oro-ileal balance methods, which can only be achieved by an invasive naso-ileal intubation in healthy participants or fistulation at the terminal ileum. Significant efforts have been made over the last 2 decades to develop noninvasive or minimally invasive methods to measure IAA digestibility in humans. The application of intrinsically labeled (with stable isotopes like 13C, 15N, and 2H) dietary proteins has helped in circumventing the invasive oro-ileal balance techniques and allowed the differentiation between endogenous and exogenous protein. The noninvasive indicator amino acid oxidation (IAAO) technique, which is routinely employed to measure IAA requirements, has been modified to estimate metabolic availability (a sum of digestibility and utilization) of IAA in foods, but provides an estimate for a single IAA at a time and is burdensome for participants. The recently developed minimally invasive dual isotope tracer method measures small intestinal digestibility of multiple amino acids at once and is suitable for use in vulnerable groups and disease conditions. However, it remains to be validated against standard oro-ileal balance techniques. This review critically evaluates and compares the currently available stable isotope-based protein quality evaluation methods with a focus on the digestibility and metabolic availability measurements in humans. In view of building a reliable DIAAS database of various protein sources and subsequently supporting protein content claims in food labeling, a re-evaluation and harmonization of the available methods are necessary.
Topics: Amino Acids; Amino Acids, Essential; Colonoscopy; Dietary Proteins; Digestion; Humans; Ileum; Isotopes
PubMed: 34755836
DOI: 10.1093/advances/nmab134 -
PloS One 2013The speed of protein digestion impacts on postprandial protein anabolism. After exercise or in the elderly, fast proteins stimulate protein synthesis more efficiently...
The speed of protein digestion impacts on postprandial protein anabolism. After exercise or in the elderly, fast proteins stimulate protein synthesis more efficiently than slow proteins. It has been shown that meat might be a source of fast proteins. However, cooking temperature, acting on the macrostructure and microstructure of the meat could affect both the speed, and efficiency, of protein digestion. This study aims to evaluate, in vivo, the effect of meat cooking on digestion parameters, in the context of a complete meal. Six minipigs fitted with an ileal cannula and an arterial catheter were used. In order to measure the true ileal digestibility, tested meat was obtained from a calf, the muscle proteins of which were intrinsically labelled with (15)N-amino acids. Three cooking temperatures (60, 75 and 95°C; core temperature for 30 min), and three levels of intake (1, 1.45, and 1.90 g protein/kg body weight) were tested. Following meat ingestion, ileal digesta and arterial blood were collected over a 9-h period. The speed of digestion, evaluated from the kinetics of amino acid appearance in blood within the first 3 h, was greater for the cooking temperature of 75°C, than for 60 or 95°C. The true ileal digestibility, which averaged 95%, was not affected by cooking temperature or by the level of meat intake. The amino acid composition of the digesta flowing at the ileum was not affected by cooking temperature. These results show that cooking temperature can modulate the speed of meat protein digestion, without affecting the efficiency of the small intestinal digestion, and consequently the entry of meat protein residues into the colon.
Topics: Amino Acids; Animals; Colon; Cooking; Dietary Proteins; Digestion; Eating; Female; Ileum; Kinetics; Meat; Nitrogen; Postprandial Period; Swine; Swine, Miniature; Temperature
PubMed: 23593443
DOI: 10.1371/journal.pone.0061252 -
The Journal of Nutrition Jan 2023The digestible indispensable amino acid score uses ileal digestibility of each indispensable amino acid (IAA) of a dietary protein to calculate its protein quality.... (Review)
Review
The digestible indispensable amino acid score uses ileal digestibility of each indispensable amino acid (IAA) of a dietary protein to calculate its protein quality. However, true ileal digestibility, which is the exclusive sum of digestion and absorption of a dietary protein up to the terminal ileum, is difficult to measure in humans. It is traditionally measured using invasive oro-ileal balance methods but can be confounded by endogenous secreted protein in the intestinal lumen, although the use of intrinsically labeled protein corrects for this. A recent, minimally invasive dual isotope tracer technique is now available to measure true IAA digestibility of dietary protein sources. This method involves simultaneous ingestion of 2 intrinsically but differently (stable) isotopically labeled proteins, a (H or N-labeled) test protein and (C-labeled) reference protein whose true IAA digestibility is known. Using a plateau-feeding protocol, the true IAA digestibility is determined by comparing the steady state ratio of blood to meal test protein IAA enrichment to the similar reference protein IAA ratio. The use of intrinsically labeled protein also distinguishes between IAA of endogenous and dietary origin. The collection of blood samples makes this method minimally invasive. As the α-N and α-H atoms of AAs of the intrinsically labeled protein are prone to label loss because of transamination, underestimation of digestibility, appropriate correction factors need to be employed when using N or H labeled test protein. The true IAA digestibility values of highly digestible animal protein by the dual isotope tracer technique are comparable to that measured by direct oro-ileal balance measurements, but no data are yet available for proteins with lower digestibility. A major advantage is that the minimally invasive method allows for true IAA digestibility measurement in humans across different age groups and physiological conditions.
Topics: Humans; Animals; Amino Acids; Digestion; Isotopes; Dietary Proteins; Diet; Ileum
PubMed: 36913451
DOI: 10.1016/j.tjnut.2022.11.017 -
Poultry Science Sep 2019Digestibility coefficients of nutrients, metabolizable energy (ME), net energy (NE) and the ratio of NE to ME (NE/ME) of 20 diets were measured in broiler chickens (1 to...
Digestibility coefficients of nutrients, metabolizable energy (ME), net energy (NE) and the ratio of NE to ME (NE/ME) of 20 diets were measured in broiler chickens (1 to 21 d). Dietary nutrients were formulated to keep similar ME/nutrient ratios, except for dietary protein, fat, and fiber using corn, soybean meal, animal protein blend, barley, poultry oil and an enzyme mixture of xylanase, glucanase, and phytase. Digestibility coefficients of nutrients and ME were measured in battery cages under free-access of feed, while NE was measured in floor pens feeding 75% of recommended ME intake each day. NE for maintenance was calculated on basis of mean metabolic weight using a coefficient from a previous study and NE for gain was calculated by body protein and fat gains using dual-energy x-ray absorptiometry. Digestibility coefficients of protein and neutral detergent fiber (NDF) were curvilinearly related to dietary protein and NDF, respectively, while digestibility coefficients of fat and starch were linearly correlated to dietary fat and starch, respectively. The inclusion of enzymes increased the digestion coefficient of NDF to predict the digestibility of protein, NDF, fat, and starch. MEn/gross energy ratio averaged 72.5% and was correlated to protein, fat, NDF, and starch. ME values were accurately predicted from chemical characteristics, where best equations were obtained from digestible nutrients. Energetic efficiencies of ME were 72% (NE/MEn) and 68% (NE/ME) and varied by about 20 and 18%, respectively. Ratios of energetic efficiency were 68% for digestible carbohydrates; 86% for digestible fat; and 76% (NE/MEn) and 59% (NE/ME) for digestible protein. According to the lowest residual standard deviation the best nutrient components to predict energy were digestible nutrients for predicting ME values (41 kcal/kg); digestible protein intake, fecal organic matter, and body fat and protein for predicting heat increment values (111 kcal/kg); and combination of ME and crude nutrient for predicting NE values (140 kcal/kg).
Topics: Animal Feed; Animal Nutritional Physiological Phenomena; Animals; Chickens; Diet; Digestion; Dose-Response Relationship, Drug; Energy Intake; Male; Nutrients; Random Allocation
PubMed: 30968142
DOI: 10.3382/ps/pez142 -
Journal of Animal Science Feb 2021Human-grade (HG) pet foods are commercially available, but they have not been well studied. Our objective was to determine the apparent total tract digestibility (ATTD)...
Human-grade (HG) pet foods are commercially available, but they have not been well studied. Our objective was to determine the apparent total tract digestibility (ATTD) of HG pet foods and evaluate their effects on fecal characteristics, microbiota, and metabolites, serum metabolites, and hematology of dogs. Twelve dogs (mean age = 5.5 ± 1.0; BW = 11.6 ± 1.6 kg) were used in a replicated 4 × 4 Latin square design (n = 12/treatment). The diets included 1) Chicken and Brown Rice Recipe (extruded; Blue Buffalo); 2) Roasted Meals Tender Chicken Recipe (fresh; Freshpet); 3) Beef and Russet Potato Recipe (HG beef; JustFoodForDogs); and 4) Chicken and White Rice Recipe (HG chicken; JustFoodForDogs). Each period consisted of 28 d, with a 6-d diet transition phase, 16 d of consuming 100% of the diet, a 5-d phase for fecal collection, and 1 d for blood collection. All data were analyzed using the Mixed Models procedure of SAS 9.4. Dogs fed the extruded diet required a higher (P < 0.05) daily food intake (dry matter basis, DMB) to maintain BW. The ATTD of dry matter (DM), organic matter (OM), energy, and acid-hydrolyzed fat (AHF) were greater (P < 0.05) in dogs fed the HG diets than those fed the fresh diet, and greater (P < 0.05) in dogs fed the fresh diet than those fed the extruded diet. Crude protein ATTD was lower (P < 0.05) for dogs fed the extruded diet than those fed all other diets. Dogs fed the extruded diet had greater (P < 0.05) fecal output (as-is; DMB) than dogs fed fresh (1.5-1.7 times greater) or HG foods (2.0-2.9 times greater). There were no differences in fecal pH, scores, and metabolites, but microbiota were affected by diet. Dogs fed HG beef had higher (P < 0.05) relative abundance of Bacteroidetes and lower (P < 0.05) relative abundance of Firmicutes than dogs fed the fresh or HG chicken diets. The Actinobacteria, Fusobacteria, Proteobacteria, and Spirochaetes phyla were unchanged (P > 0.05), but diet modified the relative abundance of nearly 20 bacterial genera. Similar to previous reports, these data demonstrate that the fecal microbiota of dogs fed HG or fresh diets is markedly different than those consuming extruded diets, likely due to ingredient, nutrient, and processing differences. Serum metabolites and hematology were not greatly affected by diet. In conclusion, the HG pet foods tested resulted in significantly reduced fecal output, were highly digestible, maintained fecal characteristics, serum chemistry, and hematology, and modified the fecal microbiota of dogs.
Topics: Animal Feed; Animal Nutritional Physiological Phenomena; Animals; Cattle; Diet; Digestion; Dogs; Feces; Gastrointestinal Tract; Humans; Microbiota; Nutrients
PubMed: 33511410
DOI: 10.1093/jas/skab028 -
Physiological Reviews Jan 2002The traditional understanding is that an entirely new complement of digestive enzymes is secreted by the pancreas into the small intestines with each meal. This is... (Review)
Review
The traditional understanding is that an entirely new complement of digestive enzymes is secreted by the pancreas into the small intestines with each meal. This is thought to be necessary because, like food itself, these enzymes are degraded during digestion. In this review we discuss experiments that bring this point of view into question. They suggest that digestive enzymes can be absorbed into blood, reaccumulated by the pancreas, and reutilized, instead of being reduced to their constituent amino acids in the intestines. This is called an enteropancreatic circulation of digestive enzymes.
Topics: Animals; Biological Transport; Digestion; Enzymes; Humans; Intestinal Mucosa; Pancreas
PubMed: 11773607
DOI: 10.1152/physrev.00022.2001