Comparison of the effect of Saccharomyces cerevisiae-Megasphaera elsdenii and buffer on growth performance, digestibility, ruminal histomorphometry, and carcass characteristics of fattening lambs in high concentrate diet.

This study aimed to investigate the effect of rumen pH-adjusting additives in the high-concentrated diet on functional traits, nutrient digestion, some meat parameters, and histomorphometry, and rumen histopathology. Twenty-four Arabia male lambs with 3 to 4 months old and initial body weight of 23.9 ± 3.15 kg were used in a completely randomized design with three treatments and eight replicates. The study was 77 days, including 14 days of the adaptation period and 63 days of the record taking and sampling period. The experimental treatments consisted of a control diet, control diet + sodium bicarbonate buffer, control diet + Megasphaera elsdenii, and Saccharomyces cerevisiae (bacterial-yeast). Rumen fluid was taken by stomach tube at 3 h after morning feeding to measure pH. The lambs were weighed every 3 weeks during the period, and the body weight changes, average daily gain, and total weight gain were measured, and the feed conversion ratio was calculated. At the end of the experiment, the lambs were slaughtered, and the longissimus dorsi muscle was prepared to determine the meat parameters. For histological studies, the abdominal rumen sac was sampled. There were no differences among treatments in dry matter intake (DMI), daily weight gain (ADG), and feed conversion ratio (P > 0.05). Propionate concentration was higher in the bacteria-yeast treatment than other treatments (P < 0.05). Protein digestibility was higher in control and bacteria-yeast treatments than buffer treatment (P < 0.05). The percentage of meat protein, carcass weight, and dressing percentage in bacterial-yeast treatment was higher than other treatments (P < 0.05). Rumen wall thickness in the buffer and bacterial-yeast receiving treatments was greater than the control treatment and was significant in the buffer treatment compared to the control treatment (P < 0.05). The thickness of rumen epithelial tissue in the buffer and bacterial-yeast recipient treatments was less than the control treatment (P < 0.05). Rumen papillae thickness was higher in the control treatment than other treatments (P < 0.05). Hydropic degeneration and parakeratosis were less in pH-regulating treatments than in control. The results showed that the use of Megasphaera elsdenii could be an effective way to modulate the ruminal fermentation conditions of lambs fed with high concentrate diets. In addition, to increaseing dressing percentage and meat protein, it can also reduce tissue damage and improve ruminal tissue structure.

Enzymatic treatment of pork protein for the enhancement of iron bioavailability.

The typical intervention for iron-deficiency anaemia is through oral supplementation with iron salts, which have unpleasant side effects. Therefore, there is a need for the development of supplements which will be absorbed more effectively and may have fewer side effects. This study investigated the effects of partially hydrolysed pork proteins on the bioavailability of non-haem iron. The peptides were derived using either pepsin or a combination of bacterial and fungal proteases, and their ability to deliver iron was evaluated in a rat intestine epithelial tissue model. The greatest iron absorption was achieved with peptides hydrolysed by pepsin of low molecular weight (<6-8 kDa). The peptides hydrolysed with bacterial and fungal enzymes may have bound to the iron too strongly, affecting bioavailability. Finally, hydrolysing proteins using pepsin in the presence of iron produces a complex that resulted in more ferritin expression than mixing the peptides with iron after hydrolysis.

Nutrimetabolomics: integrating metabolomics in nutrition to disentangle intake of animal-based foods.

Food intake and metabolization of foods is a complex and multi-facetted process that encompasses the introduction of new metabolite compounds in our body, initiation or alterations in endogenous metabolic processes and biochemical pathways, and likely also involving the activity of the gut microbial community that we host. The explorative nature of metabolomics makes it a superior tool for examining the whole response to food intake in a more thorough way and has led to the introduction of the term nutrimetabolomics. Protein derived from animal sources constitutes an important part of our diet, and there is therefore an interest in understanding how these animal-derived dietary sources influence us metabolically. This review aims to illuminate how the introduction of nutrimetabolomics has contributed to gain novel insight into metabolic and nutritional aspects related to intake of animal-based foods.

Tracking bioactive peptides and their origin proteins during the in vitro digestion of meat and meat products.

Existing reviews address bioactive peptides of meat proteins; however, comprehensive reviews summarizing the released sequences and their corresponding parent meat proteins in the digesta are limited. This review explores the bioactive peptides released during the in vitro gastrointestinal (GI) digestion of meat, connecting with parent proteins. The primary bioactivities of meat-derived peptides include angiotensin-converting enzyme (ACE) and dipeptidyl peptidase (DPP)-IV inhibition and antioxidant effects. Myofibrillar, sarcoplasmic, and stromal proteins play a significant role in peptide release during digestion. The release of bioactive peptides varies according to the parent protein and cryptides had short chains, non-toxicity, and great bioavailability and GI absorption scores. Moreover, the structural stability and bioactivities of peptides can be influenced by the digestive properties and amino acid composition of parent proteins. Investigating the properties and origins of bioactive peptides provides insights for enhancing the nutritional quality of meat and understanding its potential health benefits.

Carrageenan impact on digestive proteolysis of meat proteins in meatballs or soluble hydrolyzed collagen.

In a health-conscious age, vivid discussion has been made on the healthfulness of processed foods and food additives. This study focuses on carrageenan (CGN), an approved but debated family of sulphated galactans from algae used as gelling, thickening and stabilizing agents but with indications of possible adverse effects, including as an inhibitor of digestive proteolysis. To challenge this inhibitory hypothesis, food-grade kappa-, iota and lambda-CGN preparations were used to produce beef meatballs whose proteolysis was studied using an in vitro digestion model coupled to various proteomic analyses. Results show that CGN anti-nutritional effects are abolished in beef meatballs. Specifically, proteomic analysis of gastric digesta of myosin light chain 1 (MYL1), alpha skeletal muscle (ACTA1), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and fructose-bisphosphate aldolase (ALDOA) reveal no appreciable differences in the profiles of bioaccessible peptides. Separate digestions of a soluble collagen hydrolysate show CGN does inhibit proteolysis of soluble collagen, therefore supporting the notion that the meat matrix confers a shielding effect that eliminates CGN ability to interfere with digestive proteolysis. Thus, this work shows that CGN ability to hinder digestive proteolysis may not apply to all foods and contributes evidence important to the discussions on CGN uses, indications and regulatory status.

Glucose boosts protein oxidation/nitration during simulated gastric digestion of myofibrillar proteins by creating a severe pro-oxidative environment.

The severe pro-oxidative environment in the stomach promotes oxidation of dietary components. The pro-oxidant molecular mechanisms of reducing sugars on this environment are unknown. To investigate the mechanisms involved in protein oxidation and nitration during a simulated gastric digestion (porcine pepsin, 37 °C, 2 h) of meat proteins, these were exposed to several dietary reactive components namely myoglobin, glucose, glyoxal, myoglobin + glucose and myoglobin + glyoxal. Two versions of each experimental unit were prepared depending on the addition or absence of nitrite. Compared to control (only meat proteins), myoglobin + glucose showed the highest pro-oxidative and pro-nitrosative effect (p < 0.001), likely caused by an increase in ROS derived from the degradation of glucose during assay. Nitrite promoted the occurrence of protein nitration but decreased protein oxidation in myoglobin-added groups (p < 0.001) by, plausibly, stabilizing heme iron. These results indicate the relevant role of glyco-oxidation during digestion of red meat with other dietary components such as reducing sugars.

ε-Polylysine-mediated enhancement of the structural stability and gelling properties of myofibrillar protein under oxidative stress.

The effects of ε-polylysine (ε-PL) at different concentrations (0.005 %, 0.010 %, 0.020 %, and 0.030 %) on the structure and gelling behavior of pork myofibrillar protein (MP) under oxidative stress were explored. The incorporation of ε-PL significantly restrained oxidation-induced sulfhydryl and solubility losses (up to 9.72 % and 41.9 %, respectively) as well as protein crosslinking and aggregation. Compared with the oxidized control, ε-PL at low concentrations (0.005 % - 0.020 %) promoted further unfolding and destabilization of MP, while 0.030 % ε-PL led to refolding of MP and enhanced its thermal stability. The ε-PL-induced physicochemical changes favored the formation of a finer and more homogeneous three-dimensional network structure, therefore obviously enhancing the strength and water-holding capacity (WHC) of thermally induced oxidized MP gels, with the ε-PL at 0.020 % showed the greatest enhancement. This work revealed for the first time that ε-PL can significantly ameliorate the oxidation stability and gel-forming ability of meat proteins.

Deciphering the protein digestion of meat products for the elderly by in vitro food oral processing and gastric dynamic digestion, peptidome analysis and modeling.

The elderly population will increase sharply in the future, along with an emerging range of specific nutritional needs that include adapted food. We aimed to develop a workflow to study the fate of a food, objectify the bioavailability of nutrients in the case of the digestive physiology of the elderly, and model the fate of proteins in the stomach. Pork frankfurters were subjected to in vitro normal and deficient mastication and gastric digestion, mimicking adult and elderly food oral and digestive processing. Swallowable food boluses were characterized for granulometric and rheological properties. Biochemical analyses were conducted on the bolus and on the digesta. Macronutrients, label-free peptide quantification and identification were performed, and modeling was applied to protein digestion kinetics. After deficient mastication, the food bolus was harder with more large particles, lower free iron release and more protein oxidation. The amount of peptides released in the stomach progressively increased, but to a lower extent for the elderly digestive condition and irrespective of masticatory efficiency. 592 peptides were identified from 67 proteins. Different trajectories were observed for adult and elderly digestive conditions, and two groups of meat proteins were identified based on the rate of hydrolysis. Designing suitable foods requires in vitro tools to evaluate the possible benefit for the elderly. Besides the well-known notion of Food Oral Processing (FOP), our work broadens the concept by extending oral activity to digestion when working in a nutritional context. This new concept is named Food Oral and Digestive Processing, FODP.

Improvement of meat protein digestibility in infants and the elderly.

Meat is a valuable protein source with a balanced composition of essential amino acids and various nutrients. This review aims to identify methods to improve digestion of meat proteins, as well as evaluate the digestive characteristics of infants and the elderly. Immature digestive conditions in infants, including a high gastric pH and low protease concentration, can hinder protein digestion, thus resulting in inhibited growth and development. Likewise, gastrointestinal (GI) tract aging and chronic health problems, including tooth loss and atrophic gastritis, can lead to reduction in protein digestion and absorption in the elderly compared with those in young adults. Moderate heating and several non-thermal technologies, such as aging, enzymatic hydrolysis, ultrasound, high-pressure processing, and pulsed electric field can alter protein structure and improve protein digestion in individuals with low digestive capacity.

Impact of postmortem degradation of cytoskeletal proteins on intracellular gap, drip channel and water-holding capacity.

The present study aimed to investigate the impact of the degradation of cytoskeletal proteins (desmin, integrin, vinculin, and talin) on the formation of intracellular gap and drip channel and water-holding capacity in pork. The intensity of intact cytoskeletal proteins and the width of intracellular gap and drip channel were measured in high drip loss and low drip loss groups. The data indicate that the width of intracellular gap and drip channel explained 17% and 62% variation in drip loss, respectively, while the intensity of intact desmin, integrin, and vinculin explained 47%, 34%, and 47% variation in drip loss, respectively. The postmortem formation of intracellular gap is mainly affected by the changes in integrin and vinculin, while the formation of the drip channel is influenced by the changes in desmin. These findings suggest that postmortem formation of wide intracellular gap and drip channels is linked to increased drip loss.

Soybean meal and poultry offal meal effects on digestibility of adult dogs diets: Systematic review.

Soybean meal and poultry offal meal are protein ingredients commonly used in the formulation of commercial diets for dogs. However, there remains great variability in the data on the digestibility of each protein source. This systematic review study aimed to examine the intake, apparent nutrient digestibility coefficients and fecal output of protein sources (soybean meal and poultry offal meal) in adult dog food as reported in published studies. The article search was conducted in August 2018 in the PUBMED, SciELO, Science Direct and AGRIS indexing databases. The literature search was performed using "digestibility", "source protein" and "dog" as the main key terms combined with sub-terms to broaden the scope of the search. Criteria were defined for readability, exclusion and inclusion of articles. Results were organized in groups according to the search in the indexing databases, totaling 1,414 articles. After the works were selected following the inclusion criteria, 17 articles were evaluated in this review. According to most studies, plant-based ingredients have a less variable nutritional composition than animal-derived ingredients and poultry offal meal increases the digestibility coefficients of nutrients and energy and reduces fecal dry matter production. Factors inherent to raw-material origin, ingredient and food processing, as well as the high heterogeneity of the methodologies evaluated in the studies are directly related to the obtained results. To ensure a more accurate evaluation of the quality and of effects on the digestibility of protein sources, we recommended that articles include ingredient processing data and that the variables be evaluated under standardized study conditions.

Quantitative proteomic analysis of beef tenderness of Piemontese young bulls by SWATH-MS.

Quantitative proteomic approach is a suitable way to tackle the beef tenderness. Ten aged-beef samples from Longissimus thoracis of Piemontese breed classified as tender (n = 5) and tough (n = 5) meat were evaluated using SWATH-MS and bioinformatic tools for the identification of the proteins and pathways most influencing tenderness variability. Between the two textural groups, proteomic changes were mainly caused by 43 differentially abundant proteins (DAPs) arranged in reference patterns as displayed by the heat map analysis. Most of these DAPs were associated with energy metabolism. From the functional proteomic analysis, two clusters of proteins, including ACO2, MDH1, MDH2 and CS in one cluster and FBP2, PFKL, LDHA, TPI1 and GAPDH/S in the other cluster, suggest gluconeogenesis, glycolysis and citrate cycle as key pathways for Piemontese breed beef tenderness. These findings contribute to a deeper insight into molecular pathways related to beef tenderness.

Dual role (promotion and inhibition) of transglutaminase in mediating myofibrillar protein gelation under malondialdehyde-induced oxidative stress.

This study investigated the effects of transglutaminase (TGase) on the properties of myofibrillar protein (MP) and its heat-induced gels under malondialdehyde (MDA)-induced oxidation. The physicochemical characteristics, protein aggregation and rheological properties of MP were assessed. The gelling behaviours of MP were analysed with measurements of gel strength, cooking loss, microstructure and secondary structure. Under varying degrees of MDA oxidation, the addition of TGase always led to changes in the tertiary structure, loss of free amine and thiol groups, crosslinking of the myosin heavy chain, and decreasing solubility. However, the effect of TGase on MP gel quality differed. At 6 mmol/L MDA, the addition of TGase reduced the quality of MP gels by increasing cooking loss. However, at 12 mmol/L MDA, TGase reduced both the cooking loss and gel strength.

Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol.

Plant polyphenols applied as natural antioxidant ingredients, are known to bind to cysteine residues on meat proteins. The aim of this study was to examine the effect of light exposure on the formation of cysteine-phenol adduct in meat added 4-methylcatechol (4MC), a model polyphenol, during storage through quantitative LC-MS/MS-based analysis. Cysteine-4-methylcatechol adduct (Cys-4MC) formation in meat added 1500 ppm 4-MC increased significantly (by 50%) when stored under light in oxygen at 4 °C for 7 days as compared to storage in the dark. This was reflected by a significant decrease in thiol concentrations in the same sample. Gel electrophoresis showed loss in myosin heavy chain (MHC), and a resulting increase in cross-linked MHC (CL-MHC) and larger protein polymers in samples added 4MC. Protein blots stained with nitroblue tetrazolium (NBT) showed intensive protein-polyphenol binding in the meat samples added 4MC, but no major differences between storage conditions.

Sensory Assessment of Fish and Chicken Protein Hydrolysates. Evaluation of NMR Metabolomics Profiling as a New Prediction Tool.

Nuclear magnetic resonance (NMR) metabolomics profiling was evaluated as a new tool in sensory assessment of protein hydrolysates. Hydrolysates were produced on the basis of different raw materials (cod, salmon, and chicken), enzymes (Food Pro PNL and Bromelain), and hydrolysis time (10 and 50 min). The influence of raw material and hydrolysis parameters on sensory attributes was determined by traditional descriptive sensory analysis and 1H NMR spectroscopy. The raw material had a major influence on the attribute intensity and metabolite variation, followed by enzyme and hydrolysis time. However, the formation of bitter taste was not affected by the raw material. Partial least-squares regression (PLSR) on 1H NMR and sensory data provided good models (Q2 = 0.55-0.89) for 11 of the 17 evaluated attributes, including bitterness. Significant metabolite-attribute associations were identified. The study confirms the potential prediction of the sensory properties of protein hydrolysates from cod, salmon, and chicken based on 1H NMR metabolomics profiling.

Gut inflammation exacerbates hepatic injury in C57BL/6J mice via gut-vascular barrier dysfunction with high-fat-incorporated meat protein diets.

AIM: Meat and its derivatives provide nutrients essential for human health. However, meat consumption, along with excessive fat intake, has been associated with gut inflammation, intestinal barrier dysfunction and alterations in gut microbiota. Herein, we investigated whether and how these changes in the intestinal barrier system affect the gut liver axis and hepatic injury and eventually lead to the progression of liver syndrome such as NAFLD. METHODS: Mice were fed with high fat (60% kcal) or low fat (12% kcal) along with soybean (control), chicken and pork proteins (HFCH, HFP, LFCH, and LFP) for 12 weeks. The biomarkers for liver injury were investigated after meat protein intake along with the high fat. FINDINGS: Greater amount of fat vacuoles visible in the H&E staining increased the inflammatory cell infiltration and disorganized liver structures were observed in the HFP-fed mice. Oil Red O staining revealed that the HFP-fed and HFCH-fed mice showed more lipid droplets, confirming the increased hepatic lipid accumulation. Potential serum markers for NAFLD, ALT and AST were increased in the HF meat diet groups. Key genes responsible for hepatic inflammation and lipogenesis, such as MCP-1, IL1-ß and TNF-α were upregulated. HF meat protein diet-fed mice exhibited signs of compromised liver with increased levels of endotoxin in the liver and its binding protein in serum, upregulation of TLRs in the liver, and significant increase in TG, TC, LDL-C and HDL-C concentrations. SIGNIFICANCE: Intestinal inflammation and barrier dysfunction aggravate liver injury and fibrosis due to the intake of HF meat protein diets in mice, which may contribute to the progress of liver injury and associated complications. Gut inflammation may directly contribute to the development of NAFLD, especially of the gut vascular barricade dysfunction.

Effects of Casein, Chicken, and Pork Proteins on the Regulation of Body Fat and Blood Inflammatory Factors and Metabolite Patterns Are Largely Dependent on the Protein Level and Less Attributable to the Protein Source.

The impact of meat protein on metabolic regulation is still disputed and may be influenced by protein level. This study aimed to explore the effects of casein, pork, and chicken proteins at different protein levels (40% E vs 20% E) on body weight regulation, body fat accumulation, serum hormone levels, and inflammatory factors/metabolites in rats maintained on high-fat (45% E fat) diets for 84 d. Increased protein levels resulted in a significant reduction in body fat mass and an increase in the serum levels of the anti-inflammatory cytokine IL-10, independent of protein source. Analysis of blood via untargeted metabolomics analysis identified eight, four, and four metabolites significantly altered by protein level, protein source, and a protein level-source interaction, respectively. Together, the effects of casein, chicken, and pork protein on the regulation of body fat accumulation and blood metabolite profile are largely dependent on protein level and less attributable to the protein source.

TMT-based quantitative proteomic analysis of porcine muscle associated with postmortem meat quality.

To explore the molecular mechanisms of meat quality, four high-quality (HQ) samples and four low-quality (LQ) samples from longissimus dorsi muscles were chosen, and tandem mass tag (TMT) labeling combined with mass spectrometry (MS) were performed to find associations between meat quality and proteome profiles. The LQ meats had lower pH, lighter color, and higher drip loss compared to the HQ meats. About 140 differentially expressed proteins were identified. Functional analysis results of differentially expressed proteins showed that decreased release of Ca2+, lower contents of type II fibers, lower contents of glycogen, and decreased glycogenolysis in HQ meats indicated a lower degree of glycolysis in HQ as compared to LQ meats. Meanwhile, some differentially expressed proteins suggested that the levels of oxidative stress and apoptosis were lower in HQ meats than in LQ meats. This study reveals physiological changes between HQ and LQ meats according to the proteome profiles.

High-Meat-Protein High-Fat Diet Induced Dysbiosis of Gut Microbiota and Tryptophan Metabolism in Wistar Rats.

Meat-diet-induced changes in gut microbiota are often accompanied with the development of various metabolic and inflammatory disorders. The exact biochemical mechanism underlying these effects is not well elucidated. This study aims to evaluate how meat proteins in high-fat diets affect tryptophan metabolism in rats. The high-chicken-protein (HFHCH) or high-pork-protein (HFHP) diets increased levels of skatole and indole in cecal and colonic contents, feces, and subcutaneous adipose tissue. The HFHCH and HFHP diets also increased the abundance of Lactobacillus, the Family XIII AD3011 group, and Desulfovibrio in the cecum and colon, which may be involved in the production of skatole and indole. Additionally, high-meat-protein diets induced lower activity of skatole- and indole-metabolizing enzyme CYP2E1 in liver compared with low-meat-protein diets. This work highlights the negative impact of high meat proteins on physiological responses by inducing dysbiosis of gut microbiota and tryptophan metabolism.

High intake of chicken and pork proteins aggravates high-fat-diet-induced inflammation and disorder of hippocampal glutamatergic system.

High-fat diets have been associated with neurodegenerative diseases, which are also largely related to the type and amount of dietary proteins. However, to our knowledge, it is little known how dietary proteins affect neurodegenerative changes. In this study, we investigated the effects of dietary proteins in a high-fat diet on hippocampus functions related to enteric glial cells (EGCs) in Wistar rats that were fed either 40% or 20% (calorie) casein, chicken protein or pork protein for 12 weeks (n=10 each group). Inflammatory factors, glutamatergic system, EGCs, astrocytes and nutrient transporters were measured. A high-chicken-protein diet significantly increased the levels of systemic inflammatory factors, Tau protein and amyloid precursor protein mRNA level in the rat hippocampus. The type and level of dietary proteins in high-fat diets did not affect the gene expression of glial fibrillary acidic protein and α-synuclein (P>.05), indicating a negligible effect on astrocyte activity. However, the high-protein diets up-regulated glutamate transporters compared with the low-protein diets (P<.05), while they reduced the γ-aminobutyric acid content in high-chicken and -pork-protein diets (P<.05). Thus, compared with a low-protein diet (20%), a high-chicken or -pork-protein diet (40%) under a high-fat background could alter the balance between glutamatergic system and neurotransmitter and have a stronger effect on the interactions between hippocampal glutamatergic system and EGCs.