Phenotypic link between protein efficiency and pig welfare suggests no apparent trade-offs for mitigating nitrogen pollution.

Pig manure contributes significantly to environmental pollution through nitrogen compounds. Reducing protein in feed can help, but it may lead to damaging behaviors if pigs' nutritional needs are not met. Breeding pigs for higher protein efficiency (PE) is a long-term solution to reduce nitrogen pollution, but concerns about pig welfare remain. We studied 95 pigs involved in a project on the genetic basis of PE on a 20% protein restricted diet to investigate the phenotypic connection between PE and welfare. These pigs represented natural PE variations in the population. At around 100 days, before their PE was known, we observed their behaviors. Only three pigs engaged in tail biting and manipulation of vulnerable regions, but this was not associated with PE. There was no clear link between PE and manipulating pen mates' less vulnerable regions. Such behaviors are normal but can cause stress and injury if carried out excessively due to boredom or stress. Overall, pigs with higher PE showed no major behavioral abnormalities in this study. Considering the lack of genetic knowledge, the risk of increased harmful behaviors when selecting for higher PE appears low when inferred from this purely phenotypic association.

Food protein-derived amyloids do not accelerate amyloid ß aggregation.

The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are not associated with disease can form amyloid with similar structural characteristics as the disease-associated fibrils, which highlights the potential risk of cross-seeding of disease amyloid by amyloid-like structures encountered in our surrounding. Of particular interest are common food proteins that can be transformed into amyloid under conditions similar to cooking. We here investigate cross-seeding of amyloid-ß (Aß), a peptide known to form amyloid during the development of Alzheimer's disease, by 16 types of amyloid fibrils derived from food proteins or peptides. Kinetic studies using thioflavin T fluorescence as output show that none of the investigated protein fibrils accelerates the aggregation of Aß. In at least two cases (hen egg lysozyme and oat protein isolate) we observe retardation of the aggregation, which appears to originate from interactions between the food protein seeds and Aß in aggregated form. The results support the view that food-derived amyloid is not a risk factor for development of Aß pathology and Alzheimer's disease.

Potential implications of oxidative modification on dietary protein nutritional value: A review.

During food processing and storage, proteins are sensitive to oxidative modification, changing the structural characteristics and functional properties. Recently, the impact of dietary protein oxidation on body health has drawn increasing attention. However, few reviews summarized and highlighted the impact of oxidative modification on the nutritional value of dietary proteins and related mechanisms. Therefore, this review seeks to give an updated discussion of the effects of oxidative modification on the structural characteristics and nutritional value of dietary proteins, and elucidate the interaction with gut microbiota, intestinal tissues, and organs. Additionally, the specific mechanisms related to pathological conditions are also characterized. Dietary protein oxidation during food processing and storage change protein structure, which further influences the in vitro digestion properties of proteins. In vivo research demonstrates that oxidized dietary proteins threaten body health via complicated pathways and affect the intestinal microenvironment via gut microbiota, metabolites, and intestinal morphology. This review highlights the influence of oxidative modification on the nutritional value of dietary proteins based on organs and the intestinal tract, and illustrates the necessity of appropriate experimental design for comprehensively exploring the health consequences of oxidized dietary proteins.

Simulated gastric fluid assay for estimating the digestibility of newly expressed proteins in GE crops: Missteps in development and interpretation.

Digestive stability of a food protein in simulated gastric fluid (SGF) continues to be considered a risk factor for allergy, even though the current science does not support this belief. Methodological shortcomings of the adaption of the SGF assay for use with purified proteins has been cited as a reason to discount results that do not conform to this belief. Missteps in conducting and interpreting the results of SGF assays are reviewed here. However, these methodological shortcomings do not invalidate the conclusion that allergenic proteins are not systematically more stable to digestion than non-allergens. The growing evidence for the dual allergen exposure hypothesis, whereby sensitization to food allergens is primarily caused by dermal and inhalation exposure to food dust, and tolerization against food allergy is primarily induced by gut exposure in food, likely explains why the digestive stability of a protein is not a risk factor for allergenicity.

Analysis of the Factors Affecting Static In Vitro Pepsinolysis of Food Proteins.

In this meta-analysis, we collected 58 publications spanning the last seven decades that reported static in vitro protein gastric digestion results. A number of descriptors of the pepsinolysis process were extracted, including protein type; pepsin activity and concentration; protein concentration; pH; additives; protein form (e.g., 'native', 'emulsion', 'gel', etc.); molecular weight of the protein; treatment; temperature; and half-times (HT) of protein digestion. After careful analysis and the application of statistical techniques and regression models, several general conclusions could be extracted from the data. The protein form to digest the fastest was 'emulsion'. The rate of pepsinolysis in the emulsion was largely independent of the protein type, whereas the gastric digestion of the native protein in the solution was strongly dependent on the protein type. The pepsinolysis was shown to be strongly dependent on the structural components of the proteins digested-specifically, ß-sheet-inhibited and amino acid, leucine, methionine, and proline-promoted digestion. Interestingly, we found that additives included in the digestion mix to alter protein hydrolysis had, in general, a negligible effect in comparison to the clear importance of the protein form or additional treatment. Overall, the findings allowed for the targeted creation of foods for fast or slow protein digestion, depending on the nutritional needs.

Impact of Thermal Treatment on the Starch-Protein Interplay in Red Lentils: Connecting Molecular Features and Rheological Properties.

Thermal treatments are widely applied to gluten-free (GF) flours to change their functionality. Despite the interest in using pulses in GF formulations, the effects of thermal treatment at the molecular level and their relationship with dough rheology have not been fully addressed. Raw and heat-treated red lentils were tested for starch and protein features. Interactions with water were assessed by thermogravimetric analysis and water-holding capacity. Finally, mixing properties were investigated. The thermal treatment of red lentils induced a structural modification of both starch and proteins. In the case of starch, such changes consequently affected the kinetics of gelatinization. Flour treatment increased the temperature required for gelatinization, and led to an increased viscosity during both gelatinization and retrogradation. Regarding proteins, heat treatment promoted the formation of aggregates, mainly stabilized by hydrophobic interactions between (partially) unfolded proteins. Overall, the structural modifications of starch and proteins enhanced the hydration properties of the dough, resulting in increased consistency during mixing.

Antioxidant and Antimicrobial Peptides Derived from Food Proteins.

Recently, the demand for food proteins in the market has increased due to a rise in degenerative illnesses that are associated with the excessive production of free radicals and the unwanted side effects of various drugs, for which researchers have suggested diets rich in bioactive compounds. Some of the functional compounds present in foods are antioxidant and antimicrobial peptides, which are used to produce foods that promote health and to reduce the consumption of antibiotics. These peptides have been obtained from various sources of proteins, such as foods and agri-food by-products, via enzymatic hydrolysis and microbial fermentation. Peptides with antioxidant properties exert effective metal ion (Fe2+/Cu2+) chelating activity and lipid peroxidation inhibition, which may lead to notably beneficial effects in promoting human health and food processing. Antimicrobial peptides are small oligo-peptides generally containing from 10 to 100 amino acids, with a net positive charge and an amphipathic structure; they are the most important components of the antibacterial defense of organisms at almost all levels of life-bacteria, fungi, plants, amphibians, insects, birds and mammals-and have been suggested as natural compounds that neutralize the toxicity of reactive oxygen species generated by antibiotics and the stress generated by various exogenous sources. This review discusses what antioxidant and antimicrobial peptides are, their source, production, some bioinformatics tools used for their obtainment, emerging technologies, and health benefits.

Deciphering Changes in the Structure and IgE-Binding Ability of Ovalbumin Glycated by α-Dicarbonyl Compounds under Simulated Heating.

As a complex reaction, biological consequences of the Maillard reaction (MR) on dietary proteins need to be deciphered. Despite previous studies on the structural and antigenic properties of ovalbumin (OVA) by MR, associated changes induced by specific MR intermediates and their downstream products are largely unknown. This study focused on the impacts of glycation by α-dicarbonyl compounds (α-DCs), intermediates of MR and precursors of advanced glycation end-products (AGEs), on the structural and IgE-binding properties of ovalbumin (OVA) under simulated heating. Methylglyoxal (MGO), glyoxal (GO), and butanedione (BU) were selected as typical α-DCs to generate glycated OVA with different AGE-modifications (AGE-Ms). The results showed that reactions between OVA and α-DCs generated OVA-AGE with various degrees of modification and conformational unfolding, and the reactivity of α-DCs followed the order GO > MGO > BU. Depending on the precursor type, the levels of 10 specific AGEs were verified, and the amounts of total AGEs increased with heating temperature and α-DC dosage. Compared to native OVA, glycated OVA showed reduced IgE-binding levels but with sRAGE-binding ligands, the extent of which was associated with the contents of total AGEs and Nε-carboxymethyllysine, and changes in certain protein conformational structures. High-resolution mass spectrometry further identified different AGE-Ms on the Lys and Arg residues of OVA, confirming variations in the glycation sites and their associations with the immunoreactive epitopes of OVA under different conditions.

Effects of non-essential protein on D-glucose to control diabetes: DFT approach.

Diabetes is a disease found in every 1 out of 4 people in the world. The glucose molecule is one of the sources of energy in the body and the lack of the digestion of glucose causes diabetes type 1 and type 2. Arginine and cysteine are nonessential amino acids that contain sulfur and help maintain the metabolisms of humans. We explored the glucose-arginine (Glc-arg) and glucose-cysteine (Glc-cys) molecules by finding their structural properties, electronic properties, chemical reactivity, mechanical strength, and transport properties because these non-essential amino acid molecules inhibit glucose-stimulated insulin secretion. Density functional theory (DFT) has been implemented to study all the properties of Glc-arg and Glc-cys using SIESTA software. Glucose-arginine (Glc-arg) inhibits a large percentage of glucose secretion and shows high chemical reactivity.

UMPred-FRL: A New Approach for Accurate Prediction of Umami Peptides Using Feature Representation Learning.

Umami ingredients have been identified as important factors in food seasoning and production. Traditional experimental methods for characterizing peptides exhibiting umami sensory properties (umami peptides) are time-consuming, laborious, and costly. As a result, it is preferable to develop computational tools for the large-scale identification of available sequences in order to identify novel peptides with umami sensory properties. Although a computational tool has been developed for this purpose, its predictive performance is still insufficient. In this study, we use a feature representation learning approach to create a novel machine-learning meta-predictor called UMPred-FRL for improved umami peptide identification. We combined six well-known machine learning algorithms (extremely randomized trees, k-nearest neighbor, logistic regression, partial least squares, random forest, and support vector machine) with seven different feature encodings (amino acid composition, amphiphilic pseudo-amino acid composition, dipeptide composition, composition-transition-distribution, and pseudo-amino acid composition) to develop the final meta-predictor. Extensive experimental results demonstrated that UMPred-FRL was effective and achieved more accurate performance on the benchmark dataset compared to its baseline models, and consistently outperformed the existing method on the independent test dataset. Finally, to aid in the high-throughput identification of umami peptides, the UMPred-FRL web server was established and made freely available online. It is expected that UMPred-FRL will be a powerful tool for the cost-effective large-scale screening of candidate peptides with potential umami sensory properties.

Effects of stewing with tea polyphenol on the gel properties, microstructure, and secondary structure of boiled egg white.

This study aimed to investigatethe mechanism of stewing with tea polyphenols (TP) on the properties of boiled egg white gel (BEWG). The results indicated that, during the stewing process, soluble protein and hardness showed an overall increasing trend, while surface hydrophobicity showed a decreasing trend with blue-shift. The free sulfhydryl group showed that TP could promote the formation of disulfide bonds, and the position of immobilized water at T2 showed a decreasing trend. Environmental scanning electron microscopy and SDS-PAGE showed that the protein gel aggregation degree increased. Moreover, Fourier transform infrared spectrometry showed that protein polarity increased and that α-helices, ß-turn, intramolecular ß-sheets, as well as intermolecular antiparallel ß-sheets showed an increasing trend. Generally, TP strengthened protein aggregation by promoting the formation of disulfide and hydrogen bonds, thus enhancing the gel strength of BEWG. Moreover, the secondary structure of proteins became more stable under the action of TP, and the higher the concentration of TP, the greater the effect on BEWG. PRACTICAL APPLICATION: TP, an ideal, cheap, and safe natural food additive, can be applied to the processing of egg products because the addition of TP can significantly improve the gel strength of egg white.

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update.

Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides' efficiencies before commercial applications.

Impact of the particle-polymer interface on small- and large-scale deformation response in protein- and carbohydrate-based food matrices.

Interfaces are important regarding the mechanical behavior of foods. In particle-polymer-based food systems, the rheological effect of interface characteristics between microscopic particles and viscoelastic polymers is controversial. By using a new approach of presenting defined glass beads surfaces, which imitate functional groups of starch particle surfaces, the adhesiveness and the adsorption mechanism between particle and polymeric food matrix (protein-/carbohydrate-based) can be controlled. The combination of defined particle-polymer interfaces with a comprehensive rheological analysis gives new insights into the effect of particle-polymer interfaces on the mechanical properties of food. Independent of the matrix-type, non-adhesive particles show the strongest network at low stress (protein-based: network strength Af = 2.02 ± 0.16 ∗ 104 Pas1/z), but the fastest network breakdown under higher stress (fracture strain protein-based 4.40 ± 0.08). Adhesive particles behave inverse (Af = 1.02 ± 0.24 *104 Pas1/z; fracture strain 5.38 ± 0.32). Consequently, particle supplemented protein-/carbohydrate-based matrices have properties similar to particle reinforced rubbers and exhibit a more or less pronounced Payne effect depending on the adhesiveness. Besides the adhesiveness, the adsorption mechanism affects the deformation behavior of particle-polymer based system. The highly adhesive but unspecific adsorption of carbohydrate-based polymers at cyano-functionalized surfaces shows a similar relaxation behavior as non-adhesive surface functionalization.

Cross-Reactivity and Sequence Homology Between Alpha-Synuclein and Food Products: A Step Further for Parkinson's Disease Synucleinopathy.

INTRODUCTION: Parkinson's disease is characterized by non-motor/motor dysfunction midbrain neuronal death and α-synuclein deposits. The accepted hypothesis is that unknown environmental factors induce α-synuclein accumulation in the brain via the enteric nervous system. MATERIAL AND METHODS: Monoclonal antibodies made against recombinant α-synuclein protein or α-synuclein epitope 118-123 were applied to the antigens of 180 frequently consumed food products. The specificity of those antibody-antigen reactions was confirmed by serial dilution and inhibition studies. The Basic Local Alignment Search Tool sequence matching program was used for sequence homologies. RESULTS: While the antibody made against recombinant α-synuclein reacted significantly with 86/180 specific food antigens, the antibody made against α-synuclein epitope 118-123 reacted with only 32/180 tested food antigens. The food proteins with the greatest number of peptides that matched with α-synuclein were yeast, soybean, latex hevein, wheat germ agglutinin, potato, peanut, bean agglutinin, pea lectin, shrimp, bromelain, and lentil lectin. Conclusions: The cross-reactivity and sequence homology between α-synuclein and frequently consumed foods, reinforces the autoimmune aspect of Parkinson's disease. It is hypothesized that luminal food peptides that share cross-reactive epitopes with human α-synuclein and have molecular similarity with brain antigens are involved in the synucleinopathy. The findings deserve further confirmation by extensive research.

Protein suppresses both bitterness and oleocanthal-elicited pungency of extra virgin olive oil.

The Mediterranean diet, considered one of the healthiest in the world, is characterized in part by the major source of its fat, which is extra virgin olive oil (EVOO). Among the health benefits of consuming EVOOs is the presence of phenolic compounds, which have been shown to lower the incidence of coronary heart disease and are suspected of providing many other health benefits. These phenolic compounds also contribute to the flavor of EVOO, adding both specific pungency in the throat and bitter notes that are valued by connoisseurs but reported to be unpleasant by naïve consumers. Here, we demonstrate that some food-derived proteins, specifically from egg yolks and whey, when added to pungent and bitter EVOOs, reduce or even eliminate both the throat pungency and bitterness. The sensory loss is proportional to the food protein additions. Thus, when used in various foods recipes (e.g. mayonnaise), pungent and bitter EVOOs may lose their pungent and bitter characteristics thereby rendering them more palatable to many consumers. This sensory reduction might also indicate interaction between the proteins and the phenolic compounds, which, if confirmed, would raise the question of whether the bioactivities of EVOO phenolics remain unchanged when consumed with and without protein-containing foods.

Dietary intake of sulfur amino acids and risk of kwashiorkor malnutrition in eastern Democratic Republic of the Congo.

BACKGROUND: Kwashiorkor is an often-fatal type of severe acute malnutrition affecting hundreds of thousands of children annually, but whose etiology is still unknown. Evidence suggests inadequate sulfur amino acid (SAA) status may explain many signs of the condition but studies evaluating dietary protein intake in relation to the genesis of kwashiorkor have been conflicting. We know of no studies of kwashiorkor that have measured dietary SAAs. OBJECTIVES: We aimed to determine whether children in a population previously determined to have high prevalence of kwashiorkor [high-prevalence population (HPP)] have lower dietary intakes of SAAs than children in a low-prevalence population (LPP). METHODS: A cross-sectional census survey design of 358 children compared 2 previously identified adjacent populations of children 36-59 mo old in North Kivu Province of the Democratic Republic of the Congo. Data collected included urinary thiocyanate (SCN), cyanogens in cassava-based food products, recent history of illness, and a 24-h quantitative diet recall for the child. RESULTS: The HPP and LPP had kwashiorkor prevalence of 4.5% and 1.7%, respectively. A total of 170 children from 141 households in the LPP and 169 children from 138 households in the HPP completed the study. A higher proportion of HPP children had measurable urinary SCN (44.8% compared with 29.4%, P < 0.01). LPP children were less likely to have been ill recently (26.8% compared with 13.6%, P < 0.01). Median [IQR] intake of SAAs was 32.4 [22.9-49.3] mg/kg for the LPP and 29.6 [18.1-44.3] mg/kg for the HPP (P < 0.05). Methionine was the first limiting amino acid in both populations, with the highest risk of inadequate intake found among HPP children (35.1% compared with 23.6%, P < 0.05). CONCLUSIONS: Children in a population with a higher prevalence of kwashiorkor have lower dietary intake of SAAs than children in a population with a lower prevalence. Trial interventions to reduce incidence of kwashiorkor should consider increasing SAA intake, paying particular attention to methionine.

Higher Branched-Chain Amino Acid Intake Is Associated with Handgrip Strength among Korean Older Adults.

Sarcopenia is a disease of old age characterized by decreased muscle mass and strength. Branched-chain amino acids (BCAAs) promote muscle mass synthesis and increase muscle strength. We aimed to develop a dietary amino acid database and to examine the association between BCAA intake and handgrip strength in Korean older adults. Data from the Korea National Health and Nutrition Examination Survey 2014-2018 were used. Overall, 4852 participants aged ≥65 years were included in the study. Demographic, lifestyle, and health data were obtained through interviews and questionnaires. The 24-h recall method was used to assess dietary intake. An amino acid database was established using the 9th revision of the Korean Standard Food Composition Table. The mean handgrip strength was estimated from triplicate measurements obtained using the dominant hand. Multivariable linear regression analysis was performed to assess the association between BCAA intake and handgrip strength. Grains greatly contributed to amino acid intake; however, a significant negative association was observed between handgrip strength and increased BCAA intake through grains. In the fully adjusted model, leucine intake and handgrip strength showed a positive association. Thus, consuming BCAAs (especially leucine) via a variety of food sources can help maintain muscle health in older people.

Early-Life Metabolic and Hormonal Markers in Blood and Growth until Age 2 Years: Results from a Randomized Controlled Trial in Healthy Infants Fed a Modified Low-Protein Infant Formula.

BACKGROUND: High protein intake in early life is associated with an increased risk of childhood obesity. Dietary protein intake may be a key mechanistic modulator through alterations in endocrine and metabolic responses. OBJECTIVE: We aimed to determine the impact of different protein intake of infants on blood metabolic and hormonal markers at the age of four months. We further aimed to investigate the association between these markers and anthropometric parameters and body composition until the age of two years. DESIGN: Term infants received a modified low-protein formula (mLP) (1.7 g protein/100 kcal) or a specifically designed control formula (CTRL) (2.1 g protein/100 kcal) until 6 months of age in a double blinded RCT. The outcomes were compared with a breast-fed (BF) group. Glucose, insulin, leptin, IGF-1, IGF-BP1, -BP2, and -BP3 levels were measured at the age of 4 months. Anthropometric parameters and body composition were assessed until the age of 2 years. Groups were compared using linear regression analysis. RESULTS: No significant differences were observed in any of the blood parameters between the formula groups (n = 53 mLP; n = 44 CTRL) despite a significant difference in protein intake. Insulin and HOMA-IR were higher in both formula groups compared to the BF group (n = 36) (p < 0.001). IGF-BP1 was lower in both formula groups compared to the BF group (p < 0.01). We found a lower IGF-BP2 level in the CTRL group compared to the BF group (p < 0.01) and a higher IGF-BP3 level in the mLP group compared to the BF group (p = 0.03). There were no significant differences in glucose, leptin, and IGF-1 between the three feeding groups. We found specific associations of all early-life metabolic and hormonal blood parameters with long-term growth and body composition except for IGF-1. CONCLUSIONS: Reducing protein intake by 20% did not result in a different metabolic profile in formula-fed infants at 4 months of age. Formula-fed infants had a lower insulin sensitivity compared to breast-fed infants. We found associations between all metabolic and hormonal markers (except for IGF-1) determined at age 4 months and growth and body composition up to two years of age.