Effects of physical processing on food protein allergenicity: A focus on differences between animal and alternative proteins.

In recent years, physical technologies have been widely employed to reduce food protein allergenicity due to their simplicity and stability. This paper summarizes recent research advances in these technologies, focusing on differences in their effects on allergenicity between animal and alternative proteins. The mechanisms of allergenicity reduction and the advantages and disadvantages of these technologies were compared. It was found that heating, although affording better allergenicity reduction than non-thermal treatment technologies, affects other properties of the food. Because of their higher molecular weights and more complex structures, animal proteins are less affected by physical technologies than alternative proteins. It is worth noting that there is a scarcity of existing technology to reduce the allergenicity of food proteins, and more technologies should be explored for this purpose. In addition, better allergenicity-reducing processing technologies should be designed from the perspectives of processing conditions, technological innovations, and combined processing technologies in the future.

Low protein digestibility-corrected amino acid score and net nitrogen-to-protein conversion factor value of edible insects.

The amount of chitin, a nitrogen-containing dietary fiber, in edible insects can mislead the exact nitrogen-to-protein conversion factor (NPF) and true protein content. We determined the amino acid score (AAS), protein digestibility-corrected AAS (PDCAAS), chitin content, and net NPF of five edible insects. Additionally, the effect of the amino acid composition of migratory locust on rat growth were investigated. The AAS of the insects were ranged from 63 to 94. The chitin contents were ranged from 1.6 g/100 g to 10.7 g/100 g. The PDCAAS, calculated by AAS and gut-intestinal digestibility, ranged from 44 to 81, which was lower than casein (97). The net NPF ranged from 4.93 to 5.76, which were lower than the conventional value. Dietary migratory locust, whose PDCAAS was the lowest, decreased growth and altered lipid metabolism. Therefore, a lower PDCAAS and overestimation of net NPF of insects can affect the true protein calculations and growth.

Feature fusion-based food protein subcellular prediction for drug composition.

The structure and function of dietary proteins, as well as their subcellular prediction, are critical for designing and developing new drug compositions and understanding the pathophysiology of certain diseases. As a remedy, we provide a subcellular localization method based on feature fusion and clustering for dietary proteins. Additionally, an enhanced PseAAC (Pseudo-amino acid composition) method is suggested, which builds upon the conventional PseAAC. The study initially builds a novel model of representing the food protein sequence by integrating autocorrelation, chi density, and improved PseAAC to better convey information about the food protein sequence. After that, the dimensionality of the fused feature vectors is reduced by using principal component analysis. With prediction accuracies of 99.24% in the Gram-positive dataset and 95.33% in the Gram-negative dataset, respectively, the experimental findings demonstrate the practicability and efficacy of the proposed approach. This paper is basically exploring pseudo-amino acid composition of not any clinical aspect but exploring a pharmaceutical aspect for drug repositioning.

Inclusion of reeling wastewater-derived sericin peptides in high-protein nutrition bars for antihardening and storage stability.

The utilization of agroindustrial wastes to enrich food protein resources and the exploration of their broader applications are crucial for addressing the food crisis and achieving sustainable development goals. In this study, reeling wastewater-derived sericin was hydrolyzed using papain and trypsin to prepare sericin peptide (SRP) and was used as an antihardening ingredient of high-protein nutrition bars (HPNBs). The mechanism of the antihardening effect of SRP was elucidated by investigating the content of advanced glycation end products and protein oxidation products (carbonyl and free sulfhydryl), and the molecular weight change of HPNBs during storage before and after the addition of SRP. Our results confirmed the fortification of HPNBs with SRP, which is beneficial for the promotion and expansion of sericin applications in the food industry, with positive implications for the rational utilization of protein resources and the enrichment of food protein sources.

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.

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.

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.

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.

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.

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.

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.

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.