Search

Ovalbumin (OVA), the most abundant protein in egg whites, has been widely used in various industries. Currently, the structure of OVA has been clearly established, and the extraction of high-purified OVA has become feasible. However, the allergenicity of OVA is still a serious problem because it can cause severe allergic reactions and may even be life-threatening. The structure and allergenicity of the OVA can be altered by many processing methods. In this article, a detailed description on the structure and a comprehensive overview on the extraction protocols and the allergenicity of OVA was documented. Additionally, the information on assembly and potential applications of OVA was summarized and discussed in detail. Physical treatment, chemical modification, and microbial processing can be applied to alter the IgE-binding capacity of OVA by changing its structure and linear/sequential epitopes. Furthermore, research indicated that OVA could assemble with itself or other biomolecules into various forms (particles, fibers, gels, and nanosheets), which expanded its application in the food field. OVA also shows excellent application prospects, including food preservation, functional food ingredients and nutrient delivery. Therefore, OVA demonstrates significant investigation value as a food grade ingredient. [ABSTRACT FROM AUTHOR]

Hydrodynamic cavitation (HC) is thought weaken the allergenicity of beer gluten proteins. However, the mechanism of action has not been thoroughly studied. In this study, an HC device was used to treat wheat gliadin and two specific celiac-toxic peptides, P1 and P2. FT-IR, MFS, HPLC, and CD were used to monitor the structural characteristics of gliadin and the two peptides. HC reduced the abundance of the coeliac toxic peptides P1 and P2 in solution and the contents of secondary structure β-turns and PPII, which are related to reduced allergen immunoreactivity. This meant that both the primary and secondary structures of P1 and P2 were affected by HC, leading to fewer allergic reactions. This study was focused on the impact of HC on the secondary structures of allergens produced from gluten raw materials, and it has positive implications for reducing product allergenicity. [ABSTRACT FROM AUTHOR]

Targeting the class A Beta lactamases Omega loop is an ideal way to combat drug resistance because of its significant role in the catalytic activity and deacylation process inhibition. Therefore, the molecular docking approach with computerized peptide-based in silico screening has been applied for the identification of inhibitors of TEM-type bLs. Among the subjected 105 peptides, Chrombacin (-47.8 KJ/mol), Gassericin A (-35.7 KJ/mol), Duramycin (-34.1 KJ/mol), Brevinin-1DYa (-34.0 KJ/mol), Amoebapore A (-31.2 KJ/mol), Mundticin ATO6 (-29.0 KJ/mol), Lactocyclicin Q (-26.3 KJ/mol), Cinnamycin (-25.9 KJ/mol showed highest binding energy. Among the peptides that showed the highest docking score Elafin, Cinnamycin, Duramycin interacted with Lys 73 of the a domain of catalytic residues of TEM-1 Beta lactamases, whereas Taromycin A, Gassericin A interacted with Lys 234 of the b domain, depicting a strong inhibition and also exhibited desirable physicochemical properties. Hence further in vitro examination of these cyclic peptides against the resistant strains is warranted to help design further novel inhibitors based on their scaffolds and also for the development of an effective drug combination regime. [ABSTRACT FROM AUTHOR]

Introduction: Prior to the introduction of novel food ingredients into the food supply, safety risk assessments are required, and numerous prediction models have been developed and validated to evaluate safety. Methods: The allergenic risk potential of Helaina recombinant human lactoferrin (rhLF, Effera™), produced in Komagataella phaffii (K. phaffii) was assessed by literature search, bioinformatics sequence comparisons to known allergens, glycan allergenicity assessment, and a simulated pepsin digestion model. Results: The literature search identified no allergenic risk for Helaina rhLF, K. phaffii, or its glycans. Bioinformatics search strategies showed no significant risk for cross-reactivity or allergenicity between rhLF or the 36 residual host proteins and known human allergens. Helaina rhLF was also rapidly digested in simulated gastric fluid and its digestibility profile was comparable to human milk lactoferrin (hmLF), further demonstrating a low allergenic risk and similarity to the hmLF protein. Conclusion: Collectively, these results demonstrate a low allergenic risk potential of Helaina rhLF and do not indicate the need for further clinical testing or serum IgE binding to evaluate Helaina rhLF for risk of food allergy prior to introduction into the food supply. [ABSTRACT FROM AUTHOR]

Ovalbumin (OVA) is the most abundant protein in egg white, with excellent functional properties (e.g., gelling, foaming, emulsifying properties). Nevertheless, OVA has strong allergenicity, which is usually mediated by specific IgE thus results in gut microbiota dysbiosis and causes atopic dermatitis, asthma, and other inflammation actions. Processing technologies and the interactions with other active ingredients can influence the functional properties and allergic epitopes of OVA. This review focuses on the non-thermal processing technologies effects on the functional properties and allergenicity of OVA. Moreover, the research advance about immunomodulatory mechanisms of OVA-mediated food allergy and the role of gut microbiota in OVA allergy was summarized. Finally, the interactions between OVA and active ingredients (such as polyphenols and polysaccharides) and OVA-based delivery systems construction are summarized. Compared with traditional thermal processing technologies, novel non-thermal processing techniques have less damage to OVA nutritional value, which also improve OVA properties. OVA can interact with various active ingredients by covalent and non-covalent interactions during processing, which can alter the structure or allergic epitopes to affect OVA/active components properties. The interactions can promote OVA-based delivery systems construction, such as emulsions, hydrogels, microencapsulation, nanoparticles to encapsulate bioactive components and monitor freshness for improving foods quality and safety. [ABSTRACT FROM AUTHOR]

Bovine casein (CN) is abundant in cow milk (CM) and is a major allergen in CM. Recently, several studies have investigated the allergenicity of CN in vivo and in vitro. In this study, the potential antigenicity of enzymatically hydrolyzed CN in vitro was evaluated, and the results showed that Alcalase hydrolysis remarkably reduced the IgG-binding capacity of CN by 36.22–77.84%. Additionally, the IgE-binding capacity of CN was reduced by Alcalase (65.29%) and Protamex (68.49%) treatments. The allergenicity of CN in vivo was also assessed, and the results showed that the allergic symptoms of BALB/c mice were effectively relieved; the levels of IgG, IgE, mMCP-1, histamine, and Th2-related cytokines were reduced; and allergic inflammation of the lungs, jejunum, and spleen was significantly alleviated. These findings suggest that Alcalase, Protamex, and Flavourzyme hydrolysis could effectively reduce sensitization to CN, and our research provides a foundation for developing hypoallergenic dairy products. [ABSTRACT FROM AUTHOR]

Targeting the class A Beta lactamases Omega loop is an ideal way to combat drug resistance because of its significant role in the catalytic activity and deacylation process inhibition. Therefore, the molecular docking approach with computerized peptide-based in silico screening has been applied for the identification of inhibitors of TEM-type βLs. Among the subjected 105 peptides, Chrombacin (-47.8 KJ/mol), Gassericin A (-35.7 KJ/mol), Duramycin (-34.1 KJ/mol), Brevinin-1DYa (-34.0 KJ/mol), Amoebapore A (-31.2 KJ/mol), Mundticin ATO6 (-29.0 KJ/mol), Lactocyclicin Q (-26.3 KJ/mol), Cinnamycin (-25.9 KJ/mol showed highest binding energy. Among the peptides that showed the highest docking score Elafin, Cinnamycin, Duramycin interacted with Lys 73 of the α domain of catalytic residues of TEM-1 Beta lactamases, whereas Taromycin A, Gassericin A interacted with Lys 234 of the β domain, depicting a strong inhibition and also exhibited desirable physicochemical properties. Hence further in vitro examination of these cyclic peptides against the resistant strains is warranted to help design further novel inhibitors based on their scaffolds and also for the development of an effective drug combination regime.

ABSTRACTSince the first genetically engineered or modified crops or organisms (GMO) were approved for commercial production in 1995, no new GMO has been proven to be a hazard or cause harm to human consumers. These modifications have improved crop efficiency, reduced losses to insect pests, reduced losses to viral and microbial plant pathogens and improved drought tolerance. A few have focused on nutritional improvements producing beta carotene in Golden Rice. Regulators in the United States and countries signing the CODEX Alimentarius and Cartagena Biosafety agreements have evaluated human and animal food safety considering potential risks of allergenicity, toxicity, nutritional and anti-nutritional risks. They consider risks for non-target organisms and the environment. There are no cases where post-market surveillance has uncovered harm to consumers or the environment including potential transfer of DNA from the GMO to non-target organisms. In fact, many GMOs have helped improve production, yield and reduced risks from chemical insecticides or fungicides. Yet there are generic calls to label foods containing any genetic modification as a GMO and refusing to allow GM events to be labeled as organic. Many African countries have accepted the Cartagena Protocol as a tool to keep GM events out of their countries while facing food insecurity. The rationale for those restrictions are not rational. Other issues related to genetic diversity, seed production and environmental safety must be addressed. What can be done to increase acceptance of safe and nutritious foods as the population increases, land for cultivation is reduced and energy costs soar?

Bioaerosols are a subset of important airborne particulates that present a substantial human health hazard due to their allergenicity and infectivity. Chemical reactions in atmospheric processes can significantly influence the health hazard presented by bioaerosols; however, few studies have summarized such alterations to bioaerosols and the mechanisms involved. In this paper, we systematically review the chemical modifications of bioaerosols and the impact on their health effects, mainly focusing on the exacerbation of allergic diseases such as asthma, rhinitis, and bronchitis. Oxidation, nitration, and oligomerization induced by hydroxyl radicals, ozone, and nitrogen dioxide are the major chemical modifications affecting bioaerosols, all of which can aggravate allergenicity mainly through immunoglobulin E pathways. Such processes can even interact with climate change including the greenhouse effect, suggesting the importance of bioaerosols in the future implementation of carbon neutralization strategies. In summary, the chemical modification of bioaerosols and the subsequent impact on health hazards indicate that the combined management of both chemical and biological components is required to mitigate the health hazards of particulate air pollution.

The Middle East has witnessed a greater spread of infectious Dengue viruses, with serotype 2 (DENV-2) being the most prevalent form. Through this work, multi-epitope peptide vaccines against DENV-2 that target E and nonstructural (NS1) proteins were generated through an immunoinformatic approach. MHC class I and II and LBL epitopes among NS1 and envelope E proteins sequences were predicted and their antigenicity, toxicity, and allergenicity were investigated. Studies of the population coverage denoted the high prevalence of NS1 and envelope-E epitopes among different countries where DENV-2 endemic. Further, both the CTL and HTL epitopes retrieved from NS1 epitopes exhibited high conservancies' percentages with other DENV serotypes (1, 3, and 4). Three vaccine constructs were created and the expected immune responses for the constructs were estimated using C-IMMSIM and HADDOCK (against TLR 2,3,4,5, and 7). Molecular dynamics simulation for vaccine construct 2 with TLR4 denoted high binding affinity and stability of the construct with the receptor which might foretell favorable in vivo interaction and immune responses. [ABSTRACT FROM AUTHOR]

This study aimed to assess the effect of novel thermal glycation, utilizing microwave processing (100−150 °C) combined with sugars (glucose and lactose), on the in vitro protein digestibility, peptides, secondary structures, microstructures, and allergenic properties of Atlantic cod. The research demonstrated that microwave heating at 150 °C with glucose significantly reduced cod allergenicity by up to 16.16%, while also enhancing in vitro protein digestibility to 69.05%. Glucose was found to be more effective than lactose in conjunction with microwave heating in reducing the allergenicity of Atlantic cod. Moreover, treatments conducted at 150 °C were more effective in increasing in vitro protein digestibility and peptide content compared to those at 100 °C. This study revealed that the novel processing technique of thermal glycation effectively reduced the allergenicity of Atlantic cod. It also offered fresh insights into the potential benefits of combining microwave heating with sugars. [ABSTRACT FROM AUTHOR]

Summary: Sesame has been included in the top eight food allergens, and therefore reduction of sesame allergen potency is of great practical significance. Glycation reactions are extensively researched for their role in regulating the allergic properties of food allergens due to their distinct benefits. This study involved the glycation of sesame proteins with three different reducing sugars to generate reaction products. The structure of the reaction products was characterized by the use of spectroscopic and chromatographic techniques. The impact of glycation on the allergenic properties of sesame proteins was explored by in vitro simulated digestion tests combined with immunological techniques. The study results indicated that all three reducing sugars underwent glycation with sesame proteins, with D‐ribose showing the most significant level of glycation. During the glycation reaction of sesame proteins in this study, the proteins underwent precipitation as well as structural changes, leading to reduced immunoglobulin G (IgG) binding capacity. Glycation alters the digestive stability of sesame proteins and further reduces the ability to bind to IgG. Overall, glycation modification shows promise in decreasing the allergenicity of sesame. [ABSTRACT FROM AUTHOR]

The β′-component, a major allergen found in fish roe, is synthesized in the liver of female fish as part of the precursor of the egg yolk protein vitellogenin (Vg). Vg is distributed through the bloodstream and contributes to ovary development. In the present study, β′-component, present in Vg fragments, was detected in the muscles and internal organs of mature female salmon, with concentrations exceeding the recommended labeling level under Japan's food allergy labeling system. Additionally, total protein extracted from tissues of female salmon reacted with immunoglobulin E antibody against the salmon roe β′-component. No β′-component was detected in the tissues of mature male fish in the absence of sex hormone stimulation from females nor in immature salmon without sexual differentiation, but excess stimulation of the female sex hormone induced Vg synthesis containing the β′-component in the male fish. These findings suggest that taking into account fish sex, maturity, and sexual isolation of mature male fish could improve the safety of salmon meat for individuals with salmon roe allergy. [ABSTRACT FROM AUTHOR]

Summary: Proteins of animal origin have been used in various food formulations as they have been shown to possess excellent techno‐functional properties such as gel formation, emulsification, foam ability and stability, among others. However, the production of proteins from animal sources does come at an environmental cost due to the greenhouse effect that is attributable to the rearing of animals. To mitigate against the environmental impact of the production of protein from animal origin, research has focused on alternative proteins such as those of plant, insect or mycoprotein origin. However, there are still several issues as well as mapping of alternative proteins in terms of their nutritional profile, sensorial attributes that include taste and texture as well and the challenges that exist in mimicking proteins of animal origin that need to be addressed which would broaden the window of application of alternative proteins. Therefore, this review explores some of the alternative protein sources that have been characterised in terms of their techno‐functional characteristics and underpins the challenges such as allergenicity that exist in the use of alternative. Furthermore, this work aims to evaluate consumer perception and acceptance of alternative proteins which is pivotal in their success in food production and process as well as ensuring the safety of these proteins. As such, this work will contribute towards the existing knowledge on the possible applications of these proteins as sustainable, cheaper solutions. [ABSTRACT FROM AUTHOR]

Bovine casein is a major allergen present in cow milk to induce anaphylaxis. In this study, the potential allergenicity of enzymatically hydrolyzed casein (HC) was evaluated based on in vitro and in vivo. The results showed that Alcalase and Protamex treatment (AT, PT) reduced the potential allergenicity of CN, with the greatest reductions of 68.25% and 50.75%, respectively. In addition, in vivo results showed that HC effectively alleviated allergic response symptoms of Balb/c mice; a significant tendency toward decreased serum IgG1 and mast cell tryptase levels was observed, accompanied by a decrease of Th2‐associated IL‐4, IL‐5, and IL‐13 and an increase of IFN‐γ levels in spleen. Moreover, the inflammation of the lung, jejunum, and ileum was remarkably ameliorated. The findings indicated that HC induced a shift toward Th1 response and maintained the Th1/Th2 immune balance. Importantly, our results provide the basis for the production of hypoallergenic dairy products. [ABSTRACT FROM AUTHOR]

In this study, the interaction mechanism of isoflavones with β-conglycinin (BGG) and its effect on the structure and potential allergenicity of their complex were investigated. Fluorescence spectroscopy and circular dichroism spectroscopy were used to analyze the types of quenching, the number of binding sites, the types of forces and the secondary structure content of BGG complexes with one of the two soy isoflavones genistein (Gen) and daidzein (Dai). The structure of isoflavone-BGG complexes prepared under different conditions was characterized, and the potential allergenicity of the complexes were detected by enzyme linked immunosorbent assay (ELISA) and Western blotting. The result showed that isoflavones caused a static quench of the fluorescence of BGG, and the interaction was dominated by hydrophobic interactions, with one binding site. Furthermore, the interaction with isoflavones induced an increase in the polarity of the amino acid microenvironment of BGG, which led to unfolding of the peptide chain and a looser structure. ELISA and immunoblotting of digestion products showed that the potential allergenicity of the protein was enhanced by the binding of isoflavones. The results of this study would be helpful to understand how isoflavones affect the allergenicity of allergenic proteins in complex food matrices, and be significant for its further development and utilization for allergenicity reduction.

To compare the allergenicity of native arginine kinase (nAK) and recombinant AK (rAK) from Scylla paramamosain and to identify the predominant allergenic domain of AK, AK was divided into 4 fragments: AK-E1 (amino acid (AA) 1–92), AK-E2 (AA 87–187), AK-E3 (AA 172–265), and AK-E4 (AA 276–357) based on the distribution of epitopes and the spatial structure of the AK molecule. The four recombinant fragments were expressed in the prokaryotic system Escherichia coli, and then nAK, rAK, and the recombinant fragments were purified. The allergenicity of recombinant proteins were evaluated using BALB/c mice. The results showed that the levels of specific antibodies in the serum and the secretion of Th2 type cytokines by the splenocytes of mice sensitized with rAK significantly increased, but the immunogenicity of rAK was weaker than that of nAK. Among the 4 fragments of AK, AK-E2 had the strongest immunogenicity. Meanwhile, rAK could stimulate RBL-2H3 cells to release β-hexokinase, but it was less effective than nAK. Among the 4 expressed fragments, AK-E2 and AK-E4 had a stronger stimulating effect on effector cells. In conclusion, the rAK expressed in the prokaryotic system showed weaker immunogenicity than nAK, and among the 4 fragments of AK, AA 87–187 has the strongest immunogenicity while AA 276–357 has the strongest immunoreactivity.

AbstractThe food matrix is a complex system encompassing all constituent elements in food production. It influences the digestibility of these elements through direct interactions and affects the digestive environment. Furthermore, the gastrointestinal system possesses precise mechanisms that efficiently process dietary components into essential nutrients, effectively preventing the onset of abnormal immune responses or dysfunctional host reactions in most instances. However, the incidence of adverse food reactions is constantly increasing, and evidence indicates that this process is environmental. Adverse reactions can be categorized as toxic or nontoxic. Toxic reactions are dose-dependent and can result from natural compounds, processing-induced substances, or contaminants. Nontoxic reactions like food intolerance and hypersensitivity depend on individual susceptibility and evoke specific pathological and physiological responses. This review aims to elucidate the mechanisms underlying the occurrence of immune- (food allergies and sensitivities) and non-immune-mediated (food intolerance) reactions, emphasizing the fundamental distinctions between these two categories. Enhanced comprehension and distinction of these mechanisms will significantly contribute to advancing preventive and therapeutic approaches and establishing guidelines for food labeling concerning immune-mediated reactions. [ABSTRACT FROM AUTHOR]

Kiwifruit is widely consumed in many parts of the world. They contain a variety of bioactive substances that make them a valuable functional food source. For instance, kiwifruit contains vitamin C, polysaccharides, polyphenols (catechin, anthocyanin, chlorogenic acid, gallic acid), alkaloids (aconitine, safranin, actinidine), and terpenoids (ursolic acid, oleanolic acid), which are claimed to exhibit antioxidant, anti-inflammatory, and anticancer effects, as well as protecting against cardiovascular and cerebrovascular diseases. However, the potentially beneficial effects of most of these bioactive substances have still not been confirmed by clinical trials. This article reviews recent research on the type and physiological functions of the main bioactive components in kiwifruit. The techniques required to extract and characterize these components are discussed, as well as current challenges in kiwifruit processing. Several innovative extraction techniques have been utilized to extract bioactive substances from kiwifruits, including ultrasound- and microwave-assisted methods. Moreover, several non-thermal processing methods (such as ultrasound, high-pressure, and pulsed electric field processing) are being used to reduce the losses and increase the activity of bioactive substances, preserve the sensory qualities of the fruit, and reduce the allergenicity of kiwifruit. [ABSTRACT FROM AUTHOR]

Petrolatum, also known as petroleum jelly, is a widely used topical agent, with a variety of uses in dermatology. Despite its popularity, many myths surround this ubiquitous dermatologic staple. This review details the history of petrolatum and how it is manufactured as well as how its biologic properties make it a great moisturizer. Additionally, data on its potential for flammability, allergenicity, and comedogenicity are detailed, dispelling misconceptions about petrolatum use around oxygen and as a cause of acne. The uses and benefits of petrolatum in dermatology are wide-ranging—a patch test instrument, a vehicle for medicated ointments, and a wound care essential. Given its ubiquitous presence, it is important for dermatologists to understand the history, safety profile, and myths surrounding this humble skincare staple. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

BACKGROUND: Wheat gluten (WG) containing gliadin and glutenin are considered the main allergens in wheat allergy as a result of their glutamine‐rich peptides. Deamidation is a viable and efficient approach for protein modifications converting glutamine into glutamic acid, which may have the potential for allergenicity reduction of WG. RESULTS: Deamidation by citric acid was performed to investigate the effects on structure, allergenicity and noodle textural properties of wheat gluten (WG). WG was heated at 100 °C in 1 m citric acid to yield deamidated WG with degrees of deamidation (DD) ranging from DWG‐25 (25% DD) to DWG‐70 (70% DD). Fourier‐transform infrared and intrinsic fluorescence spectroscopy results suggested the unfolding of WG structure during deamidation, and sodium dodecyl sulphate‐polyacrylamide gel electrophoresis showed molecular weight shifts at the 35–63 kDa region, suggesting that the deamidation mainly occurred on low molecular weight glutenin subunits and γ‐ gliadin of the WG. An enzyme‐linked immunosorbent assay of deamidated WG revealed a decrease in absorbance and immunoblotting indicated that the intensities of protein bands at 35–63 kDa decreased, which suggested that deamidation of WG might have caused a greater loss of epitopes than the generation of new epitopes caused by unfolding of WG, and thereby reduction of the immunodominant immunoglobulin E binding capacity, ultimately leading to the decrease in allergenicity. DWG‐25 was used in the preparation of recombinant hypoallergenic noodles, and the hardness, elasticity, chewiness and gumminess were improved significantly by the addition of azodicarbonamide. CONCLUSION: The present shows the potential for deamidation of the WG products used in novel hypoallergenic food development. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

High hydrostatic pressure (HHP) has gained prominence in the food processing industry over the last decade. In addition to the effectiveness of microbial and enzymatic inactivation, HHP directly impacts protein structures and properties. Accordingly, this review article aims to consolidate relevant research findings elucidating the effects of HHP on protein structure, allergenicity, bioactivities, and functional properties across diverse protein sources. They encompass cereals, legumes, nuts, meat, poultry products, milk, eggs, seafood, algae, insects, seeds, and vegetables. This review provides insights into the consistent trends of HHP effects on each protein source. In conclusion, HHP induces alterations in non-covalent bonds within protein structures, leading to the unfolding of their interior regions and consequential changes in their properties. Remarkably, the allergenicity of cereals, legumes, and nuts decreases while their bioactivities and digestibility escalate. The disruption of non-covalent bonds during HHP results in the exposure of the interior hydrophobic regions to the surface microenvironment, thereby enhancing the surface hydrophobicity of proteins, particularly those derived from seeds and vegetables. HHP weakens the allergenicity and elevates the foaming properties of proteins from dairy products, including improving the gelling properties and antioxidant activities of egg proteins. Texture profiles of meat and poultry, particularly hardness, are enhanced. Furthermore, HHP demonstrates the potential to diminish the allergenicity of seafood proteins and augment insect protein bioactivities. Lastly, HHP enhances the extraction of algal bioactive components, improving their nutritional quality. [ABSTRACT FROM AUTHOR]

Marburg virus (MARV) is one of the deadliest zoonotic viruses, causing severe hemorrhagic fever in humans with high mortality rates. The development of an effective vaccine is crucial to prevent potential Marburg virus outbreaks. In this study, an in silico approach was employed to design an epitope-based vaccine to prevent MARV infections. The MARV proteins nominating NP, VP24, VP35, VP30, VP40, GP & Polymerase L was analyzed for antigenicity and non-allergenicity prediction, among these proteins VP30 protein has a 0.5636 (Probable Antigen) score and it was non-allergen. For that reason, VP30 was selected for further in silico analysis. After analysis it is found that the top ranked T-cell (MHC-I) epitopes LSKPPPPPK, ESSPTNHIPR, TQLPSKPHY, SPQDCGSPSL, FEAALWQGW, T-Cell (MHC-II) epitopes IHLDKGGQF, INTMTELHM, VTPTIYHET, YTNYHPRAR, YTGIHLDKG was epitopes & B-Cell epitopes SEIGKLDET, IHLDKGGQF, MNHENLPQDQNGV, PTCNRDHDLDNLTN was found non-toxic and non-allergen. The T-Cell (MHC-I) epitope TQLPSKPHY,T-Cell (MHC-II)epitope YTNYHPRAR & B-Cell epitope SEIGKLDET was found highly antigenic, non-toxic as well as non-allergen and it was selected for molecular docking analysis. The T-Cell (MHC-I) epitope TQLPSKPHY,T-Cell (MHC-II) epitope YTNYHPRAR shows strong structural similarity and potential binding affinity with antibody. The B-Cell epitope SEIGKLDET shows poor affinity towards antibody. In silico analysis indicate that both T-Cell epitopes becomes an effective peptide vaccine to prevent MARV infection. Our findings highlight the promise of in silico vaccine design in accelerating the development of vaccines against MARV, a highly pathogenic virus with no effective cure currently available. [ABSTRACT FROM AUTHOR]

Copyright of Modern Food Science & Technology is the property of Editorial Office of Modern Food Science & Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Electric field-based technologies offer interesting perspectives which include controlled heat dissipation (via the ohmic heating effect) and the influence of electrical variables (e.g., electroporation). These factors collectively provide an opportunity to modify the functional and technological properties of numerous food proteins, including ones from emergent plant- and microbial-based sources. Currently, numerous scientific studies are underway, contributing to the emerging body of knowledge about the effects on protein properties. In this review, "Electric Field Processing" acknowledges the broader range of technologies that fall under the umbrella of using the direct passage of electrical current in food material, giving particular focus to the ones that are industrially implemented. The structural and biological effects of electric field processing (thermal and non-thermal) on protein fractions from various sources will be addressed. For a more comprehensive contextualization of the significance of these effects, both conventional and alternative protein sources, along with their respective ingredients, will be introduced initially. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

BACKGROUND: The interaction between food allergens and plant polyphenols has become a safe and effective management strategy to prevent food allergies. Ovalbumin (OVA) is the most abundant allergen in egg whites. Resveratrol (RES) is a plant polyphenol that is abundant in red grapes, berries, and peanuts, and has an anti‐allergic effect on allergy‐related immune cells. However, there is little information about the effect of RES on the allergenicity of OVA. In this study, the effect of RES on the allergenicity of OVA was investigated. RESULTS: Molecular docking and spectroscopic studies indicated that the addition of RES changed the structure of OVA. The digestion and transfer rate of OVA–RES were effectively improved with an in vitro gastrointestinal digestion model and Caco‐2 cell model, especially when the molar ratio of OVA–RES was 1:20. Meanwhile, the KU812 cell degranulation assay proved that the potential allergenicity was remarkably decreased while the molar ratios of OVA–RES were increased to 1:20. Furthermore, hydrogen bonds and van der Waals forces were the dominating forces to stabilize the OVA–RES complexes. CONCLUSION: All the findings demonstrated that the potential allergenicity of OVA was reduced when interacting with RES, and RES can be a potential food material for preparing a hypoallergenic protein, especially for egg allergy. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

IntroductionPrior to the introduction of novel food ingredients into the food supply, safety risk assessments are required, and numerous prediction models have been developed and validated to evaluate safety.MethodsThe allergenic risk potential of Helaina recombinant human lactoferrin (rhLF, Effera™), produced in Komagataella phaffii (K. phaffii) was assessed by literature search, bioinformatics sequence comparisons to known allergens, glycan allergenicity assessment, and a simulated pepsin digestion model.ResultsThe literature search identified no allergenic risk for Helaina rhLF, K. phaffii, or its glycans. Bioinformatics search strategies showed no significant risk for cross-reactivity or allergenicity between rhLF or the 36 residual host proteins and known human allergens. Helaina rhLF was also rapidly digested in simulated gastric fluid and its digestibility profile was comparable to human milk lactoferrin (hmLF), further demonstrating a low allergenic risk and similarity to the hmLF protein. ConclusionCollectively, these results demonstrate a low allergenic risk potential of Helaina rhLF and do not indicate the need for further clinical testing or serum IgE binding to evaluate Helaina rhLF for risk of food allergy prior to introduction into the food supply.

Two monosaccharides, glucose and xylose, were used as glycosyl donors to investigate the effects of reaction time, reaction temperature, protein-to-sugar ratio and protein concentration on the wet glycosylation reaction of soybean protein isolate. The allergenicity of SPI-glucose derivative (SPI-glucose) and SPI-xylose derivative (SPI-xylose) was analyzed. SPI-glucose and SPI-xylose were used to produce the hypo-allergenic Chiba tofu. The results showed that xylose was more likely to glycosylate with SPI than glucose, but it was also more likely to produce melanoidin. The highest degree of glycosylation reaction was observed at the protein concentration of 25 mg/mL. The degree of glycosylation reaction was positively correlated with the reaction temperature, reaction time, and the amount of sugar added. The results of SDS-PAGE and fourier transform infrared spectroscopy showed that glycosylation caused covalent binding of SPI and sugar molecules, and the free amino group content of SPI was reduced. The degree of glycosylation reaction was negatively correlated with the allergenicity of SPI, and the allergenicity of SPI-xylose could be reduced by up to 50%. Chiba tofu made from SPI-xylose using glutamine aminotransferase (TGase) had good elasticity and chewiness.

Pollinosis is one of the common allergic diseases, and its morbidity continues to increase. Studies have demonstrated that air pollution is a key environmental factor that leads to the increased prevalence of pollinosis. Air pollutants and pollen allergens exert synergistic effects in stimulating allergic responses in susceptible individuals. In this article, we analyzed the relationship between air pollution and pollinosis based on the latest studies, and elaborated potential mechanisms on how air pollution increases the incidence of pollinosis and aggravates allergic reactions. Air pollutants can increase both pollen production and the levels of allergenic proteins, and enhance allergenicity of pollen allergens through structural alterations or chemical modifications. The potential mechanisms of air pollutants exacerbating pollen allergies are as follows: Air pollutants may disrupt the barrier function of the respiratory epithelium and facilitate the penetration of pollen allergens into deeper tissues. Additionally, they may accelerate the process of the release of pollen allergy-related cytokines, promoting T helper 2 (Th2) cell differentiation and exacerbating inflammatory responses in the airways. Given the limitations of existing research, future prospective studies are needed to explore the effects of mixed pollutants and different types of pollutants on pollen, and the response mechanisms of allergy-related cells and cytokines to different pollutant categories. The findings would provide a comprehensive understanding of the impacts of air pollution on pollen allergies and scientific evidence for effective protection of the heath of pollinosis patients.

Shrimp (Penaeus vannamei) proteins have been shown an allergenic potential; however, little information is available on the sensitizing and eliciting capacity of shrimp protein digestion products. In this study, a BALB/c mice model was used to explore the allergenicity of shrimp protein sample (SPS) and their gastric and gastrointestinal digestion products (GDS/GIDS). As compared with the SPS groups, the GDS/GIDS groups caused lower specific immunoglobulins (IgE/IgG1) levels (P < 0.05), but higher than the control groups, indicating that the digestion products sensitized the mice. Meanwhile, spleen index, mouse mast cell protease-1 (mMCP-1) concentration and proportion of degranulated mast cells were significantly reduced in the GDS/GIDS groups (P < 0.05); simultaneously, allergic symptoms, vascular permeability and histopathological changes of tissues were alleviated. Nevertheless, the allergenicity of digestion products cannot be eliminated and still cause systemic allergic reactions in mice. The study showed that the digestion products of shrimp still had high sensitizing and eliciting capacity.

In recent years, milk allergy has attracted more and more attention because of its increasing incidence and in-depth research on it. The glycosylation modification of milk proteins not only can improve the functional properties of dairy products, but also reduce the allergenicity of dairy products by destroying or shielding the epitope of allergen proteins. This modification has found applications in various fields such as food flavor, antioxidants and carriers. This paper introduces common glycosylation reactions in the dairy industry, discusses their advantages and disadvantages and the pattern of changes in functional properties and allergenicity of milk proteins after glycosylation, and summarizes the methods to avoid the negative effects of glycosylation reactions. This review provides a reference for the research, development and application of glycosylation modification in milk allergy and dairy processing.

Kidney beans are one of the most important economic legumes in China, and are cultivated extensively worldwide for their high nutritional value. However, food safety incidents caused by improper or inadequate cooking of kidney beans have occurred from time to time, which are generally believed to be associated with the toxicological effects of kidney bean lectins. Immunological studies show that lectins may be the major allergen in kidney beans, which have attracted significant research interest in foreign countries but have not been systematically reported in China. Therefore, in order to provide a theoretical basis for the development of hypoallergenic kidney bean foods and the rational development and utilization of kidney bean proteins, this article summarizes recent progress in immunological research on kidney bean lectins, analyzes the evidence that kidney bean lectins are allergens, and reviews food processing strategies for reducing the allergenicity of kidney bean lectins.

Total RNA was extracted from sesame seeds, and the sesame Ses i 3 gene was obtained by using reverse transcription-polymerase chain reaction (RT-PCR). The plasmid pET-22b(+) was used to construct an expression vector, and the recombinant plasmid was transformed into competent Escherichia coli BL21 (DE3) host cells for induced expression. The expressed protein was purified by Ni2+-affinity chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that the molecular mass of the expressed protein was approximately 66 kDa. The ability of the recombinant and native Ses i 3 protein to induce sesame allergy in mice was compared by using a BALB/c mouse allergy model, which was found to be similar by measuring specific antibodies (immunoglobulin E (IgE), IgG1, and IgG2a), cytokines (interleukin (IL)-4, IL-5, interferon-γ (IFN-γ) and histamines). Hence, the recombinant Ses i 3 protein can be used for future studies on the allergenicity of sesame.

Wheat flour, as the most important source of food globally, is one of the most common causative agents of food allergy. This study aimed to investigate the effects of fermentation on wheat protein digestibility and allergenicity. Protein digestibility were evaluated using the sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and enzyme-linked immunosorbent assay. The effect of protein on intestinal permeability was investigated by Caco-2 cell monolayers. Co-culture fermentation with Pediococcus acidilactici XZ31 and yeast leads to improvement in digestibility of wheat protein compared to single strain fermentation. Fermentation leads to a decrease in albumin/globulin antigenicity and an increase in gluten R5 reactivity, with the most significant changes in the co-culture group. Digestion strengthen the decrease of protein antigenicity and counteracts the difference in antigenicity induced by fermentation between groups. However, pretreatment with P. acidilactici XZ31 reduces the amount of allergens across Caco-2 monolayer and attenuates the gluten-induced increase in permeability of Caco-2 cell monolayer by reducing actin polymerization and villous atrophy. Co-culture fermentation reduces gluten-induced cell monolayer damage to a greater extent than P. acidilactici XZ31 monoculture. These results gives valuable insight into the effects of P. acidilactici XZ31 fermentation on the allergenicity and toxicity of wheat proteins, which contribute to promoting the application of multi-strain leavening agent in hypoallergenic and gluten-free wheat products.

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Summary: The production and use of kiwifruit, and their derived products, has seen rapid growth in the food industry with some 4 467 099 tonnes produced in 2021. A key area of development has been the increased use of kiwifruit waste streams to support sustainable food production systems. However, kiwifruit is emerging as a common elicitor of food allergy worldwide. Therefore, the present research focuses on summarising the current literature on kiwifruit‐induced human food allergy. Of the available information, a total of 7098 titles were found and 107 articles were included in the current study following full‐text screening. Most research concentrated on the prevalence of allergenicity and was performed within Europe, North America, Asia, Africa, South America and Oceania. Food allergy to kiwifruit ranged from oral allergy syndrome to anaphylaxis in humans. Few studies considered the need for labelling or public education. Given the increased usage of kiwifruit across a range of food streams, further research is required due to the greater focus on utilisation of these products in the food industry. [ABSTRACT FROM AUTHOR]

Shrimp is a common cause of food allergies in allergic individuals. The management of patients suffering from shrimp allergy relies on avoidance of the specific food, which compromises nutritional requirements. In this study, fermentation was performed using Lactobacillus to reduce the allergenicity of Litopenaeus vannamei. The optimal fermentation conditions using Lactobacillus helveticus TS6024 were 1% glucose, 30% minced shrimp, 2.5% inoculum level, 3% NaCl, and 60 h of incubation at 37°C, whereas those using Lactobacillus acidophilus 6005 were 2% glucose, 20% minced shrimp, 15% inoculum level, 2% NaCl, and 48 h of incubation at 42°C. Under optimal conditions, Lactobacillus helveticus TS6024 and Lactobacillus acidophilus 6005 fermentation reduced the allergenicity of shrimp by 78.97% and 70.09%, respectively. SDS-PAGE analysis showed that the band intensity of tropomyosin (36KDa) reduced evidently after the selected Lactobacillus fermentation. The hypoallergenic shrimp/shrimp products will provide optimal nutrition with reduced risk of adverse reactions in hypersensitive individuals. [ABSTRACT FROM AUTHOR]

Background: Powassan virus (POWV), a vector-borne pathogen primarily impacting humans as incidental hosts, has recently surfaced as a significant worldwide health concern, carrying the potential for severe clinical consequences or enduring neurological sequelae. Currently, there are no approved vaccines for POWV. The key to developing effective vaccines lies in identifying protective factors. Despite significant outbreaks and the absence of antiviral treatments, progress in creating an epitope-based vaccine for POWV has been slow. Aim of the work: Our aim was to employ various immunoinformatics and docking simulation methods to design an epitope-based vaccine capable of triggering a robust immune response and predict inhibitors that could potentially target therapeutic sites effectively. Methodology: At first, the complete POWV proteome was obtained from a database and scrutinized to identify the protein with the highest immunogenicity. The structural attributes of the designated protein were thoroughly explored. Subsequently, the chosen protein underwent testing to assess its capacity to stimulate both humoral and cell-mediated immunity through T and B cells. Results: The leading B cell and T cell epitopes were pinpointed as a peptide segment encompassing 7 amino acids from position 353 to 360, represented by the sequence TLAGPRSKY. This peptide exhibited the potential to interact with up to 19 different HLAs, offering extensive population coverage that ranged from 62.53% to 86.97%. To confirm the binding interaction within the HLA binding cleft, we conducted in-silico docking techniques. Furthermore, we assessed the allergenicity of these epitopes. In our post-therapeutic approach, we predicted the three-dimensional structure, conducted validation and verification processes, and subsequently performed molecular docking studies to identify potential drug-binding sites and suitable therapeutic inhibitors for the target protein. Conclusion: Nevertheless, this computational approach to epitope-based peptide vaccine design and target site prediction against POWV represents a pioneering advancement in Powassan virus research. It's important to note that the outcomes will require validation through in vitro and in vivo trials. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

This review summarized recent studies about the effects of polyphenols on the allergenicity of allergenic proteins, involving epigallocatechin gallate (EGCG), caffeic acid, chlorogenic acid, proanthocyanidins, quercetin, ferulic acid and rosmarinic acid, etc. Besides, the mechanism of polyphenols for reducing allergenicity was discussed and concluded. It was found that polyphenols could noncovalently (mainly hydrophobic interactions and hydrogen bonding) and covalently (mainly alkaline, free-radical grafting, and enzymatic method) react with allergens to induce the structural changes, resulting in the masking or/and destruction of epitopes and the reduction of allergenicity. Oral administration in murine models showed that the allergic reaction might be suppressed by regulating immune cell function, changing the levels of cytokines, suppressing of MAPK, NF-κb and allergens-presentation pathway and improving intestine function, etc. The outcome of reduced allergenicity and suppressed allergic reaction was affected by many factors such as polyphenol types, polyphenol concentration, allergen types, pH, oral timing and dosage. Moreover, the physicochemical and functional properties of allergenic proteins were improved after treatment with polyphenols. Therefore, polyphenols have the potential to produce hypoallergenic food. Further studies should focus on active concentrations and bioavailability of polyphenols, confirming optimal intake and hypoallergenic of polyphenols based on clinical trials. [ABSTRACT FROM AUTHOR]