Allergenicity Reduction in Plant Proteins

A method to reduce β-lactoglobulin (β-LG) allergenicity through non-covalent binding interactions between β-LG and plant-derived polyphenols. The method employs a combination of β-LG and specific polyphenol extracts derived from longan kernel, which form stable complexes that inhibit β-LG antigenicity without compromising protein solubility, digestibility, or emulsification. The binding process is optimized through pH adjustment and incubation conditions that balance protein stability with biological activity.

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The increasing use of plant protein isolates and hydrolysates as functional ingredients in the food industry, particularly from pulses, is increasing the incidence of allergic reactions in western countries as never before. However, plant-derived ingredients have a fundamental role in the dietary shift to a more sustainable diet as envisaged by the European Green Deal. The cross-allergenicity and the neo-allergenicity assessments are essential in the route of new plant proteins evaluation for their safe introduction in the market. This article describes the decisional tree of allergenicity assessment for novel plant proteins with an eye on the shortcomings of current methodologies.

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The publication of the cDNA sequence of the major birch pollen allergen Bet v 1 in 1989 marked a breakthrough in molecular allergology, while the elucidation of its crystal structure allowed the definition of the Bet v 1-like superfamily of proteins. This chapter examines sequences, structures, evolutionary relationships, and cross-reactivities of Bet v 1 homologous allergens. Despite sequence variations, the conserved Bet v 1 fold leads to IgE cross-reactivity among these allergens. Bet v 1 homologs exhibit diverse ligand binding, including flavonoids, bioactive lipids and cytokinins, impacting stability and allergenicity. Investigating ligands and biological roles of Bet v 1 homologous allergens reveals their impact on stability, allergenicity, and potential biochemical functions intertwining allergology with broader plant biology.

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Nutritional compositions that contain non-soy-based plant proteins, including chia proteins, hemp proteins, or combinations thereof, as a protein source in infant formulas. These compositions provide a complete protein profile, including essential amino acids, while avoiding allergenic soy proteins and high electrolyte levels found in traditional cow's milk-based formulas. The compositions contain non-soy plant proteins that support infant gut health through their unique protein structures and bioactive properties.

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Only a small fraction of proteins in plants and animals are classified as allergens. The allergenic properties are frequently attributed to certain functional characteristics of the proteins, such as a role in the plant defense against biotic and abiotic stress, to achieve the systematic acquired resistance. In line with this, eight members out of 17 functional pathogenesis-related (PR) protein families have been characterized as allergens. The present review summarizes the molecular features and allergenic significance of allergens of the PR-1 family. Not many allergens have been identified as belonging to this protein family, with most of them having a pollen origin, like mugwort or Bermuda grass. Molecular and structural features of allergenic PR-1 proteins are discussed and attributed to their IgE-reactive properties, clinical manifestation, and cross-reactivity among different foods and inhalants.

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A method to reduce peanut protein allergenicity by treating peanut protein with polyphenols and accelerating protein digestion. The method involves contacting peanut protein with polyphenols to form complexes that stabilize the protein structure and reduce allergenicity. This is done by incubating peanut protein with polyphenols like phylloquinone (vitamin K1) or rutin. The complexes formed with phylloquinone showed reduced allergenicity compared to unmodified peanut protein. Additionally, the method involves accelerating protein digestion to promote cross-linking and aggregation of peanut protein, further reducing allergenicity.

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Plant-based proteins have shown great potential as an alternative substitute for animal proteins to meet the increasing global demand. Nevertheless, several limitations mitigate plant-based protein application and utilization. As a panacea to meeting the market demand, it is imperative to modify plant-based proteins to produce improved quality and techno-functionalities compared to conventional animal protein ingredients. Enzymatic, chemical, and physical modifications have been used for plant-based proteins, which have shown exciting results in improving their techno-functional properties, digestibility, and inherent allergenicity. Among these modification methods, the low-cost, limited time, high sensitivity, and high reproducibility give enzymatic modification leverage over chemical and physical methods. This review gave a concise summary of the advantages and disadvantages of enzymatic modifications. The efficacy of enzymatic modification in producing protein ingredients from plant sources with improved techno-functional properties, digestibility, and alleviated allergenicity was... Read More

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Food allergy is an adverse immune response to certain food proteins and is currently estimated to affect about 2% of adults and 8% of children in developed countries. The most common plant sources of food allergens identified include tree nuts, peanuts, wheat, and soy. Allergens in plant proteins are more of the major factors inhibiting their wide applications. Thus, it is important to reduce the allergenicity of plant-based proteins to producing plant protein ingredients with enhanced functionality, digestibility, and nutrient bioavailability. This book chapter provides comprehensive literature of current research work performed on thermal (e.g., boiling, cooking, frying, etc.) and nonthermal food processing techniques (ultrasound, high-pressure processing, pulsed electric field, cold plasma, radiation) for mitigating the allergenicity of plant proteins. These interventions mainly modify the structure of allergens at the molecular level (via deamidation, aggregation, and hydrolysis) or promote the interactions of allergens with other food components. It appears that the structural p... Read More

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Artificial constructs for reducing allergen content in peanut seeds through targeted silencing of specific allergen genes. The constructs utilize antisense RNAi molecules to specifically target and degrade the allergenic proteins in peanut seeds, thereby reducing the allergenic potential of the plant. The antisense RNAi molecules are engineered to be complementary to specific regions of the allergenic proteins, while the sense RNAi molecule provides a complementary sequence that helps in the antisense RNAi's function. The constructs can be delivered through CRISPR-Cas9 gene editing systems, allowing for precise and efficient silencing of the target allergens. This approach enables the production of peanut seeds with significantly reduced allergen content, making them safer for consumption.

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The incidence of food allergy has been increasing in recent years which are related to the unguarded protein allergens. As a new strategy for the allergic protein modification, protein-plant polyphenol interactions as well as the most recently updated knowledges are reviewed in this paper. Various binding modes and intermolecular associations between allergenic proteins and plant polyphenols have been introduced. The sensitization reduction potential has been explored based on the conformational alterations of proteins and biological activities of polyphenols. Moreover, the factors influencing the binding of allergenic proteins to plant polyphenols and the stability of allergenic protein-plant polyphenol complexes were also discussed for the further potential application in the development of hypoallergenic food and clinical treatments.

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Hypoallergenic variants of the Mal d 1 protein, encoding them, pharmaceutical compositions containing them, and their use in immunotherapy of allergic diseases caused by Malus domestica, particularly birch pollen allergy. The variants exhibit reduced IgE-binding activity compared to the wild-type protein, with specific IgE reactivity reduction of at least 10% in sera of patients allergic to birch pollen and apple. These variants can be used in specific immunotherapy, offering a safer alternative to traditional allergen-specific immunotherapy for patients with severe allergic reactions.

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This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Fu... Read More

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Plant lipid transfer proteins (LTPs) are widespread plant food allergens, highly resistant to food processing and to the gastrointestinal environment, which have been described as the most common food allergens in the Mediterranean area. LTP allergy is widely described in adults, but it represents an emerging allergen also in the pediatric population. Little is known about the real prevalence and the clinical features of this allergy in children and it still often remains underdiagnosed in these patients. An early identification and a deeper knowledge of this allergy in childhood can avoid severe systemic reactions and improve the child's quality of life. Pediatricians should always consider the possibility of LTP involvement in cases of plant-derived food allergy.

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A processing technology for soy protein products with reduced allergenicity, enabling safe consumption for individuals with soy allergies. The process employs lactic acid fermentation by lactic acid bacteria, which selectively degrades and masks allergenic epitopes on soy protein while preserving protein nutritional value. This approach addresses the current challenges in developing soy-based food products with reduced allergenicity, particularly for those with soy allergies.

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Recombinant variants of group 5 allergens from true grasses that exhibit reduced IgE reactivity while maintaining T-cell reactivity. These variants are engineered through single-point mutations of specific proline residues in the allergen sequence, with the proline at positions 57, 58, 117, 146, 155, 211, 229 in wild-type Phl p 5.0109 being replaced with different amino acids. The variants retain the ability to induce T-cell responses while significantly reducing IgE-mediated allergic reactions, making them suitable for therapeutic applications like specific immunotherapy and DNA vaccination.

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Plant-derived foods are the most common allergenic sources in adulthood. Owing to the rapidly increasing prevalence of plant food allergies in industrialized countries, the environmental factors are suspected to play a key role in development of allergic sensitization. The present article provides an overview of ways by which chemicals may influence the development and severity of allergic reactions to plant foods, with especial focus on plant allergens up-regulated under chemical stress. In plants, a substantial part of allergens have defense-related function and their expression is highly influenced by environmental stress and diseases. Pathogenesis-related proteins (PR) account for about 25% of plant food allergens and some are responsible for extensive cross-reactions between plant-derived foods, pollen and latex allergens. Chemicals released by anthropogenic sources such as agriculture, industrial activities and traffic-related air pollutants are potential drivers of the increasing sensitization to allergenic PRs by elevating their expression and by altering their immunogenicity... Read More

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Method for reducing soybean allergenicity through alkaline protease treatment, enabling the production of hypoallergenic soybeans. The process involves treating soybeans with alkaline proteases, which selectively degrade the soybean 2S fraction while preserving the protein's functional properties. This selective proteolytic action effectively eliminates allergenic proteins without compromising the soybean's nutritional content. The resulting soybeans exhibit reduced allergenicity, making them suitable for food applications where soybeans are commonly used.

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Among a variety of molecular factors of the plant innate immune system, small proteins that transfer lipids and exhibit a broad spectrum of biological activities are of particular interest. These are lipid transfer proteins (LTPs). LTPs are interesting to researchers for three main features. The first feature is the ability of plant LTPs to bind and transfer lipids, whereby these proteins got their name and were combined into one class. The second feature is that LTPs are defense proteins that are components of plant innate immunity. The third feature is that LTPs constitute one of the most clinically important classes of plant allergens. In this review, we summarize the available data on the plant LTP structure, biological properties, diversity of functions, mechanisms of action, and practical applications, emphasizing their role in plant physiology and their significance in human life.

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Allergen extracts for immunotherapy that minimize the risk of angioedema through reduced copper-binding protein content. The extracts contain purified Ambrosia pollen allergens with specifically targeted reduction of copper-binding proteins, specifically protein A, B, C, and D. This approach enables the formulation of allergen extracts with significantly lower levels of these proteins, which are known to induce vascular permeability and angioedema in patients undergoing immunotherapy. The extracts are prepared through a targeted reduction process that selectively depletes the copper-binding proteins without compromising the allergen's immunogenic properties.

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The right choice of analytical methods for plant allergen quantification is a deciding factor for the correct assessment and labeling of allergens in processed food in view of consumer protection. The aim of the present study was to develop a validated target peptide multi-method by LC/MS/MS providing high specificity and sensitivity for plant allergen protein detection, plant identification in vegan or vegetarian products using peptide markers for quantification. The methodical concept considers the selection of target peptides of thermostable allergenic plant proteins (Gly m6 soy, Ses i6 sesame and -conglutin from white lupine) by data base research, BLAST and in silico digestion using Skyline software. Different allergenic concentration levels of these proteins were integrated into our own reference bakery products and quantified with synthesized isotopically labeled peptides after in-solution digestion using LC/MS/MS. Recovery rates within the range of 70113% and LOQ of 10 ppm50 ppm (mg allergenic food/kg) could be determined. The results are independent of thermal processing ... Read More

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