Vicilin

Abstract: Plant food allergens can be classified into families and superfamilies on the basis of their structural and functional properties. The most widespread groups of plant proteins that contain allergens are the cupin and prolamin superfamilies and the protein families of the plant defense system. The cupin superfamily includes allergenic seed storage proteins of the vicilin and legumin type present in soybeans, peanuts, and tree nuts. The prolamin superfamily includes several important types of allergens of legumes, tree nuts, cereals, fruits, and vegetables, such as the 2S albumin seed storage proteins, the nonspecific lipid transfer proteins, and the cereal α-amylase and protease inhibitors. Plant food allergens are also found among the various groups of defense proteins that enable plants to resist biotic and abiotic stress, such as the pathogenesis-related proteins, certain proteases, and protease inhibitors. This review focuses on a classification system of plant food allergens that is emerging from the synopsis of allergology and protein evolution.

Abstract: Field pea is one of the most important leguminous crops over the world. Pea protein is a relatively new type of plant proteins and has been used as a functional ingredient in global food industry. Pea protein includes four major classes (globulin, albumin, prolamin, and glutelin), in which globulin and albumin are major storage proteins in pea seeds. Globulin is soluble in salt solutions and can be further classified into legumin and vicilin. Albumin is soluble in water and regarded as metabolic and enzymatic proteins with cytosolic functions. Pea protein has a well-balanced amino acid profile with high level of lysine. The composition and structure of pea protein, as well as the processing conditions, significantly affect its physical and chemical properties, such as hydration, rheological characteristics, and surface characteristics. With its availability, low cost, nutritional values and health benefits, pea protein can be used as a novel and effective alternative to substitute for soybean or animal proteins in functional food applications.

Abstract: Extractability, extractable protein compositions, technological-functional properties of pea (Pisum sativum) proteins from six genotypes grown in Serbia were investigated. Also, the relationship between these characteristics was presented. Investigated genotypes showed significant differences in storage protein content, composition and extractability. The ratio of vicilin:legumin concentrations, as well as the ratio of vicilin + convicilin: Legumin concentrations were positively correlated with extractability. Our data suggest that the higher level of vicilin and/or a lower level of legumin have a positive influence on protein extractability. The emulsion activity index (EAI) was strongly and positively correlated with the solubility, while no significant correlation was found between emulsion stability (ESI) and solubility, nor between foaming properties and solubility. No association was evident between ESI and EAI. A moderate positive correlation between emulsion stability and foam capacity was observed. Proteins from the investigated genotypes expressed significantly different emulsifying properties and foam capacity at different pH values, whereas low foam stability was detected. It appears that genotype has considerable influence on content, composition and technological-functional properties of pea bean proteins. This fact can be very useful for food scientists in efforts to improve the quality of peas and pea protein products.