TL;DR: The physical, chemical and immunological characteristics of the legumin and vicilin preparations from Pisum sativum are summarised and the distributions of proteins with sedimentation coefficients and/or immunological determinants similar to those of legumin this article.
TL;DR: HPI can be used as a valuable source of nutrition for infants and children but has poor functional properties when compared with SPI, mainly due to its high free sulfhydryl content from sulfur-containing amino acids.
Abstract: The amino acid composition and physicochemical and functional properties of hemp (Cannabis sativa L.) protein isolate (HPI) were evaluated and compared with those of soy protein isolate (SPI). Edestin, a kind of hexameric legumin, was the major protein component. HPI had similar or higher levels of essential amino acids (except lysine), in comparison to those amino acids of SPI. The essential amino acids in HPI (except lysine and sulfur-containing amino acids) are sufficient for the FAO/WHO suggested requirements for 2−5 year old children. The protein solubility (PS) of HPI was lower than that of SPI at pH less than 8.0 but similar at above pH 8.0. HPI contained much higher free sulfhydryl (SH) content than SPI. Differential scanning calorimetry analysis showed that HPI had only one endothermic peak with denaturation temperature (Td) of about 95.0 °C, attributed to the edestin component. The Td of the endotherm was nearly unaffected by 20−40 mM sodium dodecyl sulfate but significantly decreased by 20 mM d...
TL;DR: 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: 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.
TL;DR: Genotype has considerable influence on content, composition and technological-functional properties of pea bean proteins, and this fact can be very useful for food scientists in efforts to improve the quality of peas and pea protein products.
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.
TL;DR: The refined structure of the seed storage protein phaseolin from the French bean via an alternative crystal form reveals details of the molecule hitherto unobserved and in particular the structural role of conserved residues within the broader 7 S (vicilin) family of seed storage proteins is identified.