A bean is the seed of any plant in the legume family (Fabaceae) used as a vegetable for human consumption or animal feed. The seeds are often preserved through drying, but fresh beans are also sold. Most beans are traditionally soaked and boiled, but they can be cooked in many different ways, including frying and baking, and are used in many traditional dishes throughout the world. The unripe seedpods of some varieties are also eaten whole as green beans or edamame, but fully ripened beans contain toxins like phytohemagglutinin and require cooking.
Casein is a family of related phosphoproteins that are commonly found in mammalian milk, comprising about 80% of the proteins in cow's milk and between 20% and 60% of the proteins in human milk. Sheep and cow milk have a higher casein content than other types of milk with human milk having a particularly low casein content.
Sprouting is the natural process by which seeds or spores germinate and put out shoots, and already established plants produce new leaves or buds, or other structures experience further growth.
Legumes are plants in the family Fabaceae, or the fruit or seeds of such plants. When used as a dry grain for human consumption, the seeds are also called pulses. Legumes are grown agriculturally, primarily for human consumption, but also as livestock forage and silage, and as soil-enhancing green manure. Well-known legumes include beans, chickpeas, peanuts, lentils, lupins, mesquite, carob, tamarind, alfalfa, and clover. Legumes produce a botanically unique type of fruit – a simple dry fruit that develops from a simple carpel and usually dehisces on two sides.
The globulins are a family of globular proteins that have higher molecular weights than albumins and are insoluble in pure water but dissolve in dilute salt solutions. Some globulins are produced in the liver, while others are made by the immune system. Globulins, albumins, and fibrinogen are the major blood proteins. The normal concentration of globulins in human blood is about 2.6-3.5 g/dL.
Lathyrus sativus, also known as grass pea, cicerchia, blue sweet pea, chickling pea, chickling vetch, Indian pea, white pea and white vetch, is a legume commonly grown for human consumption and livestock feed in Asia and East Africa. It is a particularly important crop in areas that are prone to drought and famine, and is thought of as an 'insurance crop' as it produces reliable yields when all other crops fail. The seeds contain a neurotoxin that causes lathyrism, a neurodegenerative disease, if eaten as a primary protein source for a prolonged period.
Vicia is a genus of over 240 species of flowering plants that are part of the legume family (Fabaceae), and which are commonly known as vetches. Member species are native to Europe, North America, South America, Asia and Africa. Some other genera of their subfamily Faboideae also have names containing "vetch", for example the vetchlings (Lathyrus) or the milk-vetches (Astragalus). The lentils are included in genus Vicia, and were formerly classified in genus Lens. The broad bean is sometimes separated in a monotypic genus Faba; although not often used today, it is of historical importance in plant taxonomy as the namesake of the order Fabales, the Fabaceae and the Faboideae. The tribe Vicieae in which the vetches are placed is named after the genus' current name. The true peas (Pisum) are among the closest living relatives of vetches.
Neurolathyrism, is a neurological disease of humans, caused by eating certain legumes of the genus Lathyrus. This disease is mainly associated with the consumption of Lathyrus sativus and to a lesser degree with Lathyrus cicera, Lathyrus ochrus and Lathyrus clymenum containing the toxin ODAP.
Gliadin is a class of proteins present in wheat and several other cereals within the grass genus Triticum. Gliadins, which are a component of gluten, are essential for giving bread the ability to rise properly during baking. Gliadins and glutenins are the two main components of the gluten fraction of the wheat seed. This gluten is found in products such as wheat flour. Gluten is split about evenly between the gliadins and glutenins, although there are variations found in different sources.
Hexosaminidase is an enzyme involved in the hydrolysis of terminal N-acetyl-D-hexosamine residues in N-acetyl-β-D-hexosaminides.
α-Bungarotoxin is one of the bungarotoxins, components of the venom of the elapid Taiwanese banded krait snake. It is a type of α-neurotoxin, a neurotoxic protein that is known to bind competitively and in a relatively irreversible manner to the nicotinic acetylcholine receptor found at the neuromuscular junction, causing paralysis, respiratory failure, and death in the victim. It has also been shown to play an antagonistic role in the binding of the α7 nicotinic acetylcholine receptor in the brain, and as such has numerous applications in neuroscience research.
Soy protein is a protein that is isolated from soybean. It is made from soybean meal that has been dehulled and defatted. Dehulled and defatted soybeans are processed into three kinds of high protein commercial products: soy flour, concentrates, and isolates. Soy protein isolate has been used since 1959 in foods for its functional properties.
The granulocyte-macrophage colony-stimulating factor receptor, also known as CD116, is a receptor for granulocyte-macrophage colony-stimulating factor, which stimulates the production of white blood cells. In contrast to M-CSF and G-CSF which are lineage specific, GM-CSF and its receptor play a role in earlier stages of development. The receptor is primarily located on neutrophils, eosinophils and monocytes/macrophages, it is also on CD34+ progenitor cells (myeloblasts) and precursors for erythroid and megakaryocytic lineages, but only in the beginning of their development.
Fatty-acyl-CoA synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.
The cupin superfamily is a diverse superfamily of proteins named after its conserved barrel domain. The superfamily includes a wide variety of enzymes as well as non-enzymatic seed storage proteins.
Pea protein is a food product and protein supplement derived and extracted from yellow and green split peas, Pisum sativum. It can be used as a dietary supplement to increase an individual's protein or other nutrient intake, or as a substitute for other food products. As a powder, it is used as an ingredient in food manufacturing, such as a thickener, foaming agent, or an emulsifier.
Canavalin is a plant protein found in the jack bean, sword bean, and related plants. It is the major storage protein found in these plants' seeds, and is one of four proteins readily isolated from the seeds; the others are concanavalin A, concanavalin B, and urease. Canavalin is a vicilin protein homologous to phaseolin.
Vicilin is a legumin-associated globulin protein. It is a storage protein found in legumes such as the pea or lentil that protects plants from fungi and microorganism. It is believed to be an allergen in pea and peanut allergy responses.
11S globulin family is a family of globulin proteins chiefly found in seeds of legumes (legumin-like), along with 7S family, often found in a protein fraction within a protein isolate. They are used as storage of important nutrients for plant growth, and therefore hardy enough to pass through the human digestive system unscathed. One common example of an 11S globulin includes glycinin derived from soy.
Cruciferin is one of the two most abundant seed storage proteins in mustard and rapeseed. They are classified as 11S globulins based on their sedimentation coefficient, and are salt soluble neutral glycoproteins. Their molecular weights range from 20 to 40 kDa. They comprise up to 50–70% of the total seed protein. Cruciferin is a comparatively larger seed storage protein than napin. It is composed of two polypeptide chains α and β. The α-chain has a mass of 30 kDa and the β-chain weighs in at 20 kDa. They are held together by a disulphide bond.
