Composition, physicochemical properties of pea protein and its application in functional foods

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...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:Critical reviews in food science and nutrition Ročník 60; číslo 15; s. 2593 - 2605
Hlavní autoři: Lu, Z. X., He, J. F., Zhang, Y. C., Bing, D. J.
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Taylor & Francis 21.08.2020
Taylor & Francis Ltd
Témata:
ISSN:1040-8398, 1549-7852, 1549-7852
On-line přístup:Získat plný text
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
Popis
Shrnutí: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.
Bibliografie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
ObjectType-Review-3
content type line 23
ISSN:1040-8398
1549-7852
1549-7852
DOI:10.1080/10408398.2019.1651248