Composition and characterization of soyabean and related products

Abstract

Soyabean contains about 48 to 50% proteins. Among these, storage proteins are predominant. 7S and 11S globulins are two storage proteins that constitute 80% of the total protein content in soyabean. Moreover, there are other less abundant storage proteins such as 2S, 9S, and 15S globulins. In addition to globulins, enzymes, protease inhibitors (Kunitz and Bowman-Birk), lectin, and other complete the soya protein content. Different methods exist to characterize soya proteins. These methods involve (1) an isolation of proteins from soya commercial products and (2) the use of analytical techniques for protein determination. Soya proteins may interact with other soya components such as minerals, phytic acid, ascorbic acid, and fiber. These interactions, which depend on soya processing and treatment, can decrease the bioavailability of minerals and proteins. Swelling, solubility, viscosity, and capacity to form a gel, an emulsion, or a foam are the main functional properties of soyabean. They are responsible for the wide use of soya in industrial processes.

Soy, phytoestrogens and their impact on reproductive health

“…Soybean (Glycine max) is composed of macronutriments such as proteins, carbohydrates and lipids. Protein content varies between 36% and 46% depending on the variety (Garcia et al, 1997;Grieshop and Fahey, 2001;Grieshop et al, 2003). The major portion of the protein component is formed by storage proteins such as 7S globulin (b-conglycinin) and 11S globulin (glycinin), which represent about 80% of the total protein content (Garcia et al, 1997).…”

Wood production, wood technology, and biotechnological impacts

“…Increase in both adhesive strength and hydrophobicity of soybean protein were also reported upon moderate esterification of free carboxyl groups of the proteins with ethanol and upon urea treatment (Sun & Bian 1999, Huang & Sun 2000a. Two of the five major soybean proteins [conglycinin (7S) and glycinin (11S) making up about 80% of the soybean storage protein; Garcia et al 1997] were shown to provide a better adhesion when treated with urea. Very interestingly, the two storage proteins differed in adhesion performance with the types of wood tested: urea-modification increased adhesion of conglycinin on cherry and walnut whilst glycinin by urea-modification obtained a better adhesion on pine (Zhang & Hua 2007).…”

Development of a capillary electrophoresis method for the determination of soybean proteins in soybean–rice gluten‐free dietary products

“…Soybean protein amino acid profile (rich in lysine, limited in sulfur amino acids) fits nicely with grain proteins (limited in lysine, rich in sulfur amino acids) resulting in a product with a higher nutritional quality than the individual components [12]. There are three kinds of proteins in soybean: (i) proteins involved in metabolism, (ii) structural proteins, and (iii) storage proteins or globulins.…”

“…This last group of proteins is present in soybean at a higher concentration. Unlike prolamins and glutelins (main proteins in cereals), globulins are sparingly soluble in water and soluble in salt solutions [12][13][14].…”