glycinin

gly·cin·in

(glī-sin'in),
The chief protein of soybeans; a globulin that is structurally similar to arachin, edestin, and excelsin.
References in periodicals archive ?
The contents of glycinin and [beta]-conglycinin were analyzed by a competitive ELISA developed in our laboratory (You et al.
Wanger and Guegeon [28] attributed the higher ES of soy protein at low ionic strength to the dissociation of oligomeric structure of HS glycinin and subsequent improvement of the surface properties.
1999) considered a soybean glycinin expressed in genetically engineered rice to be labile in SGF when the protein was digested within 30 min.
Wolf is tackling the problem by attaching monosaccharides--such as glucose--to glycinin, the major storage protein of soy.
However, the presence of antigenic proteins such as glycinin, [beta]-conglycinin and anti-nutritional factors such as TI and lectins in soybean could cause hypersensitivity for newly weaned piglets which may decrease nutrient availability and therefore restrict its' inclusion in diets fed to weaning pigs (Li et al.
d]) of soybean glycinin is 92[degrees]C [16]; this temperature is higher than the thermal denaturation temperature of most pure protein isolates, but lower than that of broad bean 11S protein, the 11S protein of sunflower and oat globulin [16].
A reduced growth performance in pigs fed soybean proteins has been associated with reduced weight gain and protein digestibility, which may be caused by a hypersensitivity to soybean proteins, glycinin, and [beta]-conglycinin.
Problematic proteins include glycinin (about 40% of the total soybean globulin proteins), [beta]-conglycinin (about 30%), and other minor proteins (Brandom and Friedman, 2002; Sun et al.
Glycinin and beta-conglycinin are the main antigen proteins in soybean meals, which can cause a transient increase in crypt cell production, and subsequent malabsorption and villus atrophy in weaned piglets (Stokes et al.
Simultaneously glycinin and [beta]-conglycinin, the two most important storage proteins in soy, are denatured and eliminated their antigenic properties.
This fermentation process by Aspergillus oryzae and Bacillus subtilis reduced trypsin inhibitor below a detection limit, reduced phytate content by 4-folds, reduced size of peptides for suitable for digestion, and reduced contents of glycinin and pconglycinin that are known as allergenic compounds in gut (Figure 10; Hong et al.
Others have shown that soya-derived saponins increased the uptake of exogenous proteins, such as glycinin, by rabbit intestine cultured in vitro, and that lectin and saponins together stimulated this uptake to a greater degree than the sum of their individual effects (Alvarez and Torres-pinedo, 1982; Johnson et al.