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This simple fractionation strategy results in less complex samples, leads to improved identification of low-abundance proteins, and a better overall view of the proteome.
Proteins like albumin, globulin, gliadin, amylase, and glutenin are important components of wheat. Albumin and globulin, two major water-soluble proteins, are responsible for several aspects of wheat grain quality.
The protein fraction with the lowest PSI was soluble glutenin, in all the analyzed genotypes (Table 2). The content of soluble glutenins ranged from 9.49% to 14.91% of total proteins and from 7.24% to 11.69% of total proteins in wholemeal of bread and durum wheat genotypes, respectively.
Wheat gluten mainly consists of two water-insoluble proteins present in flour, gliadin and glutenin, and is a substance with gum-like, specific viscoelasticity, separated by washing dough with water.
Fractionation reduces the complexity of a protein sample by separating proteins in different classes based on biophysical properties of the proteins (size, charge, cellular location, solubility etc.).

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Currently, about 95% of the wheat grown worldwide is hexaploid bread wheat, with most of the remaining 5% being tetraploid durum wheat. The ability of wheat flour to be processed into different foods is largely determined by the proteins. Mature wheat grains contain 8% to 20% proteins.
Gluten proteins can be divided into two main fractions ing to their solubility in aqueous alcohols: the soluble gliadins and the insoluble glutenins. Both fractions consist of numerous, partially closely related protein components characterized by high glutamine and proline contents.
Wheat grain proteins have traditionally been classified into four so-called Osborne fractions, ing to their solubility in water (albumins), salt solutions (globulins), aqueous alcohols (gliadins), or dilute acid or alkaline solutions (glutenins) [7].

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