Name | Gliadin from wheat |
Synonyms | GLIADIN GLIADINE gliadins WHEATGLIADIN gliadin crude Gliadin from wheat WHEAT-GAMMA-GLIADIN GLIADIN FROM WHEAT, POWDER |
CAS | 9007-90-3 |
EINECS | 232-707-7 |
Molecular Formula | C29H41N7O9 |
Molar Mass | 631.67734 |
Appearance | Morphological powder |
Merck | 4437 |
Storage Condition | 2-8℃ |
MDL | MFCD00131160 |
Safety Description | S22 - Do not breathe dust. S24/25 - Avoid contact with skin and eyes. |
WGK Germany | 3 |
FLUKA BRAND F CODES | 21 |
Reference Show more | 1. Wang Shukai, Li Fuguo. Effect of interaction between wheat protein and anthocyanin on its stability [J]. Science and technology of light industry, 2020(7):26-29. 2. [IF = 5.279] Yu Wang et al."l-Arabinose diet Gliadin-Induced Food Allergy via Regulation of Th1/Th2 Balance and ultra Regulation of Regulatory T Cells in Mice." J Agr Food Chem. 2021;69(12):3638-3646 3. [IF = 4.952] Feng Xue et al."Prevention of frozen-dough from deterioration with incorporation of glutenin-polyphenols conjugates prepared by ultrasound."Lwt Food Sci Technol. 2021 Nov;151:112141 4. [IF=3.196] Kangyi Zhang et al."Comparison of interaction mechanism between chlorogenic acid/luteolin and glutenin/gliadin by multi-spectroscopic and thermodynamic methods."J Mol Struct. 2021 Dec;1246:131219 5. [IF=6.953] Jiwei Kuang et al.Control of wheat starch rheological properties and gel structure through modulating granule structure change by reconstituted gluten fractions.Int J Biol Macromol. 2021 Nov;: 6. [IF=9.147] Jiwei Kuang et al."Influence of reconstituted gluten fractions on the short-term and long-term retrogradation of wheat starch."Food Hydrocolloid. 2022 Sep;130:107716 |
EPA chemical information | Gliadins (9007-90-3) |
A group of protein mixtures found in cereals (such as wheat, rye, etc.) seeds. It is divided into two major groups (α/β and & gamma;), which are similar in composition and nature. Rich in proline, stores most of the protein in wheat seeds. When water is present, it sticks together and makes the flour stick to form a dough. Gliadin is a monomeric protein, spherical, compared with glutenin, the surface area is smaller, the intermolecular effect is weaker, which plays a decisive role in the viscosity and ductility of the dough. Due to the reduction of gliadin disulfide bonds and the reduction of the internal structural strength of the gliadin molecule during the freezing process, the ductility of the dough will inevitably decrease; and the β-corner has an important effect on the viscosity of the protein. The reduction of β-corner in the infrared map of gliadin will lead to a decrease in the viscosity of the dough.