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. 2015 Dec 22;5:18041. doi: 10.1038/srep18041

Figure 4. Structural changes in gluten proteins by transamidation of wheat flour and gluten under reducing conditions.

Figure 4

(a) Reduced and alkylated glutenin subunit electrophoretic patterns of wheat flour and gluten (as denoted), original and derivatised with mTG alone and with n-butylamine as amine nucleophile with increasing concentrations under reducing conditions. (b) Gliadin electrophoretic patterns of wheat flour and gluten (as denoted), original and derivatised with mTG alone and with n-butylamine as amine nucleophile with increasing concentrations under reducing conditions. Reversed-phase HPLC results for gliadins (c,d) and glutenins (e,f) extracts of wheat flour and gluten, original and derivatised with mTG alone and with n-butylamine as amine nucleophile under reducing conditions. Wheat flour chromatograms are represented for a maximum absorbance of 1.0 and gluten chromatograms are represented for a maximum absorbance of 2.5. ω5, ω1, 2, α/β and γ represent the different identified gliadin proteins, and HMW and LMW represent the different glutenin subunits. Absorbance was registered at 210 nm. For sample nomenclature please consult Fig. 6.