Two alcohol soluble glutenins (ASGLUs) were extracted from gluten and further separated by column chromatography. The ASGLUs with Mw lower than 20,000 (ASGLU 1) and Mw higher than 70,000 (ASGLU 2) show the total amino acid contents of 86.71 g/100 g and 62.847 g/100 g respectively. Both of them are rich in Glu (45.574% and 43.224%) and Pro (15.447% and 16.370%) while poor in cys-s, met and lys (less than 1%). When wheat amylopectin/amylose retrogrades with those ASGLUs, the retrogradation rate of amylopectin with ASGLU 1 enhances significantly. UV-Vis, X-ray diffraction, FT-IR, DSC, CD and solid 13C NMR suggest that the double helixes of amylopectin short-chain branching are unwound during gelatinization. The hydrogen bonds of ASGLU 1 between amide and carbonyl oxygen are destroyed, meanwhile, β-sheets are unfolded. During retrogradation, ASGLU 1 with less steric hindrance gets into the crevice of amylopectin and combines with the short-chain branching by hydrogen bond. The retrogradation dynamics show that the nucleation type of amylopectin-ASGLU 1 changes from instantaneous to rod-like growth during the process of retrogradation. β-sheet of ASGLU 1 changes to β-turn and random conformations at the meantime. The results provide a key targeting to control retrogradation of dough.
Keywords: Alcohol soluble glutenins; Mechanism; Promoting retrogradation; Solid (13)C NMR; Wheat amylopectin.
Copyright © 2021 Elsevier B.V. All rights reserved.