Enhancement of crispiness in mahua through the incorporation of salt-modified wheat amylose.

Crispness is an important feature of high-quality Mahua. The results of this study demonstrate that crispness of Mahua could be enhanced by incorporating salt-modified wheat amylose in this study. The results showed that the crispness of Mahua increased from 40.63 to 20.60 g as 10% salt-modified wheat amylose (where the ratio of 50% wheat amylose and 20% NaCl solutions is 1:5, and the salt-modified time was 36 h at 4 °C) was added, and the dough was mixed at 45 °C for 12 min. It was hypothesized that the possible mechanism might involve the bound water within the intermolecular β-sheets structure of glutenin in a closed-loop system. This system was formed by the interaction of salt-modified wheat amylose with a chain length of 12-13 glucose units in a double-helical conformation. In this system, the OH-C6 of wheat amylose in double helix might react with the hydroxyl group of threonine (Thr) in the α-helical structure of glutenin to form a covalent bond, thereby stabilizing the conformation. Additionally, hydrogen bonds might form between OH-C2, C3, and C5 of wheat amylose and Gln /Pro residues located in the β-corn of glutenin. Intramolecular disulfide bonds might contribute to the stabilization of the β-sheet conformation. In the intermolecular β-sheet arrangement, hydrogen bonds might form between Gln residues and water molecules, which became entrapped within the cyclic structure formed by starch and protein matrices to hinder the evaporation of water.