Role of N-terminal domain of HMW 1Dx5 in the functional and structural properties of wheat dough

Abstract

Effects of N-terminal domain of high molecular weight glutenin subunit (HMW-GS) 1Dx5 (1Dx5-N) on functional and structural properties of wheat dough were determined by farinographic and rheological analysis, size exclusion chromatography, non-reducing/reducing SDS-PAGE, total free sulfhydryl determination, scanning electron microscopy and Fourier transform infrared spectroscopy. Results showed that 1Dx5-N improved the quality of dough with the increased water absorption, dough stability time, elastic and viscous modulus, and the decreased degree of softening, loss tangent. These improvements could be attributed to the formation of the macro-molecular weight aggregates and massive protein networks, which were favored by 1Dx5-N through disulfide bonds and hydrophobic interactions. Additionally, 1Dx5-N drove the transition of α-helix and random coil conformations to β-sheet and β-turn conformations, further demonstrating the formation of HMW-GS polymers and the enhancement of dough strength. Moreover, all the positive effects of 1Dx5-N were reinforced by edible salt NaCl.

Keywords: 1Dx5; 2-Mercaptoethanol (PubChem CID: 1567); Acrylamide (PubChem CID: 6579); Dough development; High molecular weight glutenin subunits (HMW-GS); Hydrochloric acid (PubChem CID: 313); N-terminal domain; Sodium chloride (PubChem CID: 5234); Sodium dodecyl sulfonate (PubChem CID: 3423265); Structural and functional properties; Tris (PubChem CID: 6503).