Effect of high-molecular-weight glutenin subunit deletion on gluten functionality and Chinese southern-type steamed bread quality.

High-molecular-weight glutenin subunit (HMW-GS) is key factor in gluten strength and end-use quality. However, the contribution of individual HMW-GS on dough strength and Chinese southern-type steamed bread (CSTSB) quality remained unknown. In this study, we investigated the effects of individual HMW-GS deletion on CSTSB quality. The HMW-GS deletion led to significant reductions in glutenin/gliadin ratios, disulfide bond content, and SDS-unextractable polymeric protein formation. Additionally, HMW-GS deletion resulted in decreased gluten protein chain length, molecular weight, and particle size, contributing to increased thermal instability and reduced crosslinking. The HMW-GS deletion weakened dough strength but improved CSTSB performance, particularly in Dx2d and Dy12d. In-silico analysis further revealed strong interactions between Bx7 and Dx2, primarily driven by desolvation energy, highlighting their crucial role in stabilizing gluten protein interactions.