Physicochemical alterations of wheat gluten proteins upon dough formation and frozen storage – A review from gluten, glutenin and gliadin perspectives

• Published in: Trends in food science & technology Vol. 46; no. 2; pp. 189 - 198
• Main Authors: Wang, Pei, Jin, Zhengyu, Xu, Xueming
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.12.2015
• Subjects: baked goods; bakery industry; Dough formation; dough quality; freezing; frozen dough; Frozen storage; gliadin; Gluten proteins; glutenins; grain foods; manufacturing; mixing; Physicochemical alterations; shelf life; storage time; wheat gluten; Dough formation; tanδ; G; R/E; Mw; Physicochemical alterations; DSC; SH; FTIR; η0; CLSM; Tp; GSH; AA; SS; CD; Frozen storage; SDS; Gluten proteins; GMP; SEC-MALLS; HMS; N- and C-TD; RP-HPLC; TD; SDS-PAGE; LMS; ΔH; SEM; TD-NMR; TEM
• ISSN: 0924-2244; 1879-3053
• DOI: 10.1016/j.tifs.2015.10.005

Gluten proteins are considered as quality determinants in cereal-based food product by forming the backbone structure of dough. Freezing technique has largely expanded the dough shelf life and brought revolutionary development to the bakery industry. However, deterioration of gluten network in frozen dough is one of the major factors leading to the quality loss of bakery products. During the manufacturing process of frozen dough, hydration with optimum mixing is the first and critical step to manage the control dough quality, followed by the freezing and frozen storage to achieve the long time storage of dough, which determines the final dough quality. Series of physicochemical alterations in gluten proteins occur upon the dough formation and frozen storage. Understanding these fundamental changes is important for the research community to propose more rational implementation of specific improvement principals for frozen dough. In this review, the physicochemical alterations of wheat gluten proteins are investigated from the perspectives of gluten and its component glutenin and gliadin. A more structure-ordered, homogeneous and elastic gluten network is formed at the optimum mixing stage as a consequence of glutenin and gliadin interactions. Comparative studies in different model systems demonstrate that further frozen storage exerts detrimental effects on gluten proteins in diverse ways from both gluten proteins-water interactions and structure-functionality perspectives. •Overview of physicochemical changes in gluten proteins during dough formation.•Gluten proteins in different regimes upon frozen storage were reviewed.•Alteration in gluten was interpreted from perspectives of glutenin and gliadin.