Mechanisms of Heat-Mediated Aggregation of Wheat Gluten Protein upon Pasta Processing

Abstract

During pasta processing, structural changes of protein occur, due to changes in water content, mechanical energy input, and high temperature treatments. The present paper investigates the impact of successive and intense thermal treatments (high temperature drying, cooking, and overcooking) on aggregation of gluten protein in pasta. Protein aggregation was evaluated by the measurement of sensitivity of disulfide bonds toward reduction with dithioerythritol (DTE), at different reactions times. In addition to the loss in protein extractability in sodium dodecyl sulfate buffer, heat treatments induced a drastic change in disulfide bonds sensitivity toward DTE reduction and in size-exclusion high-performance liquid chromatography profiles of fully reduced protein. The protein solubility loss was assumed to derive from the increasing connectivity of protein upon heat treatments. The increasing degree of protein upon aggregation would be due to the formation of additional interchain disulfide bonds.

Impact of mixing time and sodium stearoyl lactylate on gluten polymerization during baking of wheat flour dough

“…This can probably be related to an altered availability (due to conformational changes) of the SH groups. It may well be that (the extent and/or way of) glutenin cross-linking is affected as well, but that, due to the applied method, this was not observed, since measuring SDSEP levels gives valuable information about the extent of protein polymerization, but not on the unextractable protein structure formed by glutenin and gliadin (Wagner et al, 2011).…”

“…For bread, gluten protein polymerization in the baking phase contributes to its final structure and quality (Lagrain, Thewissen, Brijs, & Delcour, 2007), whereas, in cookies, such thermoset network determines cookie spread, the internal structure as well as the break strength (Pareyt, Van Steertegem, Brijs, Lagrain, & Delcour, 2010b). Also, during pasta making, gluten polymerization creates a three-dimensional interconnected structure (Wagner, Morel, Bonicel, & Cuq, 2011), of which the degree of protein polymerization during drying and/ or subsequent cooking determines pasta quality in terms of firmness and cooking losses . However, the relevance of structure formation of the transient network during dough mixing, and the influence of the latter on the formation and the final permanent gluten network structure in baked products has, to the best of our knowledge, never been investigated.…”

Labeling Regulations, Detection Methods, and Assay Validation

“…Law No. 26.588, which declares of national interest the clinical care, clinical and epidemiological research, and professional training in early detection, diagnosis, and treatment of CD, has been recently regulated by decree 528/2011.…”

The role of gluten proteins in production and quality of a yeast leavened sugar and fat rich wheat based food model system – 2. Impact of redox agents

“…The decreased level of SDSEP between 30 sec and 1 min of baking (Figure 1) indicated the occurrence of protein polymerization despite the high levels of sugar and fat. Unfortunately, while SDSEP levelsgive valuable information about the extent of protein polymerization, they provide neither the numbers of bonds formed nor the structure of the unextractable protein formed by glutenin and gliadin(Wagner, Morel, Bonicel, & Cuq, 2011…”