Processing conditions and transglutaminase sources to “drive” the wheat gluten dough quality

https://doi.org/10.1016/j.ifset.2020.102439Get rights and content
Under a Creative Commons license
open access

Highlights

  • Processing conditions impact gluten proteins interaction and end-use quality.

  • TGs impact is maximized in wheat-dough, but minimized in protein-rich systems.

  • Industrial harsh treatment, molding and screw-mixing reduce protein solubility.

  • More polymerization opportunities are created in mild than in harsh gluten.

Abstract

Gluten proteins are highly impacting the quality of various gluten-based products, and transglutaminases (TGs) are used to influence the protein cross-linking. In this study we monitored the interplay of “harsh” and “mild” gluten processing for dough mixing and pasta-like sheet production and TGs from a commercial and newly sourced bacteria (SB6). Despite the harshly separated gluten presenting strongly cross-linked proteins in the beginning of the mixing, similar levels of polymerization were achieved at the optimum mixing time but with differences in the secondary protein structure. TG addition increased polymerization in wheat doughs, possibly as a result of increased glutenin polymerization, while gliadins become more soluble with SB6. This enzyme also dramatically increased polymerization in mild gluten. These results show that an adequate investigation when using TGs and gluten from various origins is necessary to adequately predict the quality in various gluten-based products, thus, of great relevance to the food industry.

Industrial relevance

Currently, there is a mounting trend towards the modification of gluten proteins to improve technological features and functionality. In breadmaking, when weak flour (low protein content) is used or general stabilization is desired for technological purposes, additives can be used to stabilize the gluten protein matrix. The use of transglutaminase (TG) has grown in popularity as they promote specific cross-linking between residues of glutamine and lysine in proteins. Another way of improving dough functionality is by increasing the oxidation of disulfide groups by adding gluten which is a co-product of the starch industry. Industrial production of gluten includes the use of heating and shear forces, which may impact gluten dough-forming ability. Thus, increased understanding of the interplay of gluten processing and the impact of choice of the TG origin in gluten dough quality is highly applicable in food industry.

Keywords

Gluten separation
Transglutaminase
Polymerization
Protein-rich
Dough
Film
Crosslinking

Cited by (0)