New Insights into the Potential of Endogenous Redox Systems in Wheat Bread Dough.

Nicolas Navrot,Birte Svensson,Rikke Buhl Holstborg,Inge Povlsen,Per Hägglund

doi:10.3390/antiox7120190

Abstract

Various redox compounds are known to influence the structure of the gluten network in bread dough, and hence its strength. The cereal thioredoxin system (NTS), composed of nicotinamide adenine dinucleotide phosphate (NADPH)-dependent thioredoxin reductase (NTR) and thioredoxin (Trx), is a major reducing enzymatic system that is involved in seed formation and germination. NTS is a particularly interesting tool for food processing due to its heat stability and its broad range of protein substrates. We show here that barley NTS is capable of remodeling the gluten network and weakening bread dough. Furthermore, functional wheat Trx that is present in the dough can be recruited by the addition of recombinant barley NTR, resulting in dough weakening. These results confirm the potential of NTS, especially NTR, as a useful tool in baking for weakening strong doughs, or in flat product baking.

Highlights

Bread is a basic element of the daily diet all over the world, and standard production procedures are important for achieving reproducible quality in various production sites
Soluble dough extracts were used to estimate the contents of soluble free thiols in the dough, which likely increased when NTS was added. This softening both of dough with and without yeast showed that added NADPH-dependent thioredoxin reductase (NTR) and Trx activity were not lost due to elevated yeast metabolism in the developing dough
It is suggested that the optimization of the wheat Trx

Summary

Introduction

Bread is a basic element of the daily diet all over the world, and standard production procedures are important for achieving reproducible quality in various production sites. Nicotinamide adenine dinucleotide phosphate (NADPH)-dependent thioredoxin reductase and thioredoxin (Trx) constitute a versatile multi-enzymatic NTS that has been extensively studied in (NTR) and thioredoxin (Trx) constitute a versatile multi-enzymatic NTS that has been extensively plants. NTS functions by transferring reducing power from NADPH to various target proteins studied in plants. NTS functions by transferring reducing power from NADPH to various target via a Trx-mediated disulfide bridge reduction [10] (Figure 1B). Plant genomes typically contain proteins via a Trx-mediated disulfide bridge reduction [10] (Figure 1B). Plant Trx are highly expressed in seeds, and these very stable proteins likely remain functional raw dough. Agent to modify dough properties, if supplemented with reducing equivalents provided by NADPH We examined these hypotheses here in an experimental dough- and bread-making system.

Materials and Methods

Effect of NTS on Dough Rheological Properties

Mini Breads and Buns

Protein Extraction and Dough Thiol Content

Conclusions