Abstract
Vital gluten is a by-product of wheat starch production and commonly used in bread making, but its quality is difficult to predict. The most accurate method to determine vital gluten quality is the baking experiment, but this approach is time- and labor-intensive. Therefore, the aim was to identify faster and easier ways to predict vital gluten quality. Three different approaches, the gliadin/glutenin ratio, the gluten aggregation test and the microscale extension test, were assessed for their predictive value regarding the baking performance of 46 vital gluten samples using two recipes. Hierarchical clustering classified the vital gluten samples into 23 samples with good, 15 with medium and eight with poor quality. Protein-related parameters, such as the gliadin/glutenin ratio, were not reliable to predict gluten quality, because the correlations to the bread volumes were weak. The gluten aggregation test and the microscale extension test were reliable methods to predict vital gluten quality for use in baking based on a scoring system. Both methods need less material, time and labor compared to baking experiments. Especially, maximum torque, peak maximum time, the ratio between peak30 and peak180 as well as the corresponding distance at maximum resistance to extension seem to be suitable alternatives to predict vital gluten quality.
Highlights
Wheat gluten contains storage proteins, which are a complex mixture of more than one hundred single proteins, composed of alcohol-soluble gliadins (GLIA) and alcohol-insoluble glutenins (GLUT) (Shewry, 2019)
As baking experiments are the “golden standard” for evaluating the quality of vital gluten (Gabriel et al, 2017), the vital gluten samples G1-G46 were classified based on the specific volumes of two microbaking tests using baking mixture A and B (Table 1)
The breads made from baking mixture B generally resulted in lower specific volumes from 1.1 ml/g (G40) to 3.0 ml/g (G26) and we assume that the lower specific volumes were caused by the higher water addition
Summary
Wheat gluten contains storage proteins, which are a complex mixture of more than one hundred single proteins, composed of alcohol-soluble gliadins (GLIA) and alcohol-insoluble glutenins (GLUT) (Shewry, 2019). Gluten is typically separated from wheat flour by washing out starch and water-soluble components (Bailey, 1941). This simple experiment represents the beginning of gluten extraction and is still the basis of modern day processes like the Martin process, the batter process or variations thereof (Van der Borght, Goesaert, Veraverbeke and Delcour, 2005). Vital gluten regains its intrinsic functionality and forms a hydrated gluten network This network has the ability to retain the gas produced during dough fermentation and it stabilizes the sponge-like structure of wheat bread crumb (Neumann, Kniel and Wassermann, 1997; Ortolan, Corr^ea, da Cunha and Steel, 2017).
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call