Study of the fractional composition of wheat proteins and macaroni products during storage

The results of the molecular weight distribution of wheat proteins and macaroni products are presented. The fractional composition of proteins was determined by gel permeation chromatography on a Knauer Smartline chromatograph; preliminary hydrolysis was carried out using a thermostable bacterium α-Amylase, then it was centrifuged, filtered through a Teflon filter, and the size of protein molecules was determined by photometric detection at a wavelength of 280 nm. It has been shown that the main protein fraction in both wheat and macaroni products is a low molecular weight fraction up to 3 kD (up to 79.4% of all protein fractions). The fraction with low and medium molecular weight from 3 to 10 kD accounted for 2.7 to 48.2%, while the fraction with a molecular weight of more than 10 kD accounted for up to 15.2%. During storage, a redistribution of protein fractions and their enlargement were noted. English version of the article is available at URL: https://panor.ru/articles/study-of-the-fractional-composition-of-wheat-proteins-and-pasta-products-during-storage/74321.html

Pro-Inflammatory Effect of Gliadins and Glutenins Extracted from Different Wheat Cultivars on an In Vitro 3D Intestinal Epithelium Model

There is a need to assess the relationship between improved rheological properties and the immunogenic potential of wheat proteins. The present study aimed to investigate the in vitro effects of total protein extracts from three modern and two landrace Triticum aestivum commercial flour mixes, with significant differences in gluten strength (GS), on cell lines. Cytotoxicity and innate immune responses induced by wheat proteins were investigated using Caco-2 monocultures, two dimensional (2D) Caco-2/U937 co-cultures, and three dimensional (3D) co-cultures simulating the intestinal mucosa with Caco-2 epithelial cells situated above an extra-cellular matrix containing U937 monocytes and L929 fibroblasts. Modern wheat proteins, with increased GS, significantly reduced Caco-2 cell proliferation and vitality in monoculture and 2D co-cultures than landrace proteins. Modern wheat proteins also augmented Caco-2 monolayer disruption and tight junction protein, occludin, redistribution in 3D co-cultures. Release of interleukin-8 into the cell medium and increased U937 monocyte migration in both 2D and 3D co-cultures were similarly apparent. Immuno-activation of migrating U937 cells was evidenced from cluster of differentiation 14 (CD14) staining and CD11b-related differentiation into macrophages. The modern wheat proteins, with gluten polymorphism relatedness and increased GS, were shown to be more cytotoxic and immunogenic than the landrace wheat proteins.

Comparative Characterization of Gluten and Hydrolyzed Wheat Proteins

Hydrolyzed wheat proteins (HWPs) are widely used as functional ingredients in foods and cosmetics, because of their emulsifying and foaming properties. However, in individuals suffering from celiac disease or wheat allergy, HWPs may have a modified immunoreactivity compared to native gluten due to changes in molecular structures. Although a variety of HWPs are commercially available, there are no in-depth comparative studies that characterize the relative molecular mass (Mr) distribution, solubility, and hydrophilicity/hydrophobicity of HWPs compared to native gluten. Therefore, we aimed to fill this gap by studying the above characteristics of different commercial HWP and gluten samples. Up to 100% of the peptides/proteins in the HWP were soluble in aqueous solution, compared to about 3% in native gluten. Analysis of the Mr distribution indicated that HWPs contained high percentages of low-molecular-weight peptides/proteins and also deamidated glutamine residues. We also found considerable differences between the seven HWPs studied, so that each HWP needs to be studied in detail to help explain its potential immunoreactivity.