Changes in wheat kernel proteins induced by microwave treatment

The Impact of Gluten Friendly Flour on the Functionality of an Active Drink: Viability of Lactobacillus acidophilus in a Fermented Milk

“…As supposed elsewhere (Bevilacqua et al, 2016b; Lamacchia et al, 2016), the alternation of high temperatures to evaporation phases induces different spatial conformation of the amino acid sequences in hydrated wheat caryopses treated with the Gluten Friendly TM technology, inducing a rearrangement of the secondary and tertiary structure of the gluten proteins.…”

“…Due to some structural modifications to endosperm components, the immunogenicity of the most common epitopes involved in celiac disease was reduced in vitro (Lamacchia et al, 2016), but the nutritional and technological properties necessary to process flour into bread, pasta, and other baked goods remain unchanged. Additional researches (Bevilacqua et al, 2016b) found that bread produced with Gluten Friendly Flour (GFF) was able to modify the qualitative-quantitative composition of gut microbiota (bifidogenic effect and on the growth of lactobacilli in the gut microbiota in a complex system).…”

Wheat Seed Proteins: Factors Influencing Their Content, Composition, and Technological Properties, and Strategies to Reduce Adverse Reactions

“…Recently, Lamacchia and coworkers proposed the use of microwaves to remove antigenic properties of wheat gluten proteins and named the procedure "Gluten Friendly" (Landriscina et al, 2017). The authors claimed the method reduces antigenicity by 99% (Lamacchia, Landriscina, & D'Agnello, 2016), largely based on R5 ELISA assays. However, Gianfrani and coworkers rejected the original claims based on G12 antibody-based ELISA, mass spectrometry-based proteomics, and in vitro assay with T cells (Gianfrani et al, 2017).…”

Microwave fixation enhances gluten fibril formation in wheat endosperm

“…These properties are mainly attributed to the inherent viscoelastic nature of doughs caused by the hydration of seed storage proteins called prolamins (Payne, 1987). During heating, it has been shown that wheat gluten in gels undergoes unfolding to produce cross-linking reactions (Wang et al, 2017) and that microwave treatment of the gluten proteins induces a reduction in hydrogen bond content thus leading to structural changes from the protein's native form (Lamacchia, Landriscina, & D'Agnello, 2016). Gliadins are soluble in aqueous alcohols and contribute to the extensibility of a dough, whereas glutenins are insoluble in aqueous alcohols and mainly confer a doughs elasticity; together they form gluten (Shewry, Halford, Belton, & Tatham, 2002;Shewry, Tatham, Forde, During grain development, these proteins are deposited and accumulate in the endosperm to form a proteinaceous matrix.…”

“…Although the exact changes that occur during mixing are not completely understood, it is generally accepted that there is an exchange of disulfide bonds and protein-protein interactions within the dough to form a gluten network. During heating, it has been shown that wheat gluten in gels undergoes unfolding to produce cross-linking reactions (Wang et al, 2017) and that microwave treatment of the gluten proteins induces a reduction in hydrogen bond content thus leading to structural changes from the protein's native form (Lamacchia, Landriscina, & D'Agnello, 2016). Granting that knowledge about gluten protein chemistry, rheology, and molecular characterization has expanded tremendously in recent years, and there remains a lack of knowledge surrounding the physical and microstructural properties of the three-dimensional network that forms gluten.…”