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The enzymatic modification of wheat proteins during dough fermentation and its digestion as supported by peptidases of microbiological origin can result in the degradation of important peptides in the pathogenesis of coeliac disease. However, baking bread and the high temperature associated with this could change the physicochemical and immunological properties of proteins. Thermal changes in the spatial structure of proteins and their hydrolysis can lead to a masking or degrading of immunoreactive peptides.; Results: The addition of prolyl endopeptidase (PEP), comprising peptidases isolated from Lactobacillus acidophilus 5e2 (LA) or transglutaminase (TG) in the course of fermentation, decreases its immunoreactivity by 83.9%, 51.9% and 18.5%, respectively. An analysis of the fractional composition of gliadins revealed that γ- and ω-gliadins are the proteins most susceptible to enzymatic modification. Hydrolysis of wheat storage proteins with PEP and LA reduces the content of αβ-, γ- and ω-gliadins by 13.7%, 60.2% and 41.9% for PEP and by 22.1%, 43.5% and 36.9% for LA, respectively. Cross-linking of proteins with TG or their hydrolysis by PEP and LA peptidases during the process of forming wheat dough, followed by digesting bread samples with PEP and LA peptidases, decreases the immunoreactivity of bread hydrolysates from 2.4% to 0.02%. The content of peptide detected in polypeptide sequences is 263.4 ± 3.3, 30.9 ± 1.5 and 7.9 ± 0.4 mg kg-1 in samples of hydrolysates of bread digested with PEP, as produced from dough modified by TG, PEP and LA, respectively.; Conclusion: Enzymatic pre-modification of proteins during the process of dough fermentation decreases their immunoreactive potential, such that fewer peptides recognised by R5 antibodies are released during the digestion process from the bread matrix. Immunoreactive peptides are degraded more effectively when digestive enzymes are supported by the addition of PEP. © 2017 Society of Chemical Industry.; © 2017 Society of Chemical Industry.

Background: Water shortage during wheat vegetation causes changes in the composition of gliadins in grains, which can lead to changes in their immunoreactive properties.; Results: The investigated wheat cultivars exposed to water stress accumulated significantly lower amounts (P < 0.05) of gliadins and glutenins in grains. The composition of proteins accumulated in grains was also modified. Water shortage results in a decreased share of αβ and γ fractions in total gliadins. Grains of wheat cultivated under water stress contain significantly higher (P < 0.05) levels of ω-gliadins by 4.5% and 43.3% for Nawra and Tonacja cultivars, respectively. Water stress promotes an increase in the share of P and Q/E residues in gliadins. In protein samples R5 antibodies recognized increased amounts of gliadins matching the QQPFP sequence. Wheat proteins also reacted with IgE antibodies isolated from subjects allergic to gluten.; Conclusion: Cultivation of wheat under conditions of water stress results in the qualitative and quantitative changes of gliadins by increasing their immunoreactivity. © 2016 Society of Chemical Industry.; © 2016 Society of Chemical Industry.

BACKGROUND: This study addressed the characteristics of metabolites synthesized by Lactobacillus acidophilus 5e2, with particular attention paid to exopolysaccharides, biosurfactants, proline peptidases and antibacterial compounds. RESULTS: The strain Lb. acidophilus 5e2 synthesizes low-molecular-mass polysaccharides (340 kDa) constituted by glucose, galactose and glucosamine at a ratio of 3.3:2.8:1.0, as well as biosurfactants with a molecular mass of 32 kDa built from a protein fraction, a polysaccharide fraction and phosphate groups. It additionally synthesizes extra- and intracellular proline peptidases, including prolyl endopeptidase and thermostable low-molecular-mass (