Deamidation of gluten proteins and peptides decreases the antibody affinity in gluten analysis assays

Immunoreactivity of wheat proteins modified by hydrolysis and polymerisation

“…Similar properties of TG were observed by Fleckenstein et al [50]. In turn, Kanerva et al [51] demonstrated that chemical deamidation (0.1 mol/L, 100 °C, 2 h) of gluten proteins decreased the affinity of antibody to peptides. This process abolished the recognition of deamidated gluten peptides by omegagliadin and G12 antibody and decrease the recognition by R5 antibody.…”

“…However, peptides isolated from γ-gliadins and glutenins as a result of deamination with the participation of TG become immunodominant, strongly interacting with T cells, and are toxic for the patients with diagnosed coeliac disease [8,9]. The increase in the toxicity of peptides as a result of TG activity may reduce their detection, which results from their lower affinity for R5 antibody [51].…”

Malt hydrolysates for gluten-free applications: Autolytic and proline endopeptidase assisted removal of prolamins from wheat, barley and rye

“…The setup was calibrated by analysing the elution fractions of the wheat, barley and rye prolamin isolates (M w range w20,000e100,000) with SDS-PAGE, and by using low molecular mass prolamin peptide standards (9-mer and 33-mer, for sequences see Kanerva et al, 2011). The injection volume was 100 mL and the flow rate 0.5 mL/min.…”

Formation and properties of aqueous compatible colloidal blends between pre-gelatinized maize starch and zein

“…This higher net negative charges increases electrostatic repulsion and decreases hydrogen bonding between the zein molecules (Cabra et al, 2007;Kanerva et al, 2011). It is probable that the repulsion between the negatively charged zein molecules will keep them dispersed in the blend system and prevents aggregation.…”