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Rapid proteolysis of gluten-derived immunogenic peptides in bread by actinidin in a combined in vivo and in vitro oro-gastrointestinal digestion model.
Jayawardana, Isuri A; Boland, Mike J; Loo, Trevor S; McNabb, Warren C; Montoya, Carlos A.
Afiliação
  • Jayawardana IA; Riddet Institute, Massey University, Te Ohu Rangahau Kai Facility, Palmerston North 4474, New Zealand. carlos.montoya@agresearch.co.nz.
  • Boland MJ; School of Food and Advanced Technology, College of Sciences, Massey University, Private Bag 11 222, Palmerston North, 4442, New Zealand.
  • Loo TS; Riddet Institute, Massey University, Te Ohu Rangahau Kai Facility, Palmerston North 4474, New Zealand. carlos.montoya@agresearch.co.nz.
  • McNabb WC; School of Fundamental Sciences, College of Sciences, Massey University, Palmerston North 4442, New Zealand.
  • Montoya CA; Riddet Institute, Massey University, Te Ohu Rangahau Kai Facility, Palmerston North 4474, New Zealand. carlos.montoya@agresearch.co.nz.
Food Funct ; 13(10): 5654-5666, 2022 May 23.
Article em En | MEDLINE | ID: mdl-35510393
ABSTRACT
This study aimed to determine the ability of actinidin, a cysteine protease in green kiwifruit (Actinidia deliciosa), to hydrolyse wheat proteins and gluten-derived immunogenic peptides from a commonly consumed food matrix (bread) using a combined in vivo and in vitro oro-gastrointestinal tract (GIT) model. A chewed and spat composite bolus of bread was in vitro digested with or without purified actinidin using a human gastric simulator (HGS). Gastric digestion was conducted for 150 min with gastric emptying occurring at different time points. Emptied samples were immediately digested under simulated small intestinal conditions. Gastric and small intestinal aliquots were collected to quantify peptide profiles and nine marker immunogenic peptides (by untargeted and targeted mass spectrometry, respectively), R5 epitopes (by monoclonal antibody-based competition assay), and free amino groups released by digestion (by the o-phthaldialdehyde method). There was a significant effect (P < 0.05) of actinidin and digestion time on the hydrolysis of wheat proteins and the amount of gluten R5 epitopes of that material emptying the HGS. Actinidin accelerated 1.2-fold the gastric hydrolysis of wheat proteins during the first 20 min of digestion, which was reflected in a faster (5.5 µg min-1) reduction in the evolution of R5 epitopes. Actinidin accelerated (P < 0.05) the rate of disappearance of most of the immunogenic marker peptides. For example, in the first 20 min of small intestinal digestion, the 33-mer peptide decreased (P < 0.05) 2-fold faster (0.25 vs. 0.12 µg g-1 of bread per min) in the presence of actinidin than in the control. Untargeted peptidomics showed actinidin decreased the amounts of known immunogenic peptides in the simulated small intestinal digestion. These findings demonstrated that actinidin accelerates the hydrolysis of wheat proteins and known gluten immunogenic peptides in a commonly consumed food matrix (bread) in a combined in vivo and in vitro oro-GIT digestion model.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Actinidia / Glutens Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Actinidia / Glutens Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2022 Tipo de documento: Article