Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/242110
Type: Artigo
Title: Epitopes resistance to the simulated gastrointestinal digestion of beta-lactoglobulin submitted to two-step enzymatic modification
Author: Villas-Boas, Mariana Battaglin
Benedé, Sara
Zollner, Ricardo de Lima
Maria Netto, Flavia
Molina, Elena
Abstract: The effects beta-lactoglobulin (beta Lg) hydrolysis with alcalase or bromelain and its association with polymerization by transglutaminase (TG) on both the protein antigenicity and resistance of epitopes to in vitro digestion were investigated. Despite the polymerization with TG altered the gastric and gastrointestinal (GI) digestion patterns of the hydrolysates with bromelain, no changes were observed with alcalase. Before and after in vitro digestion, native beta Lg showed the highest IgE-binding capacity, evaluated using sera from milk-allergic patients, while the enzymatic treatments-associated or not-reduced the beta Lg antigenicity response. Seven and four epitopes were found after gastric and GI digestion of native beta Lg, respectively. After gastric digestion of the hydrolysates with bromelain, two epitopes were identified, being Tyr(42)-Leu(54) resistant to GI digestion. No epitope was found in GI digested products of hydrolysates with alcalase. Hydrolysis associated or not with polymerization reduced the number of epitopes and the IgE-binding capacity of the samples
Subject: Hidrólise
Country: Reino Unido
Editor: Elsevier
Citation: Epitopes Resistance To The Simulated Gastrointestinal Digestion Of Beta-lactoglobulin Submitted To Two-step Enzymatic Modification. Elsevier Science Bv, v. 72, p. 191-197 JUN-2015.
Rights: fechado
Identifier DOI: 10.1016/j.foodres.2015.03.044
Address: http://www.sciencedirect.com/science/article/pii/S0963996915001490
Date Issue: 2015
Appears in Collections:FCM - Artigos e Outros Documentos

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