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Título

In vitro digestion and immunoreactivity of β-lactoglobulin submitted to two-step enzymatic modification

AutorBattaglin Villas Boas, Mariana; Benedé, Sara ; Netto, Flavia Maria; Molina, Elena
Fecha de publicación2013
Citación2nd ICFD (2013)
ResumenThe allergenicity of β-Lactoglobulin (β-Lg) is mainly associated to its stable structure, which is resistant to heat and digestive process. Different treatments have been used to modify the protein structure and consequently their digestion and immunogenicity. In this study the effect of two-step enzymatic modification on the in vitro digestion and immunoreactivity of β-Lg was studied. The experimental conditions were: (a) polymerization of β-Lg using transglutaminase enzyme - TG (β-Lg 7% w/v; E:S 10 U TG g-1 of protein) followed by hydrolysis with bromelain (β-Lg 3% w/v, E:S 25 U g-1 of protein) or (b) hydrolysis of β-Lg with bromelain (β-Lg 3% w/v; E:S 25 U g-1 of protein) followed by polymerization with TG (10 U TG g-1 of protein). Following the enzymatic treatments, the samples were submitted to simulated gastric and duodenal digestion. Samples were characterized by SDS-PAGE and RP-HPLC and the immunorreactivity was measured by ELISA, using sera from milk allergic subjects. The results showed that untreated β-Lg was resistant to pepsin while the samples polymerized by TG pre (a) or post-hydrolysis (b) with bromelain showed an increase on the susceptibility to pepsin action, as evaluated by SDS-PAGE and RP-HPLC. For these treated samples, after gastrointestinal digestion, the chromatographic profile showed an increased intensity of the peaks corresponding to hydrophilic peptides, suggesting that digestion was more effective. By ELISA, the immunoreactivity of the samples modified by TG pre or post hydrolysis with bromelain was lower than of the untreated β-Lg (P < 0.05). A further reduction on immunorreactivity was observed after gastrointestinal digestion, with IgE response at least three times lower as compared to the digested from untreated β-Lg. These findings showed that the two-step enzymatic modification altered β-Lg structure and its susceptibility to gastrointestinal digestion and may have implications on the allergenic response of this protein.
DescripciónResumen del póster presentado al 2nd International Conference on Food Digestion celebrado en Madrid (España) del 6 al 8 de marzo de 2013.
URIhttp://hdl.handle.net/10261/114898
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