2005
DOI: 10.1016/j.idairyj.2004.09.001
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Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes

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Cited by 35 publications
(28 citation statements)
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“…The focus is on milk allergy and, hence, on planning suitable strategies to improve milk digestibility and tolerance. In particular, making use of the proteolytic system of lactic acid bacteria [78] or of proteases from non-human source, like papain or bromelain, the antigenicity of specific peptides could be reduced. As peptide permeation can be chemically enhanced or reduced by surfactant-like agents, strategies can also be planned to modulate the delivery and absorption of selected sequences [79].…”
Section: Resultsmentioning
confidence: 99%
“…The focus is on milk allergy and, hence, on planning suitable strategies to improve milk digestibility and tolerance. In particular, making use of the proteolytic system of lactic acid bacteria [78] or of proteases from non-human source, like papain or bromelain, the antigenicity of specific peptides could be reduced. As peptide permeation can be chemically enhanced or reduced by surfactant-like agents, strategies can also be planned to modulate the delivery and absorption of selected sequences [79].…”
Section: Resultsmentioning
confidence: 99%
“…These results suggested that the enzymatic hydrolysis could partly reduce the allergenicity of β-LG. Prioult et al (2005) studied the allergenicity of acidic peptides from bovine β-LG by hydrolysis with Bifidobacterium lactis NCC362 enzymes, and their results indicated that the peptide fragments significantly up-regulated IFN-γ and IL-10 production and down-regulated IL-4 secretion by murine splenocytes. The β-LG-derived peptides released after B. lactis hydrolysis could therefore be used as supplement in hypoallergenic infant formulas to stimulate oral tolerance induction to β-LG in babies at risk of allergy.…”
Section: Enzymatic Hydrolysismentioning
confidence: 99%
“…Hydrolysis of BLG by trypsin/chymotrypsin reduces its allergenicity, but also unmasks hidden allergenic peptides, which have been found to be recognised by specific IgE of allergic patients (Selo et al, 1999). Three tryptic peptides from BLG have been identified as major allergenic epitopes (V41-K60; Y102-R124; L149-I162) (Prioult, Pecquet, & Fliss, 2005). These immuno-reactive structures are distributed rather regularly along the BLG molecule; some of them are short linear sequences, whereas others are large fragments forming conformational epitopes.…”
Section: Introductionmentioning
confidence: 99%