title: Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin.
abstract: The whey protein β-lactoglobulin (BLG) is highly allergenic. Lactic acid bacteria can degrade milk proteins. The capacity of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 to hydrolyse the major BLG epitopes (V41-K60; Y102-R124; L149-I162) and decrease their recognition by IgE of allergic patients was evaluated. The intensity of BLG degradation was analysed by Tricine SDS-PAGE and RP-HPLC. Peptides released were identified by LC-MS/MS and the hydrolysates were tested for their capacity to inhibit IgE binding by ELISA test. L. delbrueckii subsp. bulgaricus CRL 656 degraded BLG (35%, 8h). The sequence analysis of the released peptides indicated that this strain degraded three main BLG epitopes. BLG-positive sera (3-5year old children) were used for testing IgE binding inhibition of BLG hydrolysates from the Lactobacillus strain. The hydrolysates were less immuno-reactive (32%) than the heated BLG. L. delbrueckii subsp. bulgaricus CRL 656 could be used for developing hypoallergenic dairy products.
authors.affiliation: Centro de Referencia para Lactobacilos (CERELA)-CONICET, Chacabuco 145, 4000 San Miguel de Tucumán, Argentina.
authors.forename: Micaela
authors.initials: M
authors.lastname: Pescuma
authors.forename: Elvira María
authors.initials: EM
authors.lastname: Hébert
authors.forename: Hanitra
authors.initials: H
authors.lastname: Rabesona
authors.forename: Martine
authors.initials: M
authors.lastname: Drouet
authors.forename: Yvan
authors.initials: Y
authors.lastname: Choiset
authors.forename: Thomas
authors.initials: T
authors.lastname: Haertlé
authors.forename: Fernanda
authors.initials: F
authors.lastname: Mozzi
authors.forename: Graciela Font
authors.initials: GF
authors.lastname: de Valdez
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Chobert