CENTRO DE REFERENCIA PARA LACTOBACILOS
Unidad Ejecutora - UE
Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine b-lactoglobulin
PESCUMA, M.; HEBERT, E. M.; RABESONA, H.; DROUET, M.; CHOISET, I.; HAERTLÉ, T.; MOZZI, F; FONT DE VALDEZ, G.; CHOBERT, J.M.
ELSEVIER SCI LTD
Año: 2011 vol. 127 p. 487 - 487
The whey protein b-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%, 8 h). The sequence analysis of the released peptides indicated that this strain degraded three main BLG epitopes. BLG-positive sera (3?5 year 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.