Lactobacillus delbrueckii subsp. bulgaricus CRL 454 cleaves allergenic peptides of â-lactoglobulin

PESCUMA M.; HEBERT E.M.; HAERTLÉ T.; CHOBERT, J.M.; MOZZI, F.; FONT DE VALDEZ, G.

FOOD CHEMISTRY

ELSEVIER SCI LTD

Lugar: Amsterdam; Año: 2015 vol. 170 p. 407 - 414

0308-8146

Certain lactic acid bacteria can degrade milk proteins including the whey protein β-lactoglobulin (BLG), which is highly allergenic. The capacity of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 to hydrolyze the major BLG epitopes (V41?K60; Y102?R124; L149?I162) and decrease their recognition by IgE of allergic patients was evaluated. BLG degradation was analyzed 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 35% of BLG; the sequence analysis of the released peptides indicated the cleavage of three main BLG epitopes. BLG-positive sera from 3-5 years old children were used for testing IgE binding inhibition of the obtained BLG hydrolysates. The hydrolysates were less immuno-reactive (32%) than heated BLG. The strain L. delbrueckii subsp. bulgaricus CRL 656 could be used for developing hypoallergenic dairy products