Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine beta-lactoglobulin

MICAELA PESCUMA; ELVIRA MARÍA HÉBERT; HANITRA RABESONA; MARTINE DRUET; YVAN CHOISET; TOMAS HAERTLE; FERNANDA MOZZI; GRACIELA FONT DE VALDEZ; JEAN-MARC CHOBERT

FOOD CHEMISTRY

ELSEVIER SCI LTD

Lugar: Amsterdam; Año: 2011 vol. 127 p. 487 - 492

0308-8146

Certain lactic acid bacteria can degrade milk proteins including the whey protein â- 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.