Centro de Referencia para Lactobacilos (CERELA)-CONICET, Chacabuco 145, 4000 San Miguel de Tucumán, Argentina.
Food Chem. 2011 Jul 15;127(2):487-92. doi: 10.1016/j.foodchem.2011.01.029. Epub 2011 Jan 9.
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.
乳清蛋白 β-乳球蛋白（BLG）高度致敏。乳酸菌可以降解牛奶蛋白。评估了德氏乳杆菌保加利亚亚种 CRL 656 水解主要 BLG 表位（V41-K60；Y102-R124；L149-I162）的能力，并降低其被过敏患者 IgE 的识别。通过 Tricine SDS-PAGE 和 RP-HPLC 分析 BLG 降解的强度。通过 LC-MS/MS 鉴定释放的肽，并用 ELISA 试验测试水解产物抑制 IgE 结合的能力。德氏乳杆菌保加利亚亚种 CRL 656 降解 BLG（35%，8h）。释放肽的序列分析表明，该菌株降解了三个主要的 BLG 表位。使用 BLG 阳性血清（3-5 岁儿童）测试乳酸菌菌株产生的 BLG 水解物对 IgE 结合的抑制作用。水解产物的免疫反应性（32%）低于加热的 BLG。德氏乳杆菌保加利亚亚种 CRL 656 可用于开发低致敏性乳制品。
