Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and alpha s-casein

作者：Babij Konrad^*; Bajzert Joanna; Dabrowska Anna; Szoltysik Marek; Zambrowicz Aleksandra; Lubec Gert; Stefaniak Tadeusz; Willak Janc Ewa; Chrzanowska Jozefa

来源：Amino Acids, 2015, 47(11): 2335-2343.

DOI：10.1007/s00726-015-2013-2

• Cow's milk allergy
• Whey protein hydrolysates
• alpha s-casein hydrolysates
• Cucurbita ficifolia
• Serine protease

In the present study the effect of hydrolysis with non-commercial Cucurbita ficifolia serine protease on a reduction of the IgE and IgG binding capacity of whey protein concentrate and alpha s-casein was investigated. The intensity of the protein degradation was analyzed by the degree of hydrolysis, the free amino groups content and RP-HPLC. The ability to bind the antibodies by native proteins and their hydrolysates was determined using a competitive ELISA test. Deep hydrolysis contributed to a significant reduction of immunoreactive epitopes present in WPC. In the case of IgE and IgG present in the serum pool of children with CMA, the lowest binding capacity was detected in the 24 h WPC hydrolysate, where the inhibition of the reaction with native WPC was a parts per thousand currency sign23 and a parts per thousand currency sign60 %, respectively. The analysis of the IgG reactivity in the antiserum of the immunized goat showed that the lowest antibody binding capacity was exhibited also by 24 h WPC hydrolysate at a concentration of 1000 mu g/ml where the inhibition of the reaction with nWPC was a parts per thousand currency sign47 %. One-hour hydrolysis of alpha-casein was sufficient to significant reduction of the protein antigenicity, while the longer time (5 h) of hydrolysis probably lead to the appearance of new epitopes reactive with polyclonal.

• 出版日期2015-11