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

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 αs-casein was investigated. The intensity of the protein degradation was analyzed by the degree of hydrolysis, the...

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Autores principales: Babij, Konrad, Bajzert, Joanna, Dąbrowska, Anna, Szołtysik, Marek, Zambrowicz, Aleksandra, Lubec, Gert, Stefaniak, Tadeusz, Willak-Janc, Ewa, Chrzanowska, Józefa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Vienna 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4617856/
https://www.ncbi.nlm.nih.gov/pubmed/26036686
http://dx.doi.org/10.1007/s00726-015-2013-2
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author Babij, Konrad
Bajzert, Joanna
Dąbrowska, Anna
Szołtysik, Marek
Zambrowicz, Aleksandra
Lubec, Gert
Stefaniak, Tadeusz
Willak-Janc, Ewa
Chrzanowska, Józefa
author_facet Babij, Konrad
Bajzert, Joanna
Dąbrowska, Anna
Szołtysik, Marek
Zambrowicz, Aleksandra
Lubec, Gert
Stefaniak, Tadeusz
Willak-Janc, Ewa
Chrzanowska, Józefa
author_sort Babij, Konrad
collection PubMed
description 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 αs-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 ≤23 and ≤60 %, 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 μg/ml where the inhibition of the reaction with nWPC was ≤47 %. One-hour hydrolysis of α-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.
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spelling pubmed-46178562015-10-28 Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein Babij, Konrad Bajzert, Joanna Dąbrowska, Anna Szołtysik, Marek Zambrowicz, Aleksandra Lubec, Gert Stefaniak, Tadeusz Willak-Janc, Ewa Chrzanowska, Józefa Amino Acids Original Article 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 αs-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 ≤23 and ≤60 %, 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 μg/ml where the inhibition of the reaction with nWPC was ≤47 %. One-hour hydrolysis of α-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. Springer Vienna 2015-06-03 2015 /pmc/articles/PMC4617856/ /pubmed/26036686 http://dx.doi.org/10.1007/s00726-015-2013-2 Text en © The Author(s) 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Babij, Konrad
Bajzert, Joanna
Dąbrowska, Anna
Szołtysik, Marek
Zambrowicz, Aleksandra
Lubec, Gert
Stefaniak, Tadeusz
Willak-Janc, Ewa
Chrzanowska, Józefa
Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
title Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
title_full Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
title_fullStr Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
title_full_unstemmed Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
title_short Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
title_sort hydrolysis with cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4617856/
https://www.ncbi.nlm.nih.gov/pubmed/26036686
http://dx.doi.org/10.1007/s00726-015-2013-2
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