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Reduced IgE and IgG antigenic response to milk proteins hydrolysates obtained with the use of non-commercial serine protease from Yarrowia lipolytica
•Y. lipolytica protease expresses high proteolytic activity against milk proteins.•Hydrolysis caused degradation of WPC and casein at the level of 34,2% and 31,1%•Hydrolysis significantly reduced the antigenic response to bovine milk allergens.•The enzyme may be use for production of infant milk for...
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Published in: | Food chemistry 2020-01, Vol.302, p.125350-125350, Article 125350 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •Y. lipolytica protease expresses high proteolytic activity against milk proteins.•Hydrolysis caused degradation of WPC and casein at the level of 34,2% and 31,1%•Hydrolysis significantly reduced the antigenic response to bovine milk allergens.•The enzyme may be use for production of infant milk formulas.•Hydrolysates might be used for infants with a high risk of cow milk protein allergy.
The aim of the study was to investigate the use of serine protease from Yarrowia lipolytica yeast for reduction of milk proteins allergenicity. Whey protein concentrate (WPC-80), αs-casein and their hydrolysates were analyzed for the capacity to bind IgE and IgG antibodies present in sera from patients with cow milk protein allergy using a competitive ELISA. The hydrolysis of αs-casein and whey protein concentrate contributed to a significant reduction of their immunoreactive epitopes. In case of IgE antibodies, the lowest binding capacity was detected in the 24 h hydrolysates of both proteins in which the inhibition of the reaction was ≤20 and ≤68% for αs-casein and whey protein concentrate respectively. One hour hydrolysis of WPC-80 reduced the protein antigenicity, while the longer time (5 h) might lead to the exposure of new IgE – reactive epitopes. |
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ISSN: | 0308-8146 1873-7072 |
DOI: | 10.1016/j.foodchem.2019.125350 |