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Reducing the allergenicity of whey proteins while improving their functional properties and bioactivity using
Lidong Pang1, Zhen Huang1, Runze Li1
1Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, China.
Abstract:
The aim of this study was to investigate the changes in functional properties, bioactivity and allergenicity of whey protein hydrolysates (WPH) prepared by combinations of endopeptidases and exopeptidases. The immunoglobulin E-binding capacity of WPH made by combining pineapple protease and papain with the exopeptidase ProteAXH was reduced by 47.62 % and 51.91 %, respectively, and the emulsification performance was improved by about 40 % in both cases. Multispectral results indicated that the addition of ProteAXH increased the disruption of protein conformation. Liquid chromatography coupled with tandem mass spectrometry analysis revealed that the exopeptidase altered the hydrolysis sites of the protein. Further combination with bioinformatics revealed that increased conformational disruption and altered linear epitope hydrolysis sites decreased the allergenicity of WPH. Meanwhile, the structural changes also increased the release of emulsifying peptides and bioactive peptides, thus improving the functional properties. In conclusion, these two WPHs combine hypoallergenicity with excellent functional properties and bioactivity.
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