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Description

Peanut allergy is one of most severe and persistent food allergies. While Alcalase hydrolysis significantly reduces major allergenic proteins, residual allergenicity remains a concern. This study aimed to identify resistant proteins/peptides contributing to the allergenicity of extensively hydrolyzed peanut protein concentrate (PPC). Peanut protein concentrate (PPC) at concentration of 10% was hydrolyzed with 4% Alcalase for 2-8 hours. The degree of hydrolysis (DH) increased from 34.91% to 44.68% accompanied with decreased IgE-binding. However, the SDS-PAGE and Western blot of both supernatants and precipitates with pooled sera from 7 peanut sensitive patients confirmed the presence of resistant allergenic peptides in the extensively hydrolyzed PPC, particularly, the two proteins/peptides with molecular weights 22.5kDa and 12.65kDa. To further characterize these resistant proteins/peptides, gel samples of these two peptides were sent a commercial service lab for sequencing using liquid chromatography-mass spectrometry (LC-MS/MS). The sequences obtained do not match any sequences of the native proteins in the PPC. This suggests that they are the peptides formed during Alcalase hydrolysis of larger proteins. Findings indicate that Alcalase hydrolysis alone is insufficient to eliminate peanut allergenicity. Further strategies are necessary to break down or mask all immunoreactive epitopes, enhancing the safety of peanut-based products.

Publication Date

4-1-2025

Keywords

Peanut allergy, Alcalase hydrolysis, Resistant proteins, Immunoreactivity

Identification of Allergenic Peanut Protein and Peptides Resistant to Alcalase Hydrolysis

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