TitleStructure and IgE-binding properties of α-casein treated by high hydrostatic pressure, UV-C, and far-IR radiations.
Publication TypeJournal Article
Year of Publication2016
AuthorsHu, G, Zheng, Y, Liu, Z, Deng, Y, Zhao, Y
JournalFood Chem
Date Published2016 Aug 01
KeywordsAllergens, Animals, Caseins, Electrophoresis, Polyacrylamide Gel, Food Irradiation, Hydrophobic and Hydrophilic Interactions, Hydrostatic Pressure, Immunoglobulin E, Microscopy, Atomic Force, Milk, Milk Hypersensitivity, Spectroscopy, Fourier Transform Infrared, Tandem Mass Spectrometry, Ultraviolet Rays

α-Casein was treated by high hydrostatic pressure (HHP), UV-C, or far-IR (FIR). These treatments increased roughness, α-helicity, and β-turn, but decreased β-sheet and IgE-binding reactivity. One 5-min cycle at 600-MPa pressure caused maximum α-helicity, β-turn, and surface hydrophobicity (Ho), but minimum stimulated intestinal fluid from α-casein. UV-C (15min) produced the maximum kurtosis, free sulfhydryl content (FSC), and stimulated intestinal fluid, minimum Ho, R, and simulated gastric fluid. FIR (15min) caused the minimum α-helicity and FSC, but maximum R and β-sheet. The NMR peaks of the main allergenic characteristics affected were 15-17, 23-26, 40, 53, 59 and 85-88, respectively. Generally, all treatments decreased the allergenicity of α-casein by modifying its morphology, ultrastructure, characteristic domains, and peptides. Based on the stimulated digestion tests, UV-C (15min) was more efficient for lowering α-casein allergenicity, thus decreasing the allergenicity of milk.

Alternate JournalFood Chem
PubMed ID26988474