Structure and IgE-binding properties of α-casein treated by high hydrostatic pressure, UV-C, and far-IR radiations

Abstract

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.

Keywords: Allergenicity; Far-IR; High hydrostatic pressure; NMR; Protein structure; UV-C; α-Casein.