title: 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.
authors.affiliation: Department of Food Science and Technology, Shanghai Jiao Tong University, 800 Dongchuang Road, Shanghai 200240, China.
authors.forename: Guanlan
authors.initials: G
authors.lastname: Hu
authors.affiliation: State Key Laboratory of Dairy Biotechnology, Dairy Research Institute, Bright Dairy & Food Co., Ltd, Shanghai 200436, China.
authors.forename: Yuanrong
authors.initials: Y
authors.lastname: Zheng
authors.affiliation: State Key Laboratory of Dairy Biotechnology, Dairy Research Institute, Bright Dairy & Food Co., Ltd, Shanghai 200436, China.
authors.forename: Zhenmin
authors.initials: Z
authors.lastname: Liu
authors.affiliation: Department of Food Science and Technology, Shanghai Jiao Tong University, 800 Dongchuang Road, Shanghai 200240, China. Electronic address: foodsjtu@sjtu.edu.cn.
authors.forename: Yun
authors.initials: Y
authors.lastname: Deng
authors.affiliation: Department of Food Science and Technology, Shanghai Jiao Tong University, 800 Dongchuang Road, Shanghai 200240, China; Department of Food Science & Technology, Oregon State University, Corvallis, OR 97331, USA.
authors.forename: Yanyun
authors.initials: Y
authors.lastname: Zhao
mesh_terms: D000485:Allergens / Q000737:chemistry*; D000818:Animals; D002364:Caseins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005514:Food Irradiation; D057927:Hydrophobic and Hydrophilic Interactions; D006874:Hydrostatic Pressure; D007073:Immunoglobulin E / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D008892:Milk / Q000737:chemistry; D016269:Milk Hypersensitivity / Q000517:prevention & control; D017550:Spectroscopy, Fourier Transform Infrared; D053719:Tandem Mass Spectrometry; D014466:Ultraviolet Rays
chemical_list: D000485:Allergens; D002364:Caseins; D007073:Immunoglobulin E
keywords: Allergenicity; Far-IR; High hydrostatic pressure; NMR; Protein structure; UV-C; α-Casein