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

Food Chemistry

Volumn 204, Issue , 2016, Pages 46-55

  Hu, Guanglan ^a   Zheng, Yuanrong ^b   Liu, Zhenmin ^b   Deng, Yun ^a   Zhao, Yanyun ^a,c  

^a SHANGHAI JIAO TONG UNIVERSITY   (China)

^b Technical Center   (China)

^c OREGON STATE UNIVERSITY   (United States)

Author keywords

Allergenicity; Far IR; High hydrostatic pressure; NMR; Protein structure; UV C; Casein

Indexed keywords

ALLERGENS; BINDING ENERGY; BINS; HYDRAULICS; HYDROSTATIC PRESSURE; NUCLEAR MAGNETIC RESONANCE;

ALLERGENICITY; GASTRIC FLUIDS; HIGH HYDROSTATIC PRESSURE; IGE BINDINGS; INTESTINAL FLUID; PROTEIN STRUCTURES; SULFHYDRYL CONTENT; SURFACE HYDROPHOBICITY;

CASEIN;

ALPHA CASEIN; IMMUNOGLOBULIN E; ALLERGEN; CASEIN;

ALLERGENICITY; ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; HYDROSTATIC PRESSURE; INFRARED RADIATION; INTESTINE FLUID; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN STRUCTURE; STOMACH JUICE; STRUCTURE ANALYSIS; TANDEM MASS SPECTROMETRY; ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY; ULTRASTRUCTURE; ULTRAVIOLET C RADIATION; ANIMAL; CHEMICAL PHENOMENA; CHEMISTRY; FOOD IRRADIATION; INFRARED SPECTROSCOPY; MILK; MILK HYPERSENSITIVITY; ULTRAVIOLET RADIATION;

ALLERGENS; 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;

EID: 84958984713     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.02.113     Document Type: Article

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