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Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid
Author(s) -
Stănciuc Nicoleta,
Creţu Alexandra Andreea,
Banu Iuliana,
Aprodu Iuliana
Publication year - 2018
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.8813
Subject(s) - antigenicity , chemistry , epitope , protein tertiary structure , quenching (fluorescence) , egg white , molecule , protein secondary structure , antigen , fluorescence spectroscopy , food science , biochemistry , fluorescence , organic chemistry , biology , genetics , physics , quantum mechanics
BACKGROUND Ovomucoid (OVM) is the dominant allergen found in egg white. The heat‐induced changes on chicken OVM structure and antigenic properties were assessed at acidic, neutral and alkaline pH values. RESULTS The fluorescence spectroscopy measurements indicated changes in the conformation of OVM caused by both pH and thermal treatment. The OVM molecule exhibited higher exposure of hydrophobic residues at 7.0, as indicated by the synchronous spectra, intrinsic fluorescence and quenching experiments. When heating the protein at pH 9.5, the molecular structure appeared more compact. The antigenic properties of OVM, estimated through the enzyme‐linked immunosorbent assay, appeared not to be sensitive to heat at pH 7.0 and 4.5. Single molecule level investigations indicated that the secondary and tertiary structure of OVM was affected by the thermal treatment. CONCLUSIONS Experimental results indicated over 90% reduction of the antigenicity at pH 9.5 and temperature of 100 °C. Significant changes of the linear epitopes exposure and location of the conformational epitopes were highlighted after performing heating molecular dynamics simulations of OVM from 25 °C to 100 °C. © 2017 Society of Chemical Industry