期刊
JOURNAL OF FOOD BIOCHEMISTRY
卷 45, 期 1, 页码 -出版社
WILEY
DOI: 10.1111/jfbc.13539
关键词
Alaska Pollock; glycation; IgE; IgG binding capacity; parvalbumin; structural changes
资金
- National Natural Science Foundation of China [31760445, 31960457]
- Agriculture Research System of China [CARS-45]
The study showed that glycation with different reducing sugars affected the immunoglobulin binding capacity and structure changes of PV from Alaska Pollock, indicating potential allergenicity in glycated PV.
Parvalbumin (PV) is one of the major allergens in fish. The aim of our present work was to research the influence mechanism of glycation with different reducing sugars (glucose, fructose, ribose, lactose, and galactose) on the immunoglobulin E (IgE) and immunoglobulin G (IgG) binding capacity and structure changes of PV in Alaska Pollock. PV glycated with glucose or fructose (PV-Glu/ PV-Fru) exhibited the higher IgE/IgG binding capacities than that of ribose, galactose, or lactose. During glycation, the lysine (Lyr), tyrosine (Tyr), and phenylalanine (Phe) of PV were gradually embed into core area of three-dimensional structure of protein, which reflected in the ultraviolet (UV) spectrum and fluorescence spectra. Moreover, the increase of surface hydrophobicity had confirmed the conformation alteration of glycated PV. These results suggest that there is a specific association among the change of PV in glycation and in potential allergenicity. The types and conformation of reducing sugar greatly influenced the IgE/IgG binding capacity of PV, and glycation with ribose and galactose was a promising approach for reducing the IgE/IgG binding capacity of PV from Alaska Pollock. Practical applications Parvalbumin (PV), the major allergen of fish, it can not only maintain the physiological activity of cells, but also cross react with human amyloid protein to alleviate Alzheimer's disease and Parkinson's syndrome. This study revealed that the IgE/IgG binding capacity and structural changes of PV from Alaska Pollock modified by glycation with different reducing sugars. This will help us to understand the sensitization and structural change of the glycated products after the reaction of PV with different reducing sugars. It provides an effective carbonyl source for the preparation of low antigenicity PV based on glycation and lays a foundation for glycation modification of other food allergens.
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