Ultrasonic Pretreatment Combined with Dry-State Glycation Reduced the Immunoglobulin E/Immunoglobulin G-Binding Ability of α-Lactalbumin Revealed by High-Resolution Mass Spectrometry
| Autor: | Igor A. Kaltashov, Zong-cai Tu, Hui Wang, Chendi Niu, Xiao-mei Sha, Honglin Yao, Liu Jun, Yan-hong Shao, Guang-xian Liu |
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| Rok vydání: | 2018 |
| Předmět: |
Glycosylation
Sonication Peptide Immunoglobulin E Mass spectrometry Mass Spectrometry Immunoglobulin G chemistry.chemical_compound 0404 agricultural biotechnology Glycation Animals Ultrasonics chemistry.chemical_classification Lactalbumin Chromatography biology 04 agricultural and veterinary sciences General Chemistry 040401 food science Milk chemistry Galactose biology.protein General Agricultural and Biological Sciences |
| Zdroj: | Journal of Agricultural and Food Chemistry. 66:5691-5698 |
| ISSN: | 1520-5118 0021-8561 |
| Popis: | Bovine α-lactalbumin (α-LA) is one of major food allergens in cow’s milk. The present work sought to research the effects of ultrasonic pretreatment combined with dry heating-induced glycation between α-LA and galactose on the immunoglobulin E (IgE)/immunoglobulin G (IgG)-binding ability and glycation extent of α-LA, determined by inhibition enzyme-linked immunosorbent assay and high-resolution mass spectrometry, respectively. The IgE/IgG-binding ability of glycated α-LA was significantly decreased as a result of ultrasonic pretreatment, while the average molecular weight, incorporation ratio (IR) value, location and number of glycation sites, and degree of substitution per peptide (DSP) value were elevated. When the mixtures of α-LA and galactose were pretreated by ultrasonication at 150 W/cm2, glycated α-LA possesses seven glycation sites, the highest IR and DSP values, and the lowest IgE/IgG-binding ability. Therefore, the decrease in the IgE/IgG-binding ability of α-LA depends upon not only the shield... |
| Databáze: | OpenAIRE |
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