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Reduced IgE/IgG binding capacities of bovine α-Lactalbumin by glycation after dynamic high-pressure microfluidization pretreatment evaluated by high resolution mass spectrometry
- Source :
- Food Chemistry. 299:125166
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- Dynamic high-pressure microfluidization (DHPM) pretreatment and glycation with lactose were employed to modify α-Lactalbumin (α-LA) with respect to the IgE/IgG binding capacities. No significant difference on incorporation ratio value of glycated α-LA was observed with and without DHPM pretreatment. However, IgE/IgG binding capacities of α-LA were decreased after glycation and DHPM pretreatment promoted the reduction. The lowest IgE/IgG binding capacities of glycated α-LA were obtained by DHPM pretreatment at 110 MPa. Native α-LA was mainly glycated at K62, K94, K98, whereas glycation sites and degree of substitution per peptide (DSP) were added after DHPM treatment. Therefore, the reduced IgE/IgG binding capacities of α-LA was attributed to the characteristics of glycated sites, including the amount, location, and DSP values. Interestingly, K98 played the most important role in decreasing IgE/IgG binding capacities of α-LA. The study revealed that glycation combined with DHPM was a promising way to decrease the allergenicity of proteins.
- Subjects :
- Enzyme-Linked Immunosorbent Assay
Lactose
Peptide
Immunoglobulin E
01 natural sciences
Mass Spectrometry
Analytical Chemistry
chemistry.chemical_compound
0404 agricultural biotechnology
Glycation
Pressure
Animals
Humans
Food-Processing Industry
chemistry.chemical_classification
Lactalbumin
biology
Ratio value
Lysine
010401 analytical chemistry
04 agricultural and veterinary sciences
General Medicine
Allergens
040401 food science
0104 chemical sciences
chemistry
Biochemistry
IgG binding
Immunoglobulin G
High pressure
biology.protein
Cattle
Rabbits
Food Hypersensitivity
Food Science
Subjects
Details
- ISSN :
- 03088146
- Volume :
- 299
- Database :
- OpenAIRE
- Journal :
- Food Chemistry
- Accession number :
- edsair.doi.dedup.....0bde185c1196bf5c359e71b21cde4032