Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide

Martínez, María Julia; Martos, Gustavo; Molina, Elena; Pilosof, Ana M.R.

doi:10.1016/j.foodchem.2015.07.097

Cited by 18 publications

(9 citation statements)

References 33 publications

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“…It has been shown that the immunogenicity of β-LG glycated by carboxymethyl dextran was reduced . In the research of the influence of casein glycomacropeptide on the allergenicity of β-LG, a decrease of IgE-binding ability of β-LG in the presence of casein glycamacropeptide was found . According to the literature, the IgE-binding ability of glycated β-LG was dependent on the level of Maillard reaction .…”

Section: Resultsmentioning

confidence: 99%

“…28 In the research of the influence of casein glycomacropeptide on the allergenicity of β-LG, a decrease of IgE-binding ability of β-LG in the presence of casein glycamacropeptide was found. 29 According to the literature, the IgE-binding ability of glycated β-LG was dependent on the level of Maillard reaction. 30 In our study, the decreased IgE-binding ability of glycated β-LG under DHPM pretreatment was observed.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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The Reduction in the IgE-Binding Ability of β-Lactoglobulin by Dynamic High-Pressure Microfluidization Coupled with Glycation Treatment Revealed by High-Resolution Mass Spectrometry

Chen

Wang

et al. 2017

J. Agric. Food Chem.

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Our previous study indicated that pretreatment by dynamic high-pressure microfluidization (DHPM) and glycation with galactose was a promising method for decreasing the immunoglobulin E (IgE)-binding ability of β-lactoglobulin (β-LG). In this work, the conformational alteration of β-LG subjected to DHPM and glycation treatment was investigated in relation to IgE-binding ability by orbitrap mass spectrometry. After DHPM pretreatment, lower IgE-binding ability of glycated β-LG was observed with increasing pressures. Prior to DHPM pretreatment, 11 glycated sites were identified, while the number of glycation sites was increased to 12 after pretreatment. However, there was no significant difference of the glycation sites at the pressures of 50, 100, and 200 MPa, respectively. Average degree of substitution per peptide molecule of β-LG (DSP) was investigated to assess the degree of glycation per glycation site. All of the samples pretreated by DHPM exhibited a higher glycation level than those without DHPM pretreatment. The shielding effects of epitopes owing to glycation contributed to the reduction of IgE-binding capacity. Orbitrap mass spectrometry could provide a comprehensive understanding of the nature of protein glycation.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

The Reduction in the IgE-Binding Ability of β-Lactoglobulin by Dynamic High-Pressure Microfluidization Coupled with Glycation Treatment Revealed by High-Resolution Mass Spectrometry

Chen

Wang

et al. 2017

J. Agric. Food Chem.

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“…An in vitro simulated gastrointestinal digestion model is a swift and effective method to replace in vivo digestion . The digestion degree is greatly affected by factors such as digestion time, pH, the ratio of digestive enzymes to protein allergens, processing methods of the allergen, and the food matrix. − Previous research showed that glycation affects the digestion degree of proteins . The digestion degree can change the structure and molecular weight of proteins, affecting their allergenicity.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of the Reduced IgG/IgE Binding Abilities of Glycated β-Lactoglobulin and Its Digests through High-Resolution Mass Spectrometry

Wang

et al. 2021

J. Agric. Food Chem.

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Glycation between proteins and reducing sugars is the common chemical modification in food protein, and many studies have focused on the allergenicity of the glycated protein. However, a systemic study on the allergenicity change of its digests is lacking. In this work, we explored the change rule of the digestibility and allergenicity of glycated β-Lg during in vitro gastrointestinal digestion and interpreted the mechanism using high-resolution mass spectrometry. Glycation with arabinose increased the resistance of β-Lg to digestive enzyme, with a low hydrolysis value. Indirect competitive ELISA showed that the IgG/IgE binding rates of β-Lg were reduced after glycation and further reduced after digestion, in comparison with the digests of unglycated β-Lg. There are two reasons for this phenomenon. On the one hand, 11 glycated sites were determined in the lowest allergenicity arabinose-β-Lg conjugation (Ara-β-Lg), which was distributed in the IgG and IgE linear allergic epitopes of β-Lg. On the other hand, glycation masking linear allergenic epitopes had a more significant effect on reducing allergenicity in comparison to digestive enzyme hydrolysis. These results indicated that the allergenicity of Ara-β-Lg in the human body might be lower than that of unglycated β-Lg.

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“…There are some IgE‐binding epitopes but abrogated allergenicity to an allergy mouse model in the βLg hydrolysate using chymotrypsin , supporting that the accumulation of proteolysis product of intermediate size would contribute to the reduced allergenicity. As the presence of casein glycomacropeptide, commonly found in whey, modifies the peptide profiles and reduces IgE binding of βLg hydrolysate , the purity of βLg substrate might be a modifiable factor to allergenicity of βLg hydrolysate. Notably, the safety and effectiveness of our βLg hydrolysate was demonstrated in a pilot study on 16 CMA patients (threshold amount for βLg at baseline: 0.2–30 ml of milk equivalent) ; 8 of 10 patients who completed the pilot protocol showed an increase in the threshold amount for βLg without anaphylactic reaction throughout the study.…”

Section: Discussionmentioning

confidence: 99%

T‐cell epitope‐containing hypoallergenic β‐lactoglobulin for oral immunotherapy in milk allergy

Ueno

Kato

Ohnishi

et al. 2016

Pediatric Allergy Immunology

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Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide

Cited by 18 publications

References 33 publications

The Reduction in the IgE-Binding Ability of β-Lactoglobulin by Dynamic High-Pressure Microfluidization Coupled with Glycation Treatment Revealed by High-Resolution Mass Spectrometry

The Reduction in the IgE-Binding Ability of β-Lactoglobulin by Dynamic High-Pressure Microfluidization Coupled with Glycation Treatment Revealed by High-Resolution Mass Spectrometry

Mechanism of the Reduced IgG/IgE Binding Abilities of Glycated β-Lactoglobulin and Its Digests through High-Resolution Mass Spectrometry

T‐cell epitope‐containing hypoallergenic β‐lactoglobulin for oral immunotherapy in milk allergy

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