Allergenicity of Bos d 5 in Children with Cow's Milk Allergy is Reduced by Transglutaminase Polymerization

Olivier, Celso Eduardo; Villas-Boas, Mariana Battaglin; Netto, Flávia Maria; Zollner, Ricardo de Lima

doi:10.1089/ped.2011.0101

Cited by 13 publications

(7 citation statements)

References 10 publications

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“…Some studies have determined the influence of crosslinking on the allergenic properties of proteins through the analysis of the IgE binding capacity by ELISA, Western blotting, or degranulation tests using basophil and mast cell cultures [ 30 , 31 , 32 ], but very few have determined their impact on other immune cells. Bai et al [ 33 ] observed that TG cross-linked tofu proteins reduced the levels of Th2 cytokines released by spleen cells from mice allergic to tofu protein cultured in vitro compared to native proteins.…”

Section: Resultsmentioning

confidence: 99%

IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility

et al. 2022

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Dairy foods are essential in the diet, although in some susceptible individuals they may cause allergy to cow’s milk proteins. Therefore, alternative methods are sought to reduce their allergenicity. Transglutaminase (TG) is widely used in dairy products mainly to improve texture. Although it has been claimed that TG can be used to modify the digestibility and allergenicity of foods, its impact within a real matrix has been rarely studied. The aim of this work was to assess the allergenic potential of crosslinked skim milk (SM), milk casein fraction (CN), and whey protein (WP). To this purpose, inhibition ELISA with sera from milk allergic patients, in vitro activation tests of mouse mast cells and splenocytes, and simulated gastrointestinal digestion assays were performed. The results showed that cross-linking increased the binding of IgE to WP, but decreased IgE-binding to SM and CN. However, no differences were observed in the ability of cross-linked proteins to induce mast cell degranulation compared to native proteins. The cross-linking of SM and CN reduced Th2 cytokine release from the splenocytes of sensitized mice. All TG-treated samples exhibited more resistance to in vitro digestion than the untreated proteins and the human IgE binding capacity after digestion was higher. In conclusion, TG treatment of milk proteins does not reduce the risk of eliciting allergic symptoms in cow’s milk allergic patients.

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Section: Resultsmentioning

confidence: 99%

IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility

et al. 2022

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“…30 Industrial dairy products may also be additional sources of immunologic sensitization due to the modification of native proteins. 31,32 To establish dietetic guidelines for a patient with milk intolerance, it is essential to know all of the components to which he/she is sensitive. When performing a clinical diagnosis of "lactose intolerance" based only on statistics, one assumes the risk of overlooking important comorbidities, such as allergies to whey proteins or cheese caseins.…”

Section: Discussionmentioning

confidence: 99%

Is it just lactose intolerance?

Olivier

Sl²,

Cr³

et al. 2012

allergy asthma proc

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Acquired delayed-onset hypolactasia is a common autosomal recessive condition. Cow's milk allergies, conversely, are less common conditions that may manifest with equivalent symptoms and are able to simulate and/or aggravate lactose intolerance. This study was designed to evaluate the contribution of IgE-mediated cow's milk sensitization to the symptomatology of adult patients with lactose-free diet refractory lactose intolerance. Forty-six adult patients with lactose intolerance and persistent symptoms despite a lactose-free diet underwent skin-prick test to investigate cow's milk, goat's milk, and soy protein-specific-IgE. SDS-PAGE immunoblotting was used to investigate the presence of cow's milk protein-specific IgE. The percentage of patients who had skin reactions to whole cow's milk, alpha-lactalbumin, beta-lactoglobulin, caseins, goat's milk, and soy was 69.5, 36.9, 56.5, 56.5%, 54.3, and 50%, respectively. The percentage of patients with immunoblot-detected IgE specific for alpha-lactalbumin, beta-lactoglobulin, caseins, and bovine serum albumin was 21.7, 63, 67.3, and 2.1%, respectively. IgE-mediated sensitization to cow's milk is a frequent comorbidity in subjects with lactose-free diet refractory lactose intolerance and is worth consideration in patients with this condition.

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“…Bovine β-LG is the most common allergenic protein that can cause milk allergy in susceptible individuals. α-Lactalbumin is another major allergenic protein in cow's milk containing both IgE and IgG epitopes and some of the conformational epitopes residues comprise of linear epitopes (Borad et al, 2017;Li et al, 2016;Olivier et al, 2012). Modification of the allergenic epitopes via enzymatic crosslinking could be exploited to develop hypoallergenic dairy products.…”

Section: Milk Allergymentioning

confidence: 99%

“…LAC/CA and TYR/CA had more potential in mitigating the allergenicity and IgE binding of the β-CN compared to TG-treated β-CN. Olivier et al (2012) evaluated the allergenicity of TG-crosslinked β-LG (Bos d 5) in symptomatic patients diagnosed with IgE-mediated Bos d 5 hypersensitivities. The results of skin prick test revealed a major reduction in the allergenicity of TGpolymerized β-LG compared to native β-LG in patients with IgE-mediated hypersensitivity.…”

Section: Milk Allergymentioning

confidence: 99%

Enzymatic crosslinking and food allergenicity: A comprehensive review

Ahmed

Chen

et al. 2021

Comp Rev Food Sci Food Safe

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Food allergy has become a major global public health concern. In the past decades, enzymatic crosslinking technique has been employed to mitigate the immunoreactivity of food allergens. It is an emerging non-thermal technique that can serve as a great alternative to conventional food processing approaches in developing hypoallergenic food products, owing to their benefits of high specificity and selectivity. Enzymatic crosslinking via tyrosinase (TYR), laccase (LAC), peroxidase (PO), and transglutaminase (TG) modifies the structural and biochemical properties of food allergens that subsequently cause denaturation and masking of the antigenic epitopes. LAC, TYR, and PO catalyze the oxidation of tyrosine side chains to initiate protein crosslinking, while TG initiates isopeptide bonding between lysine and glutamine residues. Enzymatic treatment produces a high molecular weight crosslinked polymer with reduced immunoreactivity and IgE-binding potential. Crosslinked allergens further inhibit mast cell degranulation due to the lower immunostimulatory potential that assists in the equilibration of T-helper (Th)1/Th2 immunobalance. This review provides an updated overview of the studies carried out in the last decade on the potential application of enzymatic crosslinking for mitigating food allergenicity that can be of importance in the context of developing hypoallergenic/non-allergenic food products.

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Allergenicity of Bos d 5 in Children with Cow's Milk Allergy is Reduced by Transglutaminase Polymerization

Cited by 13 publications

References 10 publications

IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility

IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility

Is it just lactose intolerance?

Enzymatic crosslinking and food allergenicity: A comprehensive review

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