Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients

A Taheri-Kafrani, JC Gaudin, H Rabesona… - Journal of Agricultural …, 2009 - ACS Publications
β-Lactoglobulin (β-LG) is one of the cow's major milk proteins and the most abundant whey
protein. This globular protein of about 18 kDa is folded, forming a β-barrel (or calyx) …

Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin

BM Ehn, B Ekstrand, U Bengtsson… - Journal of Agricultural …, 2004 - ACS Publications
The effect of heat treatment on the IgE binding ability of β-lactoglobulin, as pure protein or in
whole milk, was studied by inhibition of IgE antibody binding using FEIA-CAP inhibition. A …

Modification of IgE binding to β-lactoglobulin by fermentation and proteolysis of cow's milk

BM Ehn, T Allmere, E Telemo… - Journal of Agricultural …, 2005 - ACS Publications
The effect of fermentation by Lactobacilli and of proteolytic hydrolysis of whole milk on the
IgE binding ability of β-lactoglobulin was studied using an ELISA inhibition assay. Sera from …

Effect of heat treatment and enzymatic digestion on the B cell epitopes of cow's milk proteins

Y Morisawa, A Kitamura, T Ujihara… - Clinical & …, 2009 - Wiley Online Library
Background Processing milk leads to changes in clinical allergenicity. However, the
mechanism by which heat treatment affects the allergenicity of milk proteins is not fully …

Glycation of the major milk allergen β‐lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation

M Perusko, M van Roest… - Molecular nutrition & …, 2018 - Wiley Online Library
Scope During food processing, the Maillard reaction (МR) may occur, resulting in the
formation of glycated proteins. Glycated proteins are of particular importance in food …

Specific and sensitive ELISA for measurement of IgE-binding variations of milk allergen β-lactoglobulin in processed foods

J Orcajo, M Lavilla, I Martínez-de-Marañón - Analytica chimica acta, 2019 - Elsevier
Immunochemical detection of food allergens is usually based on the use of polyclonal or
monoclonal immunoglobulins G (IgG) antibodies. However, due to differences in epitopes …

Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin

M Corzo-Martínez, AC Soria, J Belloque… - International Dairy …, 2010 - Elsevier
Immunoreactivity of bovine β-lactoglobulin (β-Lg) hydrolysates obtained after a simulated
gastrointestinal digestion and previously glycated via Maillard reaction with galactose …

Allergy to the heat-labile proteins α-lactalbumin and β-lactoglobulin in mare's milk

H Gall, CM Kalveram, H Sick, W Sterry - Journal of allergy and clinical …, 1996 - Elsevier
BACKGROUND: Allergy to mare's milk is rare. Recently, however, mare's milk has been
recommended for treatment of various ailments by practitioners of “alternative medicine,” …

Structure and function of proteins involved in milk allergies

S Sharma, P Kumar, C Betzel, TP Singh - Journal of Chromatography B …, 2001 - Elsevier
Allergy to milk proteins has been defined as any adverse reaction mediated by
immunological mechanisms to one or several of proteins found in milk. The milk allergy has …

Allergy to Bovine â–Lactoglobulin: Specificity of Human IgE Using Cyanogen Bromide–Derived Peptides

I Sélo, L Négroni, C Créminon, M Yvon… - International archives of …, 1998 - karger.com
Abstract Background: Bovine β–Lactoglobulin (Blg) is a major allergen involved in allergy to
cow's milk proteins. Hydrolyzing Blg did not totally suppress its allergenicity; moreover its …