The challenge of cow milk protein allergy

El-Agamy, El-Sayed I.

doi:10.1016/j.smallrumres.2006.09.016

Cited by 253 publications

(176 citation statements)

References 57 publications

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“…β-Casein is the major fraction in caprine casein, which is similar to human casein and different from bovine casein (El-Agamy, 2006). Caprine milk lacks α s1 -casein and this may explain why caprine milk is less allergenic than bovine milk (Lara-Villoslada et al 2005).…”

Section: Comparison Of the 2-de Patterns And Identification Of Proteimentioning

confidence: 99%

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Hinz

O’Connor

Huppertz

et al. 2012

Journal of Dairy Research

125

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Proteomic analysis of bovine, caprine, buffalo, equine and camel milk highlighted significant interspecies differences. Camel milk was found to be devoid of β-lactoglobulin, whereas β-lactoglobulin was the major whey protein in bovine, buffalo, caprine, and equine milk. Five different isoforms of κ-casein were found in camel milk, analogous to the micro-heterogeneity observed for bovine κ-casein. Several spots observed in 2D-electrophoretograms of milk of all species could tentatively be identified as polypeptides arising from the enzymatic hydrolysis of caseins. The understanding gained from the proteomic comparison of these milks may be of relevance both in terms of identifying sources of hypoallergenic alternatives to bovine milk and detection of adulteration of milk samples and products.

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Section: Comparison Of the 2-de Patterns And Identification Of Proteimentioning

confidence: 99%

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Hinz

O’Connor

Huppertz

et al. 2012

Journal of Dairy Research

125

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“…Cow's milk is widely used in the production of infant foods; however, also, it is one of the most common food allergies in childhood. Cow's milk allergy is clinically an abnormal immunological reaction to cow milk proteins due to IgE-mediated reactions induced by one or more milk proteins (El-Agamy, 2007), such as the well-known two components (α-lactalbumin and β-lactoglobulin) of whey proteins. Whey proteins are protein ingredients widely used in food products, especially in the manufacture of infant milk powder.…”

Section: Introductionmentioning

confidence: 99%

Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity

Zhang

Wang

Liu

et al. 2016

CyTA - Journal of Food

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(2016) Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced invitro antigenicity, CyTA -Journal of Food, 14:4, 572-577, DOI: 10.1080/19476337.2016 To link to this article: https://doi.org/10. 1080/19476337.2016 In this study, two horseradish peroxidase (HRP)-based modifications were used to treat whey protein isolate (WPI) and skim milk powder (SKMP) at protein concentration of 50 g/L, pH 7.0, and 37°C, via dityrosine formation in protein molecules. When HRP, glucose oxidase, and glucose were used to treat WPI and SKMP, suitable usages of HRP, glucose oxidase, and glucose, and reaction time were selected from single factor trials based on relative dityrosine contents of the modified products. After that, the selected HRP plus the calculated H 2 O 2 were used to treat WPI and SKMP. Electrophoretic analysis demonstrated that the modified products contained some crosslinked proteins with greater molecular weights. Other analyses showed that the modified products had more ordered secondary structure, and higher in vitro α-lactalbumin and β-lactoglobulin antigenicity than the respective substrates. HRP-glucose oxidase-glucose system was more potent than HRP-H 2 O 2 system to enhance in vitro antigenicity of WPI and SKMP.Dos modificaciones de peroxidasa de rábano picante resultan en dos productos proteínicos con estructura secundaria ordenada y una antigenicidad in vitro mejorada RESUMEN En este estudio se utilizaron dos modificaciones de peroxidasa de rábano picante (HRP) para tratar aislado proteínico de lactosuero (WPI) y leche desnatada en polvo (SKMP) con una concentración proteínica de 50 g/L, pH 7,0 y 37°C, mediante formación de ditirosina en moléculas proteínicas. En referencia a HRP, se utilizaron glucosa oxidasa y glucosa para tratar WPI y SKMP, se seleccionaron la utilización adecuada de HRP, glucosa oxidasa y glucosa, además del tiempo de reacción de las pruebas de factor único basadas en los contenidos relativos de ditirosina de los productos modificados. Después, la HRP seleccionada y el H 2 O 2 calculado se utilizaron para tratar WPI y SKMP. El análisis electroforético demostró que los productos modificados contenían algunas proteínas reticuladas con un mayor peso molecular. Otros análisis mostraron que los productos modificados tenían más estructuras secundarias ordenadas, además de una mayor antigenicidad in vitro de lactoalbúmina α y lactoglobulina β que los substratos respectivos. El sistema HRPglucosa oxidasa-glucosa fue más potente que el sistema HRP-H 2 O 2 para mejorar la antigenicidad in vitro de WPI y SKMP. ARTICLE HISTORY

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“…In that case, another substitute or alternative must be provided as cow milk. This substitution results in an allergic disease known as cow milk protein allergy (CMPA) in 2-6% of children [1]. Nowadays, most common alternatives are soy and extensively hydrolyzed milk proteins formulae [1].…”

Section: Introductionmentioning

confidence: 99%

“…This substitution results in an allergic disease known as cow milk protein allergy (CMPA) in 2-6% of children [1]. Nowadays, most common alternatives are soy and extensively hydrolyzed milk proteins formulae [1]. However, there is evidence that 10-20% of children allergic to cow milk do not tolerate soy derivatives [2-4] and some cases of high immunological reaction to extensively hydrolyzed formulae have been reported [5][6][7].…”

Section: Introductionmentioning

confidence: 99%

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2010

Bioinformation

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Nowadays, the quality of any food used for human consumption is, to a considerable extent, considered by its possible contribution to the maintenance or improvement of the consumer's health. In developed countries there is increasing interest in goat milk and its derivates, the quality of which is considered of special importance in the light of current tendencies favouring healthy eating. In particular, goat's milk is a hypoallergenic alternative to cow's milk in the human diet. In the present work, we studied the casein alpha S1 and S2 proteins of cow, goat and sheep for comparative analysis. We found that the amino acid sequence of these proteins is almost same in goat and sheep but there are several changes at different base pairs when these two sequences are compared with cow. Prediction of secondary structures (GOR) was performed for alpha s1 and s2 proteins to gain functional insights. Our in silico study revealed considerable identity in chemical properties between goat and sheep but a considerable dissimilarity in cow with goat and sheep casein proteins. Moreover, the effect amino acid change on secondary structures in the three species is discussed. There was no significant difference found between goat and sheep alpha S1 and S2 proteins, so naturally both will be having same properties. The study concludes that sheep milk is another convenient alternative for the cow milk allergic children.Keywords: casein, alpha proteins, sequence analysis, Background:The best nutritional option for newborn infants is mother's milk; however some infants may not be exclusively breast fed during the first months of life. In that case, another substitute or alternative must be provided as cow milk. This substitution results in an allergic disease known as cow milk protein allergy (CMPA) in 2-6% of children Immunoglobulin E-mediated allergies belong to the most common forms of immunologically mediated forms of hypersensitivity reactions to food [8]. In sensitized individuals dietary intake of food can cause a variety of clinical manifestations reaching from oral allergy syndrome and gastrointestinal symptoms (e.g., vomiting, diarrhoea) to skin, respiratory, and severe systemic manifestations such as anaphylactic shock [9-11]. The development of food allergy shows a typical course [12]. It starts early in childhood mainly against Ags encountered in the initial diet (e.g., cow's milk, eggs) and affects between 4% and 6% of children. Milk is one of the first food components introduced into the diet and therefore represents one of the most important food allergen sources in terms of frequency and severity of allergic manifestations [13 -16]. The symptoms of cow's milk allergy are due to IgE-mediated activation of mast cells and basophils as well as activation of allergen-specific T cells, and they comprise a plethora of gastrointestinal, skin, respiratory, and severe systemic manifestations such as death due to anaphylactic shock. Unlike in respiratory allergy, which proceeds untreated from mild (e.g., rhinoconjuncti...

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The challenge of cow milk protein allergy

Cited by 253 publications

References 57 publications

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity

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