Effect of heat treatment on milk and egg proteins allergenicity

Background Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE‐epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk‐ or egg‐allergic chi...

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Published inPediatric allergy and immunology Vol. 25; no. 8; pp. 740 - 746
Main Authors Bloom, Katherine A., Huang, Faith R., Bencharitiwong, Ramon, Bardina, Luda, Ross, Andrew, Sampson, Hugh A., Nowak‐Węgrzyn, Anna
Format Journal Article
LanguageEnglish
Published England Wiley Subscription Services, Inc 01.12.2014
Subjects
Online AccessGet full text
ISSN0905-6157
1399-3038
1399-3038
DOI10.1111/pai.12283

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Abstract Background Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE‐epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk‐ or egg‐allergic children are tolerant to these foods in their baked forms. We sought to explore the effects of heating on milk and egg proteins and to evaluate for differences in immunolabeling among children with regard to reactivity to heated milk or egg. Methods Sera from participants in clinical dietary intervention trials were utilized. Milk and egg samples were variably heated and prepared (at times within a wheat matrix). Sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis (PAGE), protein transfer, and Western blot were completed. Results Sera from 20 milk‐allergic and 24 egg‐allergic children were utilized. Gel electrophoresis showed strongly staining casein bands that persisted for up to 60 min of heating. In contrast, β‐lactoglobulin and α‐lactalbumin bands became progressiv‐ely weaker with increasing heating times, with no detectable β‐lactoglobulin after 15–20 min of heating. The ovalbumin band became progressively weaker, whereas ovomucoid remained stable after 25 min of heating. Immunolabeling revealed that all heated milk‐reactive children possessed IgE antibodies that bound the casein fraction regardless of heating time. Presence of wheat during heating resulted in decreased IgE antibody binding to milk and egg white proteins. Conclusion Heating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.
AbstractList Background Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE‐epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk‐ or egg‐allergic children are tolerant to these foods in their baked forms. We sought to explore the effects of heating on milk and egg proteins and to evaluate for differences in immunolabeling among children with regard to reactivity to heated milk or egg. Methods Sera from participants in clinical dietary intervention trials were utilized. Milk and egg samples were variably heated and prepared (at times within a wheat matrix). Sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis (PAGE), protein transfer, and Western blot were completed. Results Sera from 20 milk‐allergic and 24 egg‐allergic children were utilized. Gel electrophoresis showed strongly staining casein bands that persisted for up to 60 min of heating. In contrast, β‐lactoglobulin and α‐lactalbumin bands became progressiv‐ely weaker with increasing heating times, with no detectable β‐lactoglobulin after 15–20 min of heating. The ovalbumin band became progressively weaker, whereas ovomucoid remained stable after 25 min of heating. Immunolabeling revealed that all heated milk‐reactive children possessed IgE antibodies that bound the casein fraction regardless of heating time. Presence of wheat during heating resulted in decreased IgE antibody binding to milk and egg white proteins. Conclusion Heating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.
Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE-epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk- or egg-allergic children are tolerant to these foods in their baked forms. We sought to explore the effects of heating on milk and egg proteins and to evaluate for differences in immunolabeling among children with regard to reactivity to heated milk or egg. Sera from participants in clinical dietary intervention trials were utilized. Milk and egg samples were variably heated and prepared (at times within a wheat matrix). Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), protein transfer, and Western blot were completed. Sera from 20 milk-allergic and 24 egg-allergic children were utilized. Gel electrophoresis showed strongly staining casein bands that persisted for up to 60 min of heating. In contrast, β-lactoglobulin and α-lactalbumin bands became progressively weaker with increasing heating times, with no detectable β-lactoglobulin after 15-20 min of heating. The ovalbumin band became progressively weaker, whereas ovomucoid remained stable after 25 min of heating. Immunolabeling revealed that all heated milk-reactive children possessed IgE antibodies that bound the casein fraction regardless of heating time. Presence of wheat during heating resulted in decreased IgE antibody binding to milk and egg white proteins. Heating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.
Background Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE-epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk- or egg-allergic children are tolerant to these foods in their baked forms. We sought to explore the effects of heating on milk and egg proteins and to evaluate for differences in immunolabeling among children with regard to reactivity to heated milk or egg. Methods Sera from participants in clinical dietary intervention trials were utilized. Milk and egg samples were variably heated and prepared (at times within a wheat matrix). Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), protein transfer, and Western blot were completed. Results Sera from 20 milk-allergic and 24 egg-allergic children were utilized. Gel electrophoresis showed strongly staining casein bands that persisted for up to 60 min of heating. In contrast, beta -lactoglobulin and alpha -lactalbumin bands became progressiv-ely weaker with increasing heating times, with no detectable beta -lactoglobulin after 15-20 min of heating. The ovalbumin band became progressively weaker, whereas ovomucoid remained stable after 25 min of heating. Immunolabeling revealed that all heated milk-reactive children possessed IgE antibodies that bound the casein fraction regardless of heating time. Presence of wheat during heating resulted in decreased IgE antibody binding to milk and egg white proteins. Conclusion Heating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.
Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE-epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk- or egg-allergic children are tolerant to these foods in their baked forms. We sought to explore the effects of heating on milk and egg proteins and to evaluate for differences in immunolabeling among children with regard to reactivity to heated milk or egg.BACKGROUNDHeating destroys many conformational epitopes and reduces allergenicity of some foods. IgE-epitope binding has been shown to be different among patients who outgrew their cow's milk or hen's egg allergy and those who did not. A significant proportion of milk- or egg-allergic children are tolerant to these foods in their baked forms. We sought to explore the effects of heating on milk and egg proteins and to evaluate for differences in immunolabeling among children with regard to reactivity to heated milk or egg.Sera from participants in clinical dietary intervention trials were utilized. Milk and egg samples were variably heated and prepared (at times within a wheat matrix). Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), protein transfer, and Western blot were completed.METHODSSera from participants in clinical dietary intervention trials were utilized. Milk and egg samples were variably heated and prepared (at times within a wheat matrix). Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), protein transfer, and Western blot were completed.Sera from 20 milk-allergic and 24 egg-allergic children were utilized. Gel electrophoresis showed strongly staining casein bands that persisted for up to 60 min of heating. In contrast, β-lactoglobulin and α-lactalbumin bands became progressively weaker with increasing heating times, with no detectable β-lactoglobulin after 15-20 min of heating. The ovalbumin band became progressively weaker, whereas ovomucoid remained stable after 25 min of heating. Immunolabeling revealed that all heated milk-reactive children possessed IgE antibodies that bound the casein fraction regardless of heating time. Presence of wheat during heating resulted in decreased IgE antibody binding to milk and egg white proteins.RESULTSSera from 20 milk-allergic and 24 egg-allergic children were utilized. Gel electrophoresis showed strongly staining casein bands that persisted for up to 60 min of heating. In contrast, β-lactoglobulin and α-lactalbumin bands became progressively weaker with increasing heating times, with no detectable β-lactoglobulin after 15-20 min of heating. The ovalbumin band became progressively weaker, whereas ovomucoid remained stable after 25 min of heating. Immunolabeling revealed that all heated milk-reactive children possessed IgE antibodies that bound the casein fraction regardless of heating time. Presence of wheat during heating resulted in decreased IgE antibody binding to milk and egg white proteins.Heating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.CONCLUSIONHeating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.
Author Ross, Andrew
Bloom, Katherine A.
Bencharitiwong, Ramon
Huang, Faith R.
Sampson, Hugh A.
Bardina, Luda
Nowak‐Węgrzyn, Anna
Author_xml – sequence: 1
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  surname: Bloom
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  organization: Icahn School of Medicine at Mount Sinai
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  fullname: Huang, Faith R.
  organization: Icahn School of Medicine at Mount Sinai
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  surname: Bencharitiwong
  fullname: Bencharitiwong, Ramon
  organization: Icahn School of Medicine at Mount Sinai
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  surname: Bardina
  fullname: Bardina, Luda
  organization: Icahn School of Medicine at Mount Sinai
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  givenname: Andrew
  surname: Ross
  fullname: Ross, Andrew
  organization: Icahn School of Medicine at Mount Sinai
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  fullname: Sampson, Hugh A.
  organization: Icahn School of Medicine at Mount Sinai
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  surname: Nowak‐Węgrzyn
  fullname: Nowak‐Węgrzyn, Anna
  organization: Icahn School of Medicine at Mount Sinai
BackLink https://www.ncbi.nlm.nih.gov/pubmed/25251921$$D View this record in MEDLINE/PubMed
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Copyright 2014 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd
2014 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.
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Issue 8
Keywords baked egg
baked milk
egg allergy
food allergy
milk allergy
Language English
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2014 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.
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Snippet Background Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE‐epitope binding has been shown to be different among...
Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE-epitope binding has been shown to be different among patients who...
Background Heating destroys many conformational epitopes and reduces allergenicity of some foods. IgE-epitope binding has been shown to be different among...
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SubjectTerms Adolescent
Allergens - immunology
Animals
baked egg
baked milk
Caseins - chemistry
Caseins - immunology
Cattle
Child
Child, Preschool
egg allergy
Egg Hypersensitivity - immunology
Egg Proteins - chemistry
Egg Proteins - immunology
Female
food allergy
Hot Temperature - adverse effects
Humans
Immunodominant Epitopes - immunology
Male
Milk - chemistry
Milk - immunology
milk allergy
Milk Hypersensitivity - immunology
Ovum - chemistry
Ovum - immunology
Protein Conformation
Triticum aestivum
Title Effect of heat treatment on milk and egg proteins allergenicity
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