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 in | Pediatric allergy and immunology Vol. 25; no. 8; pp. 740 - 746 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Wiley Subscription Services, Inc
01.12.2014
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Subjects | |
Online Access | Get full text |
ISSN | 0905-6157 1399-3038 1399-3038 |
DOI | 10.1111/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. |
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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 givenname: Katherine A. surname: Bloom fullname: Bloom, Katherine A. organization: Icahn School of Medicine at Mount Sinai – sequence: 2 givenname: Faith R. surname: Huang fullname: Huang, Faith R. organization: Icahn School of Medicine at Mount Sinai – sequence: 3 givenname: Ramon surname: Bencharitiwong fullname: Bencharitiwong, Ramon organization: Icahn School of Medicine at Mount Sinai – sequence: 4 givenname: Luda surname: Bardina fullname: Bardina, Luda organization: Icahn School of Medicine at Mount Sinai – sequence: 5 givenname: Andrew surname: Ross fullname: Ross, Andrew organization: Icahn School of Medicine at Mount Sinai – sequence: 6 givenname: Hugh A. surname: Sampson fullname: Sampson, Hugh A. organization: Icahn School of Medicine at Mount Sinai – sequence: 7 givenname: Anna 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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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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