Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid
BACKGROUND Ovomucoid (OVM) is the dominant allergen found in egg white. The heat‐induced changes on chicken OVM structure and antigenic properties were assessed at acidic, neutral and alkaline pH values. RESULTS The fluorescence spectroscopy measurements indicated changes in the conformation of OVM...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2018-06, Vol.98 (8), p.3119-3128 |
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| creator | Stănciuc, Nicoleta Creţu, Alexandra Andreea Banu, Iuliana Aprodu, Iuliana |
| description | BACKGROUND
Ovomucoid (OVM) is the dominant allergen found in egg white. The heat‐induced changes on chicken OVM structure and antigenic properties were assessed at acidic, neutral and alkaline pH values.
RESULTS
The fluorescence spectroscopy measurements indicated changes in the conformation of OVM caused by both pH and thermal treatment. The OVM molecule exhibited higher exposure of hydrophobic residues at 7.0, as indicated by the synchronous spectra, intrinsic fluorescence and quenching experiments. When heating the protein at pH 9.5, the molecular structure appeared more compact. The antigenic properties of OVM, estimated through the enzyme‐linked immunosorbent assay, appeared not to be sensitive to heat at pH 7.0 and 4.5. Single molecule level investigations indicated that the secondary and tertiary structure of OVM was affected by the thermal treatment.
CONCLUSIONS
Experimental results indicated over 90% reduction of the antigenicity at pH 9.5 and temperature of 100 °C. Significant changes of the linear epitopes exposure and location of the conformational epitopes were highlighted after performing heating molecular dynamics simulations of OVM from 25 °C to 100 °C. © 2017 Society of Chemical Industry |
| doi_str_mv | 10.1002/jsfa.8813 |
| format | Article |
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Ovomucoid (OVM) is the dominant allergen found in egg white. The heat‐induced changes on chicken OVM structure and antigenic properties were assessed at acidic, neutral and alkaline pH values.
RESULTS
The fluorescence spectroscopy measurements indicated changes in the conformation of OVM caused by both pH and thermal treatment. The OVM molecule exhibited higher exposure of hydrophobic residues at 7.0, as indicated by the synchronous spectra, intrinsic fluorescence and quenching experiments. When heating the protein at pH 9.5, the molecular structure appeared more compact. The antigenic properties of OVM, estimated through the enzyme‐linked immunosorbent assay, appeared not to be sensitive to heat at pH 7.0 and 4.5. Single molecule level investigations indicated that the secondary and tertiary structure of OVM was affected by the thermal treatment.
CONCLUSIONS
Experimental results indicated over 90% reduction of the antigenicity at pH 9.5 and temperature of 100 °C. Significant changes of the linear epitopes exposure and location of the conformational epitopes were highlighted after performing heating molecular dynamics simulations of OVM from 25 °C to 100 °C. © 2017 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.8813</identifier><identifier>PMID: 29210457</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Albumen ; Allergens ; antigenic properties ; Antigenicity ; Antigens ; Epitopes ; Exposure ; Fluorescence ; Fluorescence spectroscopy ; Heat treatment ; Heating ; Hydrophobicity ; Molecular chains ; Molecular dynamics ; Molecular structure ; ovomucoid ; pH effects ; Protein structure ; Spectrum analysis ; structural changes ; Tertiary structure</subject><ispartof>Journal of the science of food and agriculture, 2018-06, Vol.98 (8), p.3119-3128</ispartof><rights>2017 Society of Chemical Industry</rights><rights>2017 Society of Chemical Industry.</rights><rights>2018 Society of Chemical Industry</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4193-1bb9f0b10b6be24d7817f551fdcea0407918dce430c59ca38d8511ed95e58db03</citedby><cites>FETCH-LOGICAL-c4193-1bb9f0b10b6be24d7817f551fdcea0407918dce430c59ca38d8511ed95e58db03</cites><orcidid>0000-0003-2215-6826</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.8813$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.8813$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29210457$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stănciuc, Nicoleta</creatorcontrib><creatorcontrib>Creţu, Alexandra Andreea</creatorcontrib><creatorcontrib>Banu, Iuliana</creatorcontrib><creatorcontrib>Aprodu, Iuliana</creatorcontrib><title>Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>BACKGROUND
Ovomucoid (OVM) is the dominant allergen found in egg white. The heat‐induced changes on chicken OVM structure and antigenic properties were assessed at acidic, neutral and alkaline pH values.
RESULTS
The fluorescence spectroscopy measurements indicated changes in the conformation of OVM caused by both pH and thermal treatment. The OVM molecule exhibited higher exposure of hydrophobic residues at 7.0, as indicated by the synchronous spectra, intrinsic fluorescence and quenching experiments. When heating the protein at pH 9.5, the molecular structure appeared more compact. The antigenic properties of OVM, estimated through the enzyme‐linked immunosorbent assay, appeared not to be sensitive to heat at pH 7.0 and 4.5. Single molecule level investigations indicated that the secondary and tertiary structure of OVM was affected by the thermal treatment.
CONCLUSIONS
Experimental results indicated over 90% reduction of the antigenicity at pH 9.5 and temperature of 100 °C. Significant changes of the linear epitopes exposure and location of the conformational epitopes were highlighted after performing heating molecular dynamics simulations of OVM from 25 °C to 100 °C. © 2017 Society of Chemical Industry</description><subject>Albumen</subject><subject>Allergens</subject><subject>antigenic properties</subject><subject>Antigenicity</subject><subject>Antigens</subject><subject>Epitopes</subject><subject>Exposure</subject><subject>Fluorescence</subject><subject>Fluorescence spectroscopy</subject><subject>Heat treatment</subject><subject>Heating</subject><subject>Hydrophobicity</subject><subject>Molecular chains</subject><subject>Molecular dynamics</subject><subject>Molecular structure</subject><subject>ovomucoid</subject><subject>pH effects</subject><subject>Protein structure</subject><subject>Spectrum analysis</subject><subject>structural changes</subject><subject>Tertiary structure</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kEFP3DAQha2qFbssHPoHUKReyiEwk8SJfVyhLgWtxIFythzbYb1N4sVOttp_j9OFHpB6GM2M5punp0fIV4QrBMiut6GRV4xh_onMEXiVAiB8JvN4y1KKRTYjpyFsAYDzsjwhs4xnCAWt5kQs9V72yoTE9cmwMYntdlINiWumzXeyTXbexXuw_fPEhMGPahi9SWSvYw322fRW2eEw_aiNVb9Nn7i960blrD4jXxrZBnP-1hfkafXj183PdP1we3ezXKeqQJ6nWNe8gRqhLmuTFbpiWDWUYqOVkVBAxZHFschBUa5kzjSjiEZzaijTNeQL8v2oG92-jCYMorNBmbaVvXFjEMirvCihyjCi3z6gWzf6ProTGeS0LAtWsUhdHinlXQjeNGLnbSf9QSCIKXUxpS6m1CN78aY41p3R_8j3mCNwfQT-2NYc_q8k7h9Xy7-SrxqKjIU</recordid><startdate>201806</startdate><enddate>201806</enddate><creator>Stănciuc, Nicoleta</creator><creator>Creţu, Alexandra Andreea</creator><creator>Banu, Iuliana</creator><creator>Aprodu, Iuliana</creator><general>John Wiley & Sons, Ltd</general><general>John Wiley and Sons, Limited</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-2215-6826</orcidid></search><sort><creationdate>201806</creationdate><title>Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid</title><author>Stănciuc, Nicoleta ; Creţu, Alexandra Andreea ; Banu, Iuliana ; Aprodu, Iuliana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4193-1bb9f0b10b6be24d7817f551fdcea0407918dce430c59ca38d8511ed95e58db03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Albumen</topic><topic>Allergens</topic><topic>antigenic properties</topic><topic>Antigenicity</topic><topic>Antigens</topic><topic>Epitopes</topic><topic>Exposure</topic><topic>Fluorescence</topic><topic>Fluorescence spectroscopy</topic><topic>Heat treatment</topic><topic>Heating</topic><topic>Hydrophobicity</topic><topic>Molecular chains</topic><topic>Molecular dynamics</topic><topic>Molecular structure</topic><topic>ovomucoid</topic><topic>pH effects</topic><topic>Protein structure</topic><topic>Spectrum analysis</topic><topic>structural changes</topic><topic>Tertiary structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stănciuc, Nicoleta</creatorcontrib><creatorcontrib>Creţu, Alexandra Andreea</creatorcontrib><creatorcontrib>Banu, Iuliana</creatorcontrib><creatorcontrib>Aprodu, Iuliana</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stănciuc, Nicoleta</au><au>Creţu, Alexandra Andreea</au><au>Banu, Iuliana</au><au>Aprodu, Iuliana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J Sci Food Agric</addtitle><date>2018-06</date><risdate>2018</risdate><volume>98</volume><issue>8</issue><spage>3119</spage><epage>3128</epage><pages>3119-3128</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><abstract>BACKGROUND
Ovomucoid (OVM) is the dominant allergen found in egg white. The heat‐induced changes on chicken OVM structure and antigenic properties were assessed at acidic, neutral and alkaline pH values.
RESULTS
The fluorescence spectroscopy measurements indicated changes in the conformation of OVM caused by both pH and thermal treatment. The OVM molecule exhibited higher exposure of hydrophobic residues at 7.0, as indicated by the synchronous spectra, intrinsic fluorescence and quenching experiments. When heating the protein at pH 9.5, the molecular structure appeared more compact. The antigenic properties of OVM, estimated through the enzyme‐linked immunosorbent assay, appeared not to be sensitive to heat at pH 7.0 and 4.5. Single molecule level investigations indicated that the secondary and tertiary structure of OVM was affected by the thermal treatment.
CONCLUSIONS
Experimental results indicated over 90% reduction of the antigenicity at pH 9.5 and temperature of 100 °C. Significant changes of the linear epitopes exposure and location of the conformational epitopes were highlighted after performing heating molecular dynamics simulations of OVM from 25 °C to 100 °C. © 2017 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>29210457</pmid><doi>10.1002/jsfa.8813</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-2215-6826</orcidid></addata></record> |
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Albumen Allergens antigenic properties Antigenicity Antigens Epitopes Exposure Fluorescence Fluorescence spectroscopy Heat treatment Heating Hydrophobicity Molecular chains Molecular dynamics Molecular structure ovomucoid pH effects Protein structure Spectrum analysis structural changes Tertiary structure |
| title | Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid |
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