Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols
•The covalent interaction between the polyphenols and β-lactoglobulin was investigated.•The allergenicity of β-lactoglobulin was reduced after covalent conjugation with polyphenols.•The functional attributes of β-lactoglobulin were extended after covalent conjugation with polyphenols. To help produc...
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| Veröffentlicht in: | Food chemistry 2018-08, Vol.256, p.427-434 |
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| creator | Wu, Xuli Lu, Yuqin Xu, Haoxie Lin, Dongxu He, Zhendan Wu, Haiqiang Liu, Lizhong Wang, Zimei |
| description | •The covalent interaction between the polyphenols and β-lactoglobulin was investigated.•The allergenicity of β-lactoglobulin was reduced after covalent conjugation with polyphenols.•The functional attributes of β-lactoglobulin were extended after covalent conjugation with polyphenols.
To help produce hypoallergenic food, this study investigated reducing the allergenicity and improving the functional properties of bovine β-lactoglobulin (βLG) by covalent conjugation with (−)-epigallo-catechin 3-gallate (EGCG) and chlorogenic acid (CA). The covalent bond between the polyphenols and the amino acid side-chains in βLG was confirmed by MALDI-TOF-MS and SDS-PAGE. Structural analysis by fluorescence spectroscopy, circular dichroism (CD) and Fourier transform infrared (FTIR) indicated that the covalent conjugate of EGCG and CA led to the changed protein structure of βLG. Western blot analysis and enzyme-linked immunosorbent assay indicated that conjugation of βLG with these polyphenols was effective in reducing the IgE-binding capacity of βLG. The conjugates maintained the retinol-binding activity without denaturation the protein and enhanced the thermal stability with high antioxidant activity. The study provides an innovative approach to producing hypoallergenic food. |
| doi_str_mv | 10.1016/j.foodchem.2018.02.158 |
| format | Article |
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To help produce hypoallergenic food, this study investigated reducing the allergenicity and improving the functional properties of bovine β-lactoglobulin (βLG) by covalent conjugation with (−)-epigallo-catechin 3-gallate (EGCG) and chlorogenic acid (CA). The covalent bond between the polyphenols and the amino acid side-chains in βLG was confirmed by MALDI-TOF-MS and SDS-PAGE. Structural analysis by fluorescence spectroscopy, circular dichroism (CD) and Fourier transform infrared (FTIR) indicated that the covalent conjugate of EGCG and CA led to the changed protein structure of βLG. Western blot analysis and enzyme-linked immunosorbent assay indicated that conjugation of βLG with these polyphenols was effective in reducing the IgE-binding capacity of βLG. The conjugates maintained the retinol-binding activity without denaturation the protein and enhanced the thermal stability with high antioxidant activity. The study provides an innovative approach to producing hypoallergenic food.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2018.02.158</identifier><identifier>PMID: 29606470</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Allergenicity ; Antioxidant activity ; Conjugation ; Polyphenol ; β-lactoglobulin</subject><ispartof>Food chemistry, 2018-08, Vol.256, p.427-434</ispartof><rights>2018 Elsevier Ltd</rights><rights>Copyright © 2018 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-ed8120332da47e7feafdab6734fc4078e7a44d910598aecda7215b6d976d979f3</citedby><cites>FETCH-LOGICAL-c368t-ed8120332da47e7feafdab6734fc4078e7a44d910598aecda7215b6d976d979f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2018.02.158$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29606470$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, Xuli</creatorcontrib><creatorcontrib>Lu, Yuqin</creatorcontrib><creatorcontrib>Xu, Haoxie</creatorcontrib><creatorcontrib>Lin, Dongxu</creatorcontrib><creatorcontrib>He, Zhendan</creatorcontrib><creatorcontrib>Wu, Haiqiang</creatorcontrib><creatorcontrib>Liu, Lizhong</creatorcontrib><creatorcontrib>Wang, Zimei</creatorcontrib><title>Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•The covalent interaction between the polyphenols and β-lactoglobulin was investigated.•The allergenicity of β-lactoglobulin was reduced after covalent conjugation with polyphenols.•The functional attributes of β-lactoglobulin were extended after covalent conjugation with polyphenols.
To help produce hypoallergenic food, this study investigated reducing the allergenicity and improving the functional properties of bovine β-lactoglobulin (βLG) by covalent conjugation with (−)-epigallo-catechin 3-gallate (EGCG) and chlorogenic acid (CA). The covalent bond between the polyphenols and the amino acid side-chains in βLG was confirmed by MALDI-TOF-MS and SDS-PAGE. Structural analysis by fluorescence spectroscopy, circular dichroism (CD) and Fourier transform infrared (FTIR) indicated that the covalent conjugate of EGCG and CA led to the changed protein structure of βLG. Western blot analysis and enzyme-linked immunosorbent assay indicated that conjugation of βLG with these polyphenols was effective in reducing the IgE-binding capacity of βLG. The conjugates maintained the retinol-binding activity without denaturation the protein and enhanced the thermal stability with high antioxidant activity. The study provides an innovative approach to producing hypoallergenic food.</description><subject>Allergenicity</subject><subject>Antioxidant activity</subject><subject>Conjugation</subject><subject>Polyphenol</subject><subject>β-lactoglobulin</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFkM1q3DAQgEVJSbZJXiHomIvdkey15FtLyB8ECqU5C1ka72rRSq4lJ-xr9UH6TLHZpNcehpnDN38fIVcMSgas-bor-xit2eK-5MBkCbxka_mJrJgUVSFA8BOyggpkIVndnJEvKe0AYGFPyRlvG2hqASuCP9FOxoUNzVuk2nscNxicoUYP2rh8oLGnf_8UXpscNz52k3eBdgdq4ov2GPJchN200dnFQF9d3lLrMOvxQIfoD8MWQ_TpgnzutU94-Z7PyfPd7a-bh-Lpx_3jzfenwlSNzAVayThUFbe6Fih61L3VXSOqujc1CIlC17VtGaxbqdFYLThbd41txRJtX52T6-PcYYy_J0xZ7V0y6L0OGKek-CxAtouiGW2OqBljSiP2ahjdfr5bMVCLYrVTH4rVok0BV7PiufHqfcfU7dH-a_twOgPfjgDOn744HFUyDoNB60Y0Wdno_rfjDQqMk5o</recordid><startdate>20180801</startdate><enddate>20180801</enddate><creator>Wu, Xuli</creator><creator>Lu, Yuqin</creator><creator>Xu, Haoxie</creator><creator>Lin, Dongxu</creator><creator>He, Zhendan</creator><creator>Wu, Haiqiang</creator><creator>Liu, Lizhong</creator><creator>Wang, Zimei</creator><general>Elsevier Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20180801</creationdate><title>Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols</title><author>Wu, Xuli ; Lu, Yuqin ; Xu, Haoxie ; Lin, Dongxu ; He, Zhendan ; Wu, Haiqiang ; Liu, Lizhong ; Wang, Zimei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-ed8120332da47e7feafdab6734fc4078e7a44d910598aecda7215b6d976d979f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Allergenicity</topic><topic>Antioxidant activity</topic><topic>Conjugation</topic><topic>Polyphenol</topic><topic>β-lactoglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Xuli</creatorcontrib><creatorcontrib>Lu, Yuqin</creatorcontrib><creatorcontrib>Xu, Haoxie</creatorcontrib><creatorcontrib>Lin, Dongxu</creatorcontrib><creatorcontrib>He, Zhendan</creatorcontrib><creatorcontrib>Wu, Haiqiang</creatorcontrib><creatorcontrib>Liu, Lizhong</creatorcontrib><creatorcontrib>Wang, Zimei</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Xuli</au><au>Lu, Yuqin</au><au>Xu, Haoxie</au><au>Lin, Dongxu</au><au>He, Zhendan</au><au>Wu, Haiqiang</au><au>Liu, Lizhong</au><au>Wang, Zimei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2018-08-01</date><risdate>2018</risdate><volume>256</volume><spage>427</spage><epage>434</epage><pages>427-434</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•The covalent interaction between the polyphenols and β-lactoglobulin was investigated.•The allergenicity of β-lactoglobulin was reduced after covalent conjugation with polyphenols.•The functional attributes of β-lactoglobulin were extended after covalent conjugation with polyphenols.
To help produce hypoallergenic food, this study investigated reducing the allergenicity and improving the functional properties of bovine β-lactoglobulin (βLG) by covalent conjugation with (−)-epigallo-catechin 3-gallate (EGCG) and chlorogenic acid (CA). The covalent bond between the polyphenols and the amino acid side-chains in βLG was confirmed by MALDI-TOF-MS and SDS-PAGE. Structural analysis by fluorescence spectroscopy, circular dichroism (CD) and Fourier transform infrared (FTIR) indicated that the covalent conjugate of EGCG and CA led to the changed protein structure of βLG. Western blot analysis and enzyme-linked immunosorbent assay indicated that conjugation of βLG with these polyphenols was effective in reducing the IgE-binding capacity of βLG. The conjugates maintained the retinol-binding activity without denaturation the protein and enhanced the thermal stability with high antioxidant activity. The study provides an innovative approach to producing hypoallergenic food.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>29606470</pmid><doi>10.1016/j.foodchem.2018.02.158</doi><tpages>8</tpages></addata></record> |
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| subjects | Allergenicity Antioxidant activity Conjugation Polyphenol β-lactoglobulin |
| title | Reducing the allergenic capacity of β-lactoglobulin by covalent conjugation with dietary polyphenols |
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