Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein
Kiwifruit is a significant elicitor of allergy both in children and adults. Digestibility of two kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), was assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of fo...
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| Veröffentlicht in: | Molecular nutrition & food research 2008-10, Vol.52 (10), p.1130-1139 |
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| creator | Bublin, Merima Radauer, Christian Knulst, André Wagner, Stefan Scheiner, Otto Mackie, Alan R Mills, E.N. Clare Breiteneder, Heimo |
| description | Kiwifruit is a significant elicitor of allergy both in children and adults. Digestibility of two kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), was assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum. Act d 1 precipitated in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeded slowly. The residual precipitate redissolved completely in simulated duodenal fluid at pH 6.5 and was partially digested. Forty percent of Act d 2 remained intact during gastric digestion and were cleaved by duodenal proteases into large fragments covalently linked by disulfide bonds. Both digested allergen samples displayed nearly unchanged IgE binding abilities. Circular dichroism spectra were used to analyze heat and acid-induced unfolding. Thermal stability of both allergens was strongly pH dependent. While Act d 1 was irreversibly destabilized in acidic solutions, heat-induced denaturation of Act d 2 at pH 2 was fully reversible. IgE binding to Act d 2 but not Act d 1 was detected in processed food products. The stability of Act d 1 and Act d 2 provides one explanation for the allergenic potency of kiwifruit. |
| doi_str_mv | 10.1002/mnfr.200700167 |
| format | Article |
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Both digested allergen samples displayed nearly unchanged IgE binding abilities. Circular dichroism spectra were used to analyze heat and acid-induced unfolding. Thermal stability of both allergens was strongly pH dependent. While Act d 1 was irreversibly destabilized in acidic solutions, heat-induced denaturation of Act d 2 at pH 2 was fully reversible. IgE binding to Act d 2 but not Act d 1 was detected in processed food products. The stability of Act d 1 and Act d 2 provides one explanation for the allergenic potency of kiwifruit.</description><identifier>ISSN: 1613-4125</identifier><identifier>EISSN: 1613-4133</identifier><identifier>EISSN: 1521-3803</identifier><identifier>DOI: 10.1002/mnfr.200700167</identifier><identifier>PMID: 18655003</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>Actinidia - adverse effects ; Actinidia - chemistry ; Actinidia - immunology ; Actinidin ; Allergen ; Allergens - immunology ; Allergens - metabolism ; Antigens, Plant - immunology ; Antigens, Plant - metabolism ; Biological and medical sciences ; Circular Dichroism ; Cysteine Endopeptidases - immunology ; Cysteine Endopeptidases - metabolism ; Digestion ; Food allergy ; Food Hypersensitivity - immunology ; Food Hypersensitivity - metabolism ; Food industries ; Fruit and vegetable industries ; Fundamental and applied biological sciences. 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Clare</creatorcontrib><creatorcontrib>Breiteneder, Heimo</creatorcontrib><title>Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein</title><title>Molecular nutrition & food research</title><addtitle>Mol. Nutr. Food Res</addtitle><description>Kiwifruit is a significant elicitor of allergy both in children and adults. Digestibility of two kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), was assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum. Act d 1 precipitated in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeded slowly. The residual precipitate redissolved completely in simulated duodenal fluid at pH 6.5 and was partially digested. Forty percent of Act d 2 remained intact during gastric digestion and were cleaved by duodenal proteases into large fragments covalently linked by disulfide bonds. Both digested allergen samples displayed nearly unchanged IgE binding abilities. Circular dichroism spectra were used to analyze heat and acid-induced unfolding. Thermal stability of both allergens was strongly pH dependent. While Act d 1 was irreversibly destabilized in acidic solutions, heat-induced denaturation of Act d 2 at pH 2 was fully reversible. IgE binding to Act d 2 but not Act d 1 was detected in processed food products. The stability of Act d 1 and Act d 2 provides one explanation for the allergenic potency of kiwifruit.</description><subject>Actinidia - adverse effects</subject><subject>Actinidia - chemistry</subject><subject>Actinidia - immunology</subject><subject>Actinidin</subject><subject>Allergen</subject><subject>Allergens - immunology</subject><subject>Allergens - metabolism</subject><subject>Antigens, Plant - immunology</subject><subject>Antigens, Plant - metabolism</subject><subject>Biological and medical sciences</subject><subject>Circular Dichroism</subject><subject>Cysteine Endopeptidases - immunology</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Digestion</subject><subject>Food allergy</subject><subject>Food Hypersensitivity - immunology</subject><subject>Food Hypersensitivity - metabolism</subject><subject>Food industries</subject><subject>Fruit and vegetable industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kiwifruit</subject><subject>Methods of analysis, processing and quality control, regulation, standards</subject><subject>Plant Proteins - immunology</subject><subject>Plant Proteins - metabolism</subject><subject>Thaumatin-like protein</subject><issn>1613-4125</issn><issn>1613-4133</issn><issn>1521-3803</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhiMEoqVw5Qi-wKlZxnbs7B6rVVtQlyIBFUdr4tip2cRp7azK_hF-Lw5ZBW49eT6ed2Y8k2WvKSwoAPvQeRsWDKAEoLJ8kh1TSXleUM6fzjYTR9mLGH8CcMoK_jw7okspRHKPs9_n1ho9RNJb0mAcQu_8YOLgPLakds1o9p6gr8mtwRRuSHKHW0OwbU1ojHfaDftRPga37sHNmUjO9EBqQk8J6iR1tfOnf0tNcZacpMJdNxbOW7c15C70g3H-ZfbMYhvNq8N7kt1cnH9ff8w3Xy4_rc82uRaclblkS86QWWMoLUpua2ZELa2lpioRKLNpEYBMcss01iWnFa_salkVghUAheQn2fupbup7v0ufVZ2L2rQtetPvopIrKUpJl4-CDGQhCgYJXEygDn2MwVh1F1yHYa8oqPFkajyZmk-WBG8OlXdVZ-p_-OFGCXh3ADBqbG1Ar12cOQalWAkYR1xN3INrzf6Rturz9cXX_4fIJ62Lg_k1azFsVcqWQv24vlQlY-JqLa_UJvFvJ95ir7AJaZ6bbwzStqkQVC6B_wEmA8fv</recordid><startdate>200810</startdate><enddate>200810</enddate><creator>Bublin, Merima</creator><creator>Radauer, Christian</creator><creator>Knulst, André</creator><creator>Wagner, Stefan</creator><creator>Scheiner, Otto</creator><creator>Mackie, Alan R</creator><creator>Mills, E.N. Clare</creator><creator>Breiteneder, Heimo</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley-VCH-Verl</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>200810</creationdate><title>Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein</title><author>Bublin, Merima ; Radauer, Christian ; Knulst, André ; Wagner, Stefan ; Scheiner, Otto ; Mackie, Alan R ; Mills, E.N. Clare ; Breiteneder, Heimo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5327-62832a2fee11473fd2e5d6ff1eb7a012f4130a263f2cad731b3bf98b452400463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Actinidia - adverse effects</topic><topic>Actinidia - chemistry</topic><topic>Actinidia - immunology</topic><topic>Actinidin</topic><topic>Allergen</topic><topic>Allergens - immunology</topic><topic>Allergens - metabolism</topic><topic>Antigens, Plant - immunology</topic><topic>Antigens, Plant - metabolism</topic><topic>Biological and medical sciences</topic><topic>Circular Dichroism</topic><topic>Cysteine Endopeptidases - immunology</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>Digestion</topic><topic>Food allergy</topic><topic>Food Hypersensitivity - immunology</topic><topic>Food Hypersensitivity - metabolism</topic><topic>Food industries</topic><topic>Fruit and vegetable industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kiwifruit</topic><topic>Methods of analysis, processing and quality control, regulation, standards</topic><topic>Plant Proteins - immunology</topic><topic>Plant Proteins - metabolism</topic><topic>Thaumatin-like protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bublin, Merima</creatorcontrib><creatorcontrib>Radauer, Christian</creatorcontrib><creatorcontrib>Knulst, André</creatorcontrib><creatorcontrib>Wagner, Stefan</creatorcontrib><creatorcontrib>Scheiner, Otto</creatorcontrib><creatorcontrib>Mackie, Alan R</creatorcontrib><creatorcontrib>Mills, E.N. Clare</creatorcontrib><creatorcontrib>Breiteneder, Heimo</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular nutrition & food research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bublin, Merima</au><au>Radauer, Christian</au><au>Knulst, André</au><au>Wagner, Stefan</au><au>Scheiner, Otto</au><au>Mackie, Alan R</au><au>Mills, E.N. Clare</au><au>Breiteneder, Heimo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein</atitle><jtitle>Molecular nutrition & food research</jtitle><addtitle>Mol. Nutr. Food Res</addtitle><date>2008-10</date><risdate>2008</risdate><volume>52</volume><issue>10</issue><spage>1130</spage><epage>1139</epage><pages>1130-1139</pages><issn>1613-4125</issn><eissn>1613-4133</eissn><eissn>1521-3803</eissn><abstract>Kiwifruit is a significant elicitor of allergy both in children and adults. Digestibility of two kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), was assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum. Act d 1 precipitated in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeded slowly. The residual precipitate redissolved completely in simulated duodenal fluid at pH 6.5 and was partially digested. Forty percent of Act d 2 remained intact during gastric digestion and were cleaved by duodenal proteases into large fragments covalently linked by disulfide bonds. Both digested allergen samples displayed nearly unchanged IgE binding abilities. Circular dichroism spectra were used to analyze heat and acid-induced unfolding. Thermal stability of both allergens was strongly pH dependent. While Act d 1 was irreversibly destabilized in acidic solutions, heat-induced denaturation of Act d 2 at pH 2 was fully reversible. IgE binding to Act d 2 but not Act d 1 was detected in processed food products. The stability of Act d 1 and Act d 2 provides one explanation for the allergenic potency of kiwifruit.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>18655003</pmid><doi>10.1002/mnfr.200700167</doi><tpages>10</tpages></addata></record> |
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| ispartof | Molecular nutrition & food research, 2008-10, Vol.52 (10), p.1130-1139 |
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| subjects | Actinidia - adverse effects Actinidia - chemistry Actinidia - immunology Actinidin Allergen Allergens - immunology Allergens - metabolism Antigens, Plant - immunology Antigens, Plant - metabolism Biological and medical sciences Circular Dichroism Cysteine Endopeptidases - immunology Cysteine Endopeptidases - metabolism Digestion Food allergy Food Hypersensitivity - immunology Food Hypersensitivity - metabolism Food industries Fruit and vegetable industries Fundamental and applied biological sciences. Psychology General aspects Hot Temperature Humans Hydrogen-Ion Concentration Kiwifruit Methods of analysis, processing and quality control, regulation, standards Plant Proteins - immunology Plant Proteins - metabolism Thaumatin-like protein |
| title | Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein |
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