Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation

Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigat...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Claude, Mathilde [verfasserIn] Lupi, Roberta [verfasserIn] Picariello, Gianluca [verfasserIn] Drouet, Martine [verfasserIn] Larré, Colette [verfasserIn] Denery-Papini, Sandra [verfasserIn] Brossard, Chantal [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	Allergenicity Digestibility Egg allergy Food structure Basophil degranulation

Übergeordnetes Werk:	Enthalten in: Food research international - New York, NY [u.a.] : Elsevier, 1992, 118, Seite 108-114
Übergeordnetes Werk:	volume:118 ; pages:108-114

DOI / URN:	10.1016/j.foodres.2017.11.040

Katalog-ID:	ELV001920243

Internformat


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245	1	0	\|a Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
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520			\|a Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked.
650		4	\|a Allergenicity
650		4	\|a Digestibility
650		4	\|a Egg allergy
650		4	\|a Food structure
650		4	\|a Basophil degranulation
700	1		\|a Lupi, Roberta \|e verfasserin \|4 aut
700	1		\|a Picariello, Gianluca \|e verfasserin \|4 aut
700	1		\|a Drouet, Martine \|e verfasserin \|4 aut
700	1		\|a Larré, Colette \|e verfasserin \|4 aut
700	1		\|a Denery-Papini, Sandra \|e verfasserin \|4 aut
700	1		\|a Brossard, Chantal \|e verfasserin \|0 (orcid)0000-0002-9480-1583 \|4 aut
773	0	8	\|i Enthalten in \|t Food research international \|d New York, NY [u.a.] : Elsevier, 1992 \|g 118, Seite 108-114 \|h Online-Ressource \|w (DE-627)300898541 \|w (DE-600)1483651-8 \|w (DE-576)25526660X \|x 1873-7145 \|7 nnns
773	1	8	\|g volume:118 \|g pages:108-114
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912			\|a GBV_ILN_100
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912			\|a GBV_ILN_105
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912			\|a GBV_ILN_151
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912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
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912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2098
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
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912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
936	b	k	\|a 58.34 \|j Lebensmitteltechnologie
951			\|a AR
952			\|d 118 \|h 108-114

Indexfelder

author_variant	m c mc r l rl g p gp m d md c l cl s d p sdp c b cb
matchkey_str	article:18737145:2017----::ietodfeetyfettebltontvadhralageaeoabm
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publishDate	2017
allfields	10.1016/j.foodres.2017.11.040 doi (DE-627)ELV001920243 (ELSEVIER)S0963-9969(17)30809-8 DE-627 ger DE-627 rda eng 630 640 540 660 DE-600 58.34 bkl Claude, Mathilde verfasserin aut Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation 2017 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked. Allergenicity Digestibility Egg allergy Food structure Basophil degranulation Lupi, Roberta verfasserin aut Picariello, Gianluca verfasserin aut Drouet, Martine verfasserin aut Larré, Colette verfasserin aut Denery-Papini, Sandra verfasserin aut Brossard, Chantal verfasserin (orcid)0000-0002-9480-1583 aut Enthalten in Food research international New York, NY [u.a.] : Elsevier, 1992 118, Seite 108-114 Online-Ressource (DE-627)300898541 (DE-600)1483651-8 (DE-576)25526660X 1873-7145 nnns volume:118 pages:108-114 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2098 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 58.34 Lebensmitteltechnologie AR 118 108-114
spelling	10.1016/j.foodres.2017.11.040 doi (DE-627)ELV001920243 (ELSEVIER)S0963-9969(17)30809-8 DE-627 ger DE-627 rda eng 630 640 540 660 DE-600 58.34 bkl Claude, Mathilde verfasserin aut Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation 2017 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked. Allergenicity Digestibility Egg allergy Food structure Basophil degranulation Lupi, Roberta verfasserin aut Picariello, Gianluca verfasserin aut Drouet, Martine verfasserin aut Larré, Colette verfasserin aut Denery-Papini, Sandra verfasserin aut Brossard, Chantal verfasserin (orcid)0000-0002-9480-1583 aut Enthalten in Food research international New York, NY [u.a.] : Elsevier, 1992 118, Seite 108-114 Online-Ressource (DE-627)300898541 (DE-600)1483651-8 (DE-576)25526660X 1873-7145 nnns volume:118 pages:108-114 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2098 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 58.34 Lebensmitteltechnologie AR 118 108-114
allfields_unstemmed	10.1016/j.foodres.2017.11.040 doi (DE-627)ELV001920243 (ELSEVIER)S0963-9969(17)30809-8 DE-627 ger DE-627 rda eng 630 640 540 660 DE-600 58.34 bkl Claude, Mathilde verfasserin aut Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation 2017 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked. Allergenicity Digestibility Egg allergy Food structure Basophil degranulation Lupi, Roberta verfasserin aut Picariello, Gianluca verfasserin aut Drouet, Martine verfasserin aut Larré, Colette verfasserin aut Denery-Papini, Sandra verfasserin aut Brossard, Chantal verfasserin (orcid)0000-0002-9480-1583 aut Enthalten in Food research international New York, NY [u.a.] : Elsevier, 1992 118, Seite 108-114 Online-Ressource (DE-627)300898541 (DE-600)1483651-8 (DE-576)25526660X 1873-7145 nnns volume:118 pages:108-114 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2098 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 58.34 Lebensmitteltechnologie AR 118 108-114
allfieldsGer	10.1016/j.foodres.2017.11.040 doi (DE-627)ELV001920243 (ELSEVIER)S0963-9969(17)30809-8 DE-627 ger DE-627 rda eng 630 640 540 660 DE-600 58.34 bkl Claude, Mathilde verfasserin aut Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation 2017 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked. Allergenicity Digestibility Egg allergy Food structure Basophil degranulation Lupi, Roberta verfasserin aut Picariello, Gianluca verfasserin aut Drouet, Martine verfasserin aut Larré, Colette verfasserin aut Denery-Papini, Sandra verfasserin aut Brossard, Chantal verfasserin (orcid)0000-0002-9480-1583 aut Enthalten in Food research international New York, NY [u.a.] : Elsevier, 1992 118, Seite 108-114 Online-Ressource (DE-627)300898541 (DE-600)1483651-8 (DE-576)25526660X 1873-7145 nnns volume:118 pages:108-114 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2098 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 58.34 Lebensmitteltechnologie AR 118 108-114
allfieldsSound	10.1016/j.foodres.2017.11.040 doi (DE-627)ELV001920243 (ELSEVIER)S0963-9969(17)30809-8 DE-627 ger DE-627 rda eng 630 640 540 660 DE-600 58.34 bkl Claude, Mathilde verfasserin aut Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation 2017 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked. Allergenicity Digestibility Egg allergy Food structure Basophil degranulation Lupi, Roberta verfasserin aut Picariello, Gianluca verfasserin aut Drouet, Martine verfasserin aut Larré, Colette verfasserin aut Denery-Papini, Sandra verfasserin aut Brossard, Chantal verfasserin (orcid)0000-0002-9480-1583 aut Enthalten in Food research international New York, NY [u.a.] : Elsevier, 1992 118, Seite 108-114 Online-Ressource (DE-627)300898541 (DE-600)1483651-8 (DE-576)25526660X 1873-7145 nnns volume:118 pages:108-114 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2098 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 58.34 Lebensmitteltechnologie AR 118 108-114
language	English
source	Enthalten in Food research international 118, Seite 108-114 volume:118 pages:108-114
sourceStr	Enthalten in Food research international 118, Seite 108-114 volume:118 pages:108-114
format_phy_str_mv	Article
bklname	Lebensmitteltechnologie
institution	findex.gbv.de
topic_facet	Allergenicity Digestibility Egg allergy Food structure Basophil degranulation
dewey-raw	630
isfreeaccess_bool	false
container_title	Food research international
authorswithroles_txt_mv	Claude, Mathilde @@aut@@ Lupi, Roberta @@aut@@ Picariello, Gianluca @@aut@@ Drouet, Martine @@aut@@ Larré, Colette @@aut@@ Denery-Papini, Sandra @@aut@@ Brossard, Chantal @@aut@@
publishDateDaySort_date	2017-01-01T00:00:00Z
hierarchy_top_id	300898541
dewey-sort	3630
id	ELV001920243
language_de	englisch
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author	Claude, Mathilde
spellingShingle	Claude, Mathilde ddc 630 bkl 58.34 misc Allergenicity misc Digestibility misc Egg allergy misc Food structure misc Basophil degranulation Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
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title	Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
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title_full	Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
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title_sort	digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
title_auth	Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
abstract	Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked.
abstractGer	Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked.
abstract_unstemmed	Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked.
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title_short	Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation
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author2	Lupi, Roberta Picariello, Gianluca Drouet, Martine Larré, Colette Denery-Papini, Sandra Brossard, Chantal
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up_date	2024-07-06T23:00:59.797Z
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Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. 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Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation

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