TY  - JOUR
AU  - Costa, Joana
AU  - Villa, Caterina
AU  - Verhoeckx, Kitty
AU  - Ćirković-Veličković, Tanja
AU  - Schrama, Denise
AU  - Roncada, Paola
AU  - Rodrigues, Pedro M.
AU  - Piras, Cristian
AU  - Martín-Pedraza, Laura
AU  - Monaci, Linda
AU  - Molina, Elena
AU  - Mazzucchelli, Gabriel
AU  - Mafra, Isabel
AU  - Lupi, Roberta
AU  - Lozano-Ojalvo, Daniel
AU  - Larré, Colette
AU  - Klueber, Julia
AU  - Gelencser, Eva
AU  - Bueno-Diaz, Cristina
AU  - Diaz-Perales, Araceli
AU  - Benedé, Sara
AU  - Bavaro, Simona Lucia
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5791
AB  - Key determinants for the development of an allergic response to an otherwise ‘harmless’ food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing. Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens.
T2  - Clinical Reviews in Allergy & Immunology
T1  - Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?
VL  - 62
IS  - 1
SP  - 1
EP  - 36
DO  - 10.1007/s12016-020-08826-1
ER  - 

@article{
author = "Costa, Joana and Villa, Caterina and Verhoeckx, Kitty and Ćirković-Veličković, Tanja and Schrama, Denise and Roncada, Paola and Rodrigues, Pedro M. and Piras, Cristian and Martín-Pedraza, Laura and Monaci, Linda and Molina, Elena and Mazzucchelli, Gabriel and Mafra, Isabel and Lupi, Roberta and Lozano-Ojalvo, Daniel and Larré, Colette and Klueber, Julia and Gelencser, Eva and Bueno-Diaz, Cristina and Diaz-Perales, Araceli and Benedé, Sara and Bavaro, Simona Lucia and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
abstract = "Key determinants for the development of an allergic response to an otherwise ‘harmless’ food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing. Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens.",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?",
volume = "62",
number = "1",
pages = "1-36",
doi = "10.1007/s12016-020-08826-1"
}

Costa, J., Villa, C., Verhoeckx, K., Ćirković-Veličković, T., Schrama, D., Roncada, P., Rodrigues, P. M., Piras, C., Martín-Pedraza, L., Monaci, L., Molina, E., Mazzucchelli, G., Mafra, I., Lupi, R., Lozano-Ojalvo, D., Larré, C., Klueber, J., Gelencser, E., Bueno-Diaz, C., Diaz-Perales, A., Benedé, S., Bavaro, S. L., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?. in Clinical Reviews in Allergy & Immunology, 62(1), 1-36.
https://doi.org/10.1007/s12016-020-08826-1

Costa J, Villa C, Verhoeckx K, Ćirković-Veličković T, Schrama D, Roncada P, Rodrigues PM, Piras C, Martín-Pedraza L, Monaci L, Molina E, Mazzucchelli G, Mafra I, Lupi R, Lozano-Ojalvo D, Larré C, Klueber J, Gelencser E, Bueno-Diaz C, Diaz-Perales A, Benedé S, Bavaro SL, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?. in Clinical Reviews in Allergy & Immunology. 2022;62(1):1-36.
doi:10.1007/s12016-020-08826-1 .

Costa, Joana, Villa, Caterina, Verhoeckx, Kitty, Ćirković-Veličković, Tanja, Schrama, Denise, Roncada, Paola, Rodrigues, Pedro M., Piras, Cristian, Martín-Pedraza, Laura, Monaci, Linda, Molina, Elena, Mazzucchelli, Gabriel, Mafra, Isabel, Lupi, Roberta, Lozano-Ojalvo, Daniel, Larré, Colette, Klueber, Julia, Gelencser, Eva, Bueno-Diaz, Cristina, Diaz-Perales, Araceli, Benedé, Sara, Bavaro, Simona Lucia, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?" in Clinical Reviews in Allergy & Immunology, 62, no. 1 (2022):1-36,
https://doi.org/10.1007/s12016-020-08826-1 . .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5772
AB  - Background: In vitro pepsin digestion is important factor when assessing protein food
allergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;
however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. There
are only two studies employing in vitro INFOGEST digestion harmonized protocol on
hazelnut with its full matrix. The aim of this study was to assess immunoreactivity of raw
and roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9
allergen purified from these two sources.
Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.
Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, were
assessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structural
analyses.
Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yet
their large fragments survived partially. Cor a 8 was protected by lipids, retaining capability
to bind its specific antibody. Roasting did not significantly affect secondary structure of the
most abundant hazelnut allergen, Cor a 9.
Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera of
hazelnut allergic patients with oral-gastric allergen digests.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart
SP  - 62
EP  - 62
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5772
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: In vitro pepsin digestion is important factor when assessing protein food
allergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;
however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. There
are only two studies employing in vitro INFOGEST digestion harmonized protocol on
hazelnut with its full matrix. The aim of this study was to assess immunoreactivity of raw
and roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9
allergen purified from these two sources.
Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.
Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, were
assessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structural
analyses.
Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yet
their large fragments survived partially. Cor a 8 was protected by lipids, retaining capability
to bind its specific antibody. Roasting did not significantly affect secondary structure of the
most abundant hazelnut allergen, Cor a 9.
Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera of
hazelnut allergic patients with oral-gastric allergen digests.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart",
pages = "62-62",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5772"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 62-62.
https://hdl.handle.net/21.15107/rcub_cherry_5772

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:62-62.
https://hdl.handle.net/21.15107/rcub_cherry_5772 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):62-62,
https://hdl.handle.net/21.15107/rcub_cherry_5772 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5764
AB  - Most of the hazelnut proteins are resistant to proteolysis in the gastrointestinal tract, and the survival
of their large fragments are essential for their sensitizing capacity. Usually, studies were carried out
on purified proteins, paying no attention to the potential impact of the food matrix and thermal
treatment on allergenicity. Obtained hazelnut peptides after gastric digestion, especially those with
potential IgE binding epitopes, highlight the need for further studies on their IgE reactivity. The aim
of this study was to investigate and compare digestion stability and allergenicity of large and small
peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized
and physiologically relevant in vitro conditions, after thermal treatment (roasting as most abundant
type of thermal treatment). In vitro simulated oral and gastric phase digestion was carried out with
ground raw and roasted hazelnut kernels according to INFOGEST protocol. Digested proteins were
extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE biding
was probed with allergic patients’ sera via ELISA and 2D immunoblot. The most abundant hazelnut
allergens within 2DE map were acidic and basic chains of Cor a 9 and Cor a 11. Digestion-resistant
peptides of Cor a 11 and Cor a 9 were able to bind patients’ IgE. Roasted hazelnut is more prone to
gastric digestion than the raw sample, and cause milder IgE response in patients. Gastric phase
digestion of raw and roasted hazelnut kernels resulted in partial extraction and digestion of Cor a 11
and Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results
demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since
they remained mostly intact after 2 h of gastric (pepsin) phase and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June
T1  - Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol
SP  - 36
EP  - 36
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5764
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Most of the hazelnut proteins are resistant to proteolysis in the gastrointestinal tract, and the survival
of their large fragments are essential for their sensitizing capacity. Usually, studies were carried out
on purified proteins, paying no attention to the potential impact of the food matrix and thermal
treatment on allergenicity. Obtained hazelnut peptides after gastric digestion, especially those with
potential IgE binding epitopes, highlight the need for further studies on their IgE reactivity. The aim
of this study was to investigate and compare digestion stability and allergenicity of large and small
peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized
and physiologically relevant in vitro conditions, after thermal treatment (roasting as most abundant
type of thermal treatment). In vitro simulated oral and gastric phase digestion was carried out with
ground raw and roasted hazelnut kernels according to INFOGEST protocol. Digested proteins were
extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE biding
was probed with allergic patients’ sera via ELISA and 2D immunoblot. The most abundant hazelnut
allergens within 2DE map were acidic and basic chains of Cor a 9 and Cor a 11. Digestion-resistant
peptides of Cor a 11 and Cor a 9 were able to bind patients’ IgE. Roasted hazelnut is more prone to
gastric digestion than the raw sample, and cause milder IgE response in patients. Gastric phase
digestion of raw and roasted hazelnut kernels resulted in partial extraction and digestion of Cor a 11
and Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results
demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since
they remained mostly intact after 2 h of gastric (pepsin) phase and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June",
title = "Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol",
pages = "36-36",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5764"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June
Univerzitet u Beogradu - Hemijski fakultet., 36-36.
https://hdl.handle.net/21.15107/rcub_cherry_5764

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June. 2021;:36-36.
https://hdl.handle.net/21.15107/rcub_cherry_5764 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol" in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June (2021):36-36,
https://hdl.handle.net/21.15107/rcub_cherry_5764 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5721
AB  - Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.
Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.
Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.
Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a
11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products
SP  - 25
EP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5721
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Mihailović, Jelena and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.
Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.
Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.
Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a
11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5721"
}

Prodić, I., Smiljanić, K., Mihailović, J., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2019). Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet., 25-25.
https://hdl.handle.net/21.15107/rcub_cherry_5721

Prodić I, Smiljanić K, Mihailović J, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;:25-25.
https://hdl.handle.net/21.15107/rcub_cherry_5721 .

Prodić, Ivana, Smiljanić, Katarina, Mihailović, Jelena, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019 (2019):25-25,
https://hdl.handle.net/21.15107/rcub_cherry_5721 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Dubiela, Pawel
AU  - Mihailović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5719
AB  - Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.
Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.
Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.
Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.
Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.
PB  - IMPARAS Cost Action FA1402
C3  - Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018
T1  - Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion
SP  - 59
EP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5719
ER  - 

@conference{
author = "Prodić, Ivana and Dubiela, Pawel and Mihailović, Jelena and Stanić-Vučinić, Dragana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.
Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.
Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.
Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.
Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.",
publisher = "IMPARAS Cost Action FA1402",
journal = "Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018",
title = "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5719"
}

Prodić, I., Dubiela, P., Mihailović, J., Stanić-Vučinić, D., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2018). Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018
IMPARAS Cost Action FA1402., 59-59.
https://hdl.handle.net/21.15107/rcub_cherry_5719

Prodić I, Dubiela P, Mihailović J, Stanić-Vučinić D, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018. 2018;:59-59.
https://hdl.handle.net/21.15107/rcub_cherry_5719 .

Prodić, Ivana, Dubiela, Pawel, Mihailović, Jelena, Stanić-Vučinić, Dragana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion" in Proceedings of the 4th International ImpARAS 
Conference, Portici (Naples), Italy, June 19-21, 2018 (2018):59-59,
https://hdl.handle.net/21.15107/rcub_cherry_5719 .