TY  - CONF
AU  - Smiljanić, Katarina
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Divac Rankov, Aleksandra
AU  - Ljujic, Mila
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5950
AB  - Although e-cigarette are still considered a safer alternative to traditional cigarettes, a
growing body of evidence points to their harmful effects on a range of cellular processes .
In this study lung BEAS 2B epithelial cells were treated for 24 h with sub-cytotoxic
concentration1 of e-cigarette vapour, with and without (w/o) nicotine and (w/o) flavor. The
comprehensive proteome analysis was performed via high resolution mass spectrometry
based proteomics (Orbitrap Exploris 240, Thermo Scientific, USA) and relative, label free
quantification of protein expression and their post-translational and chemical modifications
by PEAKS X Pro Studio (BSI Ltd, Ontario, Canada). E-cigarette liquids induced
significant depletion in total number of proteins and impairment of mitochondrial function
in treated cells. Increased presence of post-translational modifications, including
environmentally-driven toxic&harmful, and those classified as direct oxidative
modifications, were observed especially in combined nicotine+flavour treatment
and flavour treatment without nicotine, beside control, pure nicotine and base
liquid treatments. There is a need to study further biological effects of e-cigarettes in
more details, given their widespread use
PB  - Kragujevac : Univerzitet, Prirodno-matematički fakultet
C3  - Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac
T1  - Proteomic and protein modification profiling of lung cells BEAS 2B upon different electronic cigarette vapour treatments
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5950
ER  - 

@conference{
author = "Smiljanić, Katarina and Trifunović, Sara and Prodić, Ivana and Divac Rankov, Aleksandra and Ljujic, Mila",
year = "2023",
abstract = "Although e-cigarette are still considered a safer alternative to traditional cigarettes, a
growing body of evidence points to their harmful effects on a range of cellular processes .
In this study lung BEAS 2B epithelial cells were treated for 24 h with sub-cytotoxic
concentration1 of e-cigarette vapour, with and without (w/o) nicotine and (w/o) flavor. The
comprehensive proteome analysis was performed via high resolution mass spectrometry
based proteomics (Orbitrap Exploris 240, Thermo Scientific, USA) and relative, label free
quantification of protein expression and their post-translational and chemical modifications
by PEAKS X Pro Studio (BSI Ltd, Ontario, Canada). E-cigarette liquids induced
significant depletion in total number of proteins and impairment of mitochondrial function
in treated cells. Increased presence of post-translational modifications, including
environmentally-driven toxic&harmful, and those classified as direct oxidative
modifications, were observed especially in combined nicotine+flavour treatment
and flavour treatment without nicotine, beside control, pure nicotine and base
liquid treatments. There is a need to study further biological effects of e-cigarettes in
more details, given their widespread use",
publisher = "Kragujevac : Univerzitet, Prirodno-matematički fakultet",
journal = "Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac",
title = "Proteomic and protein modification profiling of lung cells BEAS 2B upon different electronic cigarette vapour treatments",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5950"
}

Smiljanić, K., Trifunović, S., Prodić, I., Divac Rankov, A.,& Ljujic, M.. (2023). Proteomic and protein modification profiling of lung cells BEAS 2B upon different electronic cigarette vapour treatments. in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac
Kragujevac : Univerzitet, Prirodno-matematički fakultet..
https://hdl.handle.net/21.15107/rcub_cherry_5950

Smiljanić K, Trifunović S, Prodić I, Divac Rankov A, Ljujic M. Proteomic and protein modification profiling of lung cells BEAS 2B upon different electronic cigarette vapour treatments. in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac. 2023;.
https://hdl.handle.net/21.15107/rcub_cherry_5950 .

Smiljanić, Katarina, Trifunović, Sara, Prodić, Ivana, Divac Rankov, Aleksandra, Ljujic, Mila, "Proteomic and protein modification profiling of lung cells BEAS 2B upon different electronic cigarette vapour treatments" in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac (2023),
https://hdl.handle.net/21.15107/rcub_cherry_5950 .

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Trifunović, Sara
AU  - Krstić-Ristivojević, Maja
AU  - Aćimović, Milica G.
AU  - Stanković Jeremić, Jovana
AU  - Lončar, Biljana
AU  - Tešević, Vele
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6203
AB  - As byproducts of essential oil distillation, hydrolates are used in natural cosmetics/biomedicine due to their beneficial skin effects. However, data on their safety with relevant biological targets, such as human skin cells, are scarce. Therefore, we have tested nine hydrolates from the Lamiaceae family with skin fibroblasts that are responsible for extracellular collagenous matrix builds. Thyme, oregano, and winter savoury hydrolates showed several times higher total phenolics, which correlated strongly with their radical scavenging and antioxidative capacity; there was no correlation between their viability profiles and the reducing sugar levels. No proteins/peptides were detected. All hydrolates appeared safe for prolonged skin exposure except for 10-fold diluted lavender, which showed cytotoxicity (~20%), as well as rosemary and lavandin (~10%) using viability, DNA synthesis, and cell count testing. Clary sage, oregano, lemon balm, and thyme hydrolates (10-fold diluted) increased fibroblast viability and/or proliferation by 10–30% compared with the control, while their viability remained unaffected by Mentha and winter savoury. In line with the STITCH database, increased viability could be attributed to thymol presence in oregano and thyme hydrolates in lemon balm, which is most likely attributable to neral and geranial. The proliferative effect of clary sage could be supported by alpha-terpineol, not linalool. The major volatile organic compounds (VOCs) associated with cytotoxic effects on fibroblasts were borneol, 1,8-cineole, and terpinene-4-ol. Further research with pure compounds is warranted to confirm the roles of VOCs in the observed effects that are relevant to cosmetic and wound healing aspects.
PB  - MDPI
T2  - Antioxidants
T1  - Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts
VL  - 12
IS  - 11
DO  - 10.3390/antiox12111988
ER  - 

@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Trifunović, Sara and Krstić-Ristivojević, Maja and Aćimović, Milica G. and Stanković Jeremić, Jovana and Lončar, Biljana and Tešević, Vele",
year = "2023",
abstract = "As byproducts of essential oil distillation, hydrolates are used in natural cosmetics/biomedicine due to their beneficial skin effects. However, data on their safety with relevant biological targets, such as human skin cells, are scarce. Therefore, we have tested nine hydrolates from the Lamiaceae family with skin fibroblasts that are responsible for extracellular collagenous matrix builds. Thyme, oregano, and winter savoury hydrolates showed several times higher total phenolics, which correlated strongly with their radical scavenging and antioxidative capacity; there was no correlation between their viability profiles and the reducing sugar levels. No proteins/peptides were detected. All hydrolates appeared safe for prolonged skin exposure except for 10-fold diluted lavender, which showed cytotoxicity (~20%), as well as rosemary and lavandin (~10%) using viability, DNA synthesis, and cell count testing. Clary sage, oregano, lemon balm, and thyme hydrolates (10-fold diluted) increased fibroblast viability and/or proliferation by 10–30% compared with the control, while their viability remained unaffected by Mentha and winter savoury. In line with the STITCH database, increased viability could be attributed to thymol presence in oregano and thyme hydrolates in lemon balm, which is most likely attributable to neral and geranial. The proliferative effect of clary sage could be supported by alpha-terpineol, not linalool. The major volatile organic compounds (VOCs) associated with cytotoxic effects on fibroblasts were borneol, 1,8-cineole, and terpinene-4-ol. Further research with pure compounds is warranted to confirm the roles of VOCs in the observed effects that are relevant to cosmetic and wound healing aspects.",
publisher = "MDPI",
journal = "Antioxidants",
title = "Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts",
volume = "12",
number = "11",
doi = "10.3390/antiox12111988"
}

Smiljanić, K., Prodić, I., Trifunović, S., Krstić-Ristivojević, M., Aćimović, M. G., Stanković Jeremić, J., Lončar, B.,& Tešević, V.. (2023). Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts. in Antioxidants
MDPI., 12(11).
https://doi.org/10.3390/antiox12111988

Smiljanić K, Prodić I, Trifunović S, Krstić-Ristivojević M, Aćimović MG, Stanković Jeremić J, Lončar B, Tešević V. Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts. in Antioxidants. 2023;12(11).
doi:10.3390/antiox12111988 .

Smiljanić, Katarina, Prodić, Ivana, Trifunović, Sara, Krstić-Ristivojević, Maja, Aćimović, Milica G., Stanković Jeremić, Jovana, Lončar, Biljana, Tešević, Vele, "Multistep Approach Points to Compounds Responsible for the Biological Activity and Safety of Hydrolates from Nine Lamiaceae Medicinal Plants on Human Skin Fibroblasts" in Antioxidants, 12, no. 11 (2023),
https://doi.org/10.3390/antiox12111988 . .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Krstić-Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5952
AB  - Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.
PB  - MDPI
T2  - Antioxidants
T1  - Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies
VL  - 12
IS  - 4
SP  - 886
DO  - 10.3390/antiox12040886
ER  - 

@article{
author = "Prodić, Ivana and Krstić-Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.",
publisher = "MDPI",
journal = "Antioxidants",
title = "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies",
volume = "12",
number = "4",
pages = "886",
doi = "10.3390/antiox12040886"
}

Prodić, I., Krstić-Ristivojević, M.,& Smiljanić, K.. (2023). Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants
MDPI., 12(4), 886.
https://doi.org/10.3390/antiox12040886

Prodić I, Krstić-Ristivojević M, Smiljanić K. Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants. 2023;12(4):886.
doi:10.3390/antiox12040886 .

Prodić, Ivana, Krstić-Ristivojević, Maja, Smiljanić, Katarina, "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies" in Antioxidants, 12, no. 4 (2023):886,
https://doi.org/10.3390/antiox12040886 . .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5765
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
VL  - 405
SP  - 134981
DO  - 10.1016/j.foodchem.2022.134981
ER  - 

@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
volume = "405",
pages = "134981",
doi = "10.1016/j.foodchem.2022.134981"
}

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .

TY  - CONF
AU  - Prodić, Ivana
AU  - Burazer, Lidija
AU  - Đorić, Nataša
AU  - Krstić-Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - https://kongres2023.preventivnapedijatrija.rs/wp-content/uploads/2023/06/knjiga-sazetaka.pdf
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5954
AB  - Background and Aim: Epidemiological studies pointed at the connection between
pollution (e.g., traffic emissions) and an increased percentage of people suffering from
respiratory allergies, including the pediatric population. Field studies provided the most
relevant assessment of the effects of the intensity and variety of urban and industrial
contamination on the structure and allergenic potency of pollen allergens. Therefore, the
aim of the present work was to compare allergenic profiles of
Dactylis glomerata pollen
(DGP) collected in the specific urban and rural areas (Kruševac and suburbs), to assess
pollen structures and immunoglobulin E (IgE) reactivity to pollen of school children
population allergic to grass pollens.
PB  - Udruženje za preventivnu pedijatriju Srbije
C3  - Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
T1  - Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart
SP  - 58
EP  - 58
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5954
ER  - 

@conference{
author = "Prodić, Ivana and Burazer, Lidija and Đorić, Nataša and Krstić-Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Background and Aim: Epidemiological studies pointed at the connection between
pollution (e.g., traffic emissions) and an increased percentage of people suffering from
respiratory allergies, including the pediatric population. Field studies provided the most
relevant assessment of the effects of the intensity and variety of urban and industrial
contamination on the structure and allergenic potency of pollen allergens. Therefore, the
aim of the present work was to compare allergenic profiles of
Dactylis glomerata pollen
(DGP) collected in the specific urban and rural areas (Kruševac and suburbs), to assess
pollen structures and immunoglobulin E (IgE) reactivity to pollen of school children
population allergic to grass pollens.",
publisher = "Udruženje za preventivnu pedijatriju Srbije",
journal = "Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.",
title = "Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart",
pages = "58-58",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5954"
}

Prodić, I., Burazer, L., Đorić, N., Krstić-Ristivojević, M.,& Smiljanić, K.. (2023). Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
Udruženje za preventivnu pedijatriju Srbije., 58-58.
https://hdl.handle.net/21.15107/rcub_cherry_5954

Prodić I, Burazer L, Đorić N, Krstić-Ristivojević M, Smiljanić K. Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.. 2023;:58-58.
https://hdl.handle.net/21.15107/rcub_cherry_5954 .

Prodić, Ivana, Burazer, Lidija, Đorić, Nataša, Krstić-Ristivojević, Maja, Smiljanić, Katarina, "Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart" in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023. (2023):58-58,
https://hdl.handle.net/21.15107/rcub_cherry_5954 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
PY  - 2023
UR  - https://kongres2023.preventivnapedijatrija.rs/knjiga-apstrakata/
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5953
AB  - Food allergies have increased dramatically in the last decade, especially in developed
countries. Food tolerance requires strict maintenance of a specific microbial portfolio in
the gastrointestinal tract, as changes in the gut microbiome can lead to its disruption,
which in turn causes inflammation and pathogenic gut conditions leading to the
development of food allergies. Any environmental factors that lead to a disturbance
and/or malfunction of the gastrointestinal tract and digestive performance favor the
development of food allergies.
Based on that, what do we know about the role of increasing anthropogenic chemicals,
including emerging ones, resulting from the new global situation?
There is awareness that their effects are multifaceted, e.g., chemicals affect the growth of
plants and animals and thus the quality of the food produced. In addition, chemicals affect
our food during its production and processing, but also affect our body and
gastrointestinal tract. It is time to fill the knowledge gaps and understand how these
interactions between environmental triggers such as industrial and traffic pollution,
transition and heavy metals, pesticides, chemtrails, etc., affect food allergens and their
allergenicity, adjuvant effects, and the increasing prevalence of food allergies.
Some improvements in this area are already being made through advances in ‘omics’
technologies (i.e., proteomics, genomics, metabolomics) and systems biology approaches
that will hopefully provide a scientific understanding of the relationship between
increasing food allergies and the increasingly present wide variety of anthropogenic
chemicals in our environment.
PB  - Udruženje za preventivnu pedijatriju Srbije
C3  - Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
T1  - Food allergies on the rise: the role of anthropogenic chemicals
SP  - 27
EP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5953
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana",
year = "2023",
abstract = "Food allergies have increased dramatically in the last decade, especially in developed
countries. Food tolerance requires strict maintenance of a specific microbial portfolio in
the gastrointestinal tract, as changes in the gut microbiome can lead to its disruption,
which in turn causes inflammation and pathogenic gut conditions leading to the
development of food allergies. Any environmental factors that lead to a disturbance
and/or malfunction of the gastrointestinal tract and digestive performance favor the
development of food allergies.
Based on that, what do we know about the role of increasing anthropogenic chemicals,
including emerging ones, resulting from the new global situation?
There is awareness that their effects are multifaceted, e.g., chemicals affect the growth of
plants and animals and thus the quality of the food produced. In addition, chemicals affect
our food during its production and processing, but also affect our body and
gastrointestinal tract. It is time to fill the knowledge gaps and understand how these
interactions between environmental triggers such as industrial and traffic pollution,
transition and heavy metals, pesticides, chemtrails, etc., affect food allergens and their
allergenicity, adjuvant effects, and the increasing prevalence of food allergies.
Some improvements in this area are already being made through advances in ‘omics’
technologies (i.e., proteomics, genomics, metabolomics) and systems biology approaches
that will hopefully provide a scientific understanding of the relationship between
increasing food allergies and the increasingly present wide variety of anthropogenic
chemicals in our environment.",
publisher = "Udruženje za preventivnu pedijatriju Srbije",
journal = "Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.",
title = "Food allergies on the rise: the role of anthropogenic chemicals",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5953"
}

Smiljanić, K.,& Prodić, I.. (2023). Food allergies on the rise: the role of anthropogenic chemicals. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
Udruženje za preventivnu pedijatriju Srbije., 27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5953

Smiljanić K, Prodić I. Food allergies on the rise: the role of anthropogenic chemicals. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.. 2023;:27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5953 .

Smiljanić, Katarina, Prodić, Ivana, "Food allergies on the rise: the role of anthropogenic chemicals" in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023. (2023):27-27,
https://hdl.handle.net/21.15107/rcub_cherry_5953 .

TY  - JOUR
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5781
AB  - : Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs
PB  - MDPI
T2  - Foods
T1  - Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
VL  - 11
IS  - 24
SP  - 3993
DO  - 10.3390/foods11243993
ER  - 

@article{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = ": Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs",
publisher = "MDPI",
journal = "Foods",
title = "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting",
volume = "11",
number = "24",
pages = "3993",
doi = "10.3390/foods11243993"
}

Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods
MDPI., 11(24), 3993.
https://doi.org/10.3390/foods11243993

Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods. 2022;11(24):3993.
doi:10.3390/foods11243993 .

Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting" in Foods, 11, no. 24 (2022):3993,
https://doi.org/10.3390/foods11243993 . .

TY  - DATA
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5708
AB  - Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
PB  - MDPI
T2  - Foods
T1  - Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993
VL  - 11
IS  - 24
EP  - 3993
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5708
ER  - 

@misc{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993",
volume = "11",
number = "24",
pages = "3993",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5708"
}

Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods
MDPI., 11(24).
https://hdl.handle.net/21.15107/rcub_cherry_5708

Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods. 2022;11(24):null-3993.
https://hdl.handle.net/21.15107/rcub_cherry_5708 .

Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993" in Foods, 11, no. 24 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5708 .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Ballmer-Weber, Barbara
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5653
AB  - Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.
PB  - MDPI
T2  - Foods
T1  - INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity
VL  - 11
SP  - 2914
DO  - 10.3390/foods11182914
ER  - 

@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Ballmer-Weber, Barbara and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.",
publisher = "MDPI",
journal = "Foods",
title = "INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity",
volume = "11",
pages = "2914",
doi = "10.3390/foods11182914"
}

Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods
MDPI., 11, 2914.
https://doi.org/10.3390/foods11182914

Prodić I, Smiljanić K, Nagl C, Ballmer-Weber B, Hoffmann-Sommergruber K, Ćirković-Veličković T. INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods. 2022;11:2914.
doi:10.3390/foods11182914 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Ballmer-Weber, Barbara, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity" in Foods, 11 (2022):2914,
https://doi.org/10.3390/foods11182914 . .

TY  - DATA
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Ballmer-Weber, Barbara
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://doi.org/10.3390/foods11182914
AB  - Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.
PB  - MDPI
T2  - Foods
T1  - Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914
VL  - 11
SP  - 2914
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5657
ER  - 

@misc{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Ballmer-Weber, Barbara and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914",
volume = "11",
pages = "2914",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5657"
}

Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914. in Foods
MDPI., 11, 2914.
https://hdl.handle.net/21.15107/rcub_cherry_5657

Prodić I, Smiljanić K, Nagl C, Ballmer-Weber B, Hoffmann-Sommergruber K, Ćirković-Veličković T. Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914. in Foods. 2022;11:2914.
https://hdl.handle.net/21.15107/rcub_cherry_5657 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Ballmer-Weber, Barbara, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914" in Foods, 11 (2022):2914,
https://hdl.handle.net/21.15107/rcub_cherry_5657 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5716
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting
SP  - 71
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5716
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5716"
}

Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 71-71.
https://hdl.handle.net/21.15107/rcub_cherry_5716

Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cherry_5716 .

Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cherry_5716 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5773
AB  - Background: We have undertaken study on our porcine-derived trypsin generated
proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to
assess possible facilitating/hindrance effects on trypsin digestion efficacy caused by post-
translational and chemical modifications (PTMs) positioned on K/R residues. If potential
hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just
augmented and more pronounced within human intestinal digestion. The logic for such
reasoning is in inferior performance of human trypsin compared to porcine-derived used in
proteomic digestion protocols, also the lower trypsin-to-sample ratio and much shorter
digestion times, even though gastric digestion precedes and trypsin is not the sole digestive
enzyme.
Methods: Novel method was developed to decipher outcomes at scissile bonds using PEAKS
Studio-X+ in reassessment of high-resolution tandem mass spectrometry data on 18h-long
trypsin digestion protocol.
Results: In eight modified K/R residues involving methylation, dihydroxy and formylation,
differences in extent of miscleavage between modified and unmodified peptides, were
significantly higher (>10%) in modified peptides.
Conclusion: It is important to elucidate impact of modifications on trypsin digestion
performance, but also on other proteases involved in digestion process due to possible
effects on allergenicity of food proteins/peptides.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications
SP  - 18
EP  - 18
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5773
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: We have undertaken study on our porcine-derived trypsin generated
proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to
assess possible facilitating/hindrance effects on trypsin digestion efficacy caused by post-
translational and chemical modifications (PTMs) positioned on K/R residues. If potential
hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just
augmented and more pronounced within human intestinal digestion. The logic for such
reasoning is in inferior performance of human trypsin compared to porcine-derived used in
proteomic digestion protocols, also the lower trypsin-to-sample ratio and much shorter
digestion times, even though gastric digestion precedes and trypsin is not the sole digestive
enzyme.
Methods: Novel method was developed to decipher outcomes at scissile bonds using PEAKS
Studio-X+ in reassessment of high-resolution tandem mass spectrometry data on 18h-long
trypsin digestion protocol.
Results: In eight modified K/R residues involving methylation, dihydroxy and formylation,
differences in extent of miscleavage between modified and unmodified peptides, were
significantly higher (>10%) in modified peptides.
Conclusion: It is important to elucidate impact of modifications on trypsin digestion
performance, but also on other proteases involved in digestion process due to possible
effects on allergenicity of food proteins/peptides.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications",
pages = "18-18",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5773"
}

Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 18-18.
https://hdl.handle.net/21.15107/rcub_cherry_5773

Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:18-18.
https://hdl.handle.net/21.15107/rcub_cherry_5773 .

Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):18-18,
https://hdl.handle.net/21.15107/rcub_cherry_5773 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Prodić, Ivana
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5763
AB  - Post-translational modifications (PTMs) occur in many forms, and broadly influence protein behavior.
High-resolution tandem mass spectrometry coupled with engines for the identification of unspecified
PTMs, is a first-choice method for their global mapping. The significance of untargeted, in-depth PTM
profiling of various proteomes and its method development, just emerged, in contrast to proteomic studies
dealing with few selected static and dynamic modifications. In 2018, we have finalized our first study of
comprehensive analysis of multiple polluted and environmentally preserved Timothy grass pollen
samples that included novel method of relative quantification of proteins expressions and of open,
quantitative PTM profiling. It was among the first ones that has appeared in the proteomics field. In
addition to this, relative quantitative PTMs profiling of the raw and roasted peanut allergens was
completed in 2020, including validation of the method by specific antibodies. This peanut PTM study was
inspiration for the idea that porcine trypsin used in proteomic experiments can serve as a probe to
decipher differences in scissile bond hydrolysis caused by PTMs, with the steric and/or charge changes
causing possible hindrance or facilitation to its activity. We further hypothesized that effects observed
would be even more pronounced with human trypsin, since it is less efficient compared to the porcine
counterpart. Finally, we developed dual manual method to reassess our data of the major peanut allergen
Ara h 1 from the raw and roasted peanut, to confirm or rule out the first hypothesis (do PTMs positioned
on lysine/arginine residues facilitate or hinder porcine trypsin digestion efficacy). We believe that this
topic is relevant from the aspect of human gastrointestinal digestion of food allergens and PTMs
introduced by food processing. For further advancement in this area, novel algorithms based on deep
machine learning, capable of reporting cleavage and miscleavage events separately within unmodified
and modified part of protein sequences are warranted.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021
T1  - Methods Development for Protein and Modifications Profiling
SP  - 11
EP  - 11
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5763
ER  - 

@conference{
author = "Smiljanić, Katarina and Đukić, Teodora and Vasović, Tamara and Prodić, Ivana and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Post-translational modifications (PTMs) occur in many forms, and broadly influence protein behavior.
High-resolution tandem mass spectrometry coupled with engines for the identification of unspecified
PTMs, is a first-choice method for their global mapping. The significance of untargeted, in-depth PTM
profiling of various proteomes and its method development, just emerged, in contrast to proteomic studies
dealing with few selected static and dynamic modifications. In 2018, we have finalized our first study of
comprehensive analysis of multiple polluted and environmentally preserved Timothy grass pollen
samples that included novel method of relative quantification of proteins expressions and of open,
quantitative PTM profiling. It was among the first ones that has appeared in the proteomics field. In
addition to this, relative quantitative PTMs profiling of the raw and roasted peanut allergens was
completed in 2020, including validation of the method by specific antibodies. This peanut PTM study was
inspiration for the idea that porcine trypsin used in proteomic experiments can serve as a probe to
decipher differences in scissile bond hydrolysis caused by PTMs, with the steric and/or charge changes
causing possible hindrance or facilitation to its activity. We further hypothesized that effects observed
would be even more pronounced with human trypsin, since it is less efficient compared to the porcine
counterpart. Finally, we developed dual manual method to reassess our data of the major peanut allergen
Ara h 1 from the raw and roasted peanut, to confirm or rule out the first hypothesis (do PTMs positioned
on lysine/arginine residues facilitate or hinder porcine trypsin digestion efficacy). We believe that this
topic is relevant from the aspect of human gastrointestinal digestion of food allergens and PTMs
introduced by food processing. For further advancement in this area, novel algorithms based on deep
machine learning, capable of reporting cleavage and miscleavage events separately within unmodified
and modified part of protein sequences are warranted.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021",
title = "Methods Development for Protein and Modifications Profiling",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5763"
}

Smiljanić, K., Đukić, T., Vasović, T., Prodić, I., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Methods Development for Protein and Modifications Profiling. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021
Univerzitet u Beogradu - Hemijski fakultet., 11-11.
https://hdl.handle.net/21.15107/rcub_cherry_5763

Smiljanić K, Đukić T, Vasović T, Prodić I, Jovanović VB, Ćirković-Veličković T. Methods Development for Protein and Modifications Profiling. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021. 2021;:11-11.
https://hdl.handle.net/21.15107/rcub_cherry_5763 .

Smiljanić, Katarina, Đukić, Teodora, Vasović, Tamara, Prodić, Ivana, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Methods Development for Protein and Modifications Profiling" in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021 (2021):11-11,
https://hdl.handle.net/21.15107/rcub_cherry_5763 .

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/123456789/5730
AB  - Cor a 9 is one of the most common hazelnut allergen, a non-glycosylated protein, consisting of two subunits, an acidic (ranging between 35-40 kDa) and a basic subunit (ranging between 20-25 kDa). Very important fact is that the acid chain carries the immunoreactivity, according to literature. The survival of large fragments of Cor a 9 is necessary for its ability to sensitize individual. The aim of this study was to investigate Cor a 9, and to compare the digestive stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut grains in standardized and physiologically relevant in vitro conditions, after heat treatment (roasting as the most abundant type of heat treatment). In vitro simulated phases of oral and gastric digestion were performed with ground raw and roasted hazelnut kernels according to the 1.0 INFOGEST protocol. After digestion proteins were extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE test was examined in the sera of allergic patients using ELISA and 2D immunoblot. The focus of the research was on the analysis of the 2DE map by Image 2D Master Platinum 7.0 software, comparing region of acid and basic Cor a 9 from raw and roasted hazelnut. Cor a 9 peptides are resistant to gastric digestion, and are able to bind IgE patients. Roasted hazelnuts are more prone to digestion in the stomach than the raw sample and cause a milder IgE response in patients. The gastric digestion phase of raw and roasted hazelnut grains resulted in partial extraction and digestion of Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results show significant resistance of Cor a 9 raw and roasted hazelnuts to digestion in the stomach, as they remained mostly intact after 2 hours of gastric (pepsin) phase and retained their allergenicity.
PB  - Belgrade : University of Belgrade
C3  - Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021
T1  - Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion
SP  - 142
EP  - 142
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5730
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 9 is one of the most common hazelnut allergen, a non-glycosylated protein, consisting of two subunits, an acidic (ranging between 35-40 kDa) and a basic subunit (ranging between 20-25 kDa). Very important fact is that the acid chain carries the immunoreactivity, according to literature. The survival of large fragments of Cor a 9 is necessary for its ability to sensitize individual. The aim of this study was to investigate Cor a 9, and to compare the digestive stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut grains in standardized and physiologically relevant in vitro conditions, after heat treatment (roasting as the most abundant type of heat treatment). In vitro simulated phases of oral and gastric digestion were performed with ground raw and roasted hazelnut kernels according to the 1.0 INFOGEST protocol. After digestion proteins were extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE test was examined in the sera of allergic patients using ELISA and 2D immunoblot. The focus of the research was on the analysis of the 2DE map by Image 2D Master Platinum 7.0 software, comparing region of acid and basic Cor a 9 from raw and roasted hazelnut. Cor a 9 peptides are resistant to gastric digestion, and are able to bind IgE patients. Roasted hazelnuts are more prone to digestion in the stomach than the raw sample and cause a milder IgE response in patients. The gastric digestion phase of raw and roasted hazelnut grains resulted in partial extraction and digestion of Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results show significant resistance of Cor a 9 raw and roasted hazelnuts to digestion in the stomach, as they remained mostly intact after 2 hours of gastric (pepsin) phase and retained their allergenicity.",
publisher = "Belgrade : University of Belgrade",
journal = "Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021",
title = "Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion",
pages = "142-142",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5730"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion. in Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021
Belgrade : University of Belgrade., 142-142.
https://hdl.handle.net/21.15107/rcub_cherry_5730

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion. in Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021. 2021;:142-142.
https://hdl.handle.net/21.15107/rcub_cherry_5730 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion" in Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021 (2021):142-142,
https://hdl.handle.net/21.15107/rcub_cherry_5730 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5762
AB  - Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress
T1  - Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol
SP  - 126
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5762
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress",
title = "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol",
pages = "126-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5762"
}

Prodić, I., Smiljanić, K., Nagl, C., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress
Sociedade Portuguesa de Química., 126-126.
https://hdl.handle.net/21.15107/rcub_cherry_5762

Prodić I, Smiljanić K, Nagl C, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress. 2021;:126-126.
https://hdl.handle.net/21.15107/rcub_cherry_5762 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol" in Book of Abstracts of the XXI EuroFoodChem Congress (2021):126-126,
https://hdl.handle.net/21.15107/rcub_cherry_5762 .

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  - CHAP
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5728
AB  - Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. 
A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.
PB  - New York : Nova Science Publisher
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications
VL  - 4
SP  - 158
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5728
ER  - 

@inbook{
author = "Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. 
A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.",
publisher = "New York : Nova Science Publisher",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications",
volume = "4",
pages = "158",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5728"
}

Smiljanić, K., Mihailović, J., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2020). Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publisher., 4, 158.
https://hdl.handle.net/21.15107/rcub_cherry_5728

Smiljanić K, Mihailović J, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;4:158.
https://hdl.handle.net/21.15107/rcub_cherry_5728 .

Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 4 (2020):158,
https://hdl.handle.net/21.15107/rcub_cherry_5728 .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Apostolović, Danijela
AU  - Smiljanić, Katarina
AU  - Đukić, Teodora
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5727
PB  - Medical University of Vienna - MUW
C3  - Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020
T1  - Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs)
SP  - 1
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5727
ER  - 

@conference{
author = "Mihailović, Jelena and Apostolović, Danijela and Smiljanić, Katarina and Đukić, Teodora and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2020",
publisher = "Medical University of Vienna - MUW",
journal = "Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020",
title = "Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs)",
pages = "1-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5727"
}

Mihailović, J., Apostolović, D., Smiljanić, K., Đukić, T., Prodić, I.,& Ćirković-Veličković, T.. (2020). Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs). in Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020
Medical University of Vienna - MUW., 1-7.
https://hdl.handle.net/21.15107/rcub_cherry_5727

Mihailović J, Apostolović D, Smiljanić K, Đukić T, Prodić I, Ćirković-Veličković T. Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs). in Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020. 2020;:1-7.
https://hdl.handle.net/21.15107/rcub_cherry_5727 .

Mihailović, Jelena, Apostolović, Danijela, Smiljanić, Katarina, Đukić, Teodora, Prodić, Ivana, Ćirković-Veličković, Tanja, "Immunoproteomics study of raw and roasted major peanut allergen post translational modifications (PTMs)" in Abstract Book of the 2nd FoodEnTwin Workshop “Experimental Animal models for food and environment”, Vienna, February 6-7, 2020 (2020):1-7,
https://hdl.handle.net/21.15107/rcub_cherry_5727 .

TY  - CHAP
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Radosavljević, Jelena
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5726
AB  - Common properties of food allergens are prominent resistance to heat treatment and enzyme proteolysis. Stability of the proteins upon gastrointestinal proteolysis of food highly correlates with its allergenic potential. At this moment, the scientific community is putting a lot of effort to connect the available knowledge on the structure and function of food proteins, with stability to proteolysis in order to provide the most reliable prediction tool for allergenicity of novel proteins. Moreover, choosing the conditions under which gastrointestinal proteolysis is simulated may profoundly affect the results of assays and allergenicity assessment. At the beginning of research, for the link between allergenicity and proteolytic stability, purified allergens were used. However, this approchad was proved to be prone to production of erroneous data, since the proteolytic stability of purified proteins was frequently affected by the methodology used for protein purification and the ratio of protens to digestive enzymes used in the assays. Nowadays, the scientific community thrives to establish in vitro digestion protocols that mimic physiological conditions and take into account complex compositon of the food. New studies support this tendency, since it was shown that the presence of various biomolecules in food matrix affects the proteolysis in the simulated gastrointestinal conditions. On top of that, survival of intact proteins upon proteolysis seems not to be necessary, but frequently protein fragments of higher molecular weight with partially preserved structure might be enough to elicit allergic reaction in sensitized individuals.
PB  - New York : Nova Science Publishers
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Food Allergens’ Susceptibility to Proteolysis
VL  - 6
SP  - 220
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5726
ER  - 

@inbook{
author = "Prodić, Ivana and Smiljanić, Katarina and Radosavljević, Jelena",
year = "2020",
abstract = "Common properties of food allergens are prominent resistance to heat treatment and enzyme proteolysis. Stability of the proteins upon gastrointestinal proteolysis of food highly correlates with its allergenic potential. At this moment, the scientific community is putting a lot of effort to connect the available knowledge on the structure and function of food proteins, with stability to proteolysis in order to provide the most reliable prediction tool for allergenicity of novel proteins. Moreover, choosing the conditions under which gastrointestinal proteolysis is simulated may profoundly affect the results of assays and allergenicity assessment. At the beginning of research, for the link between allergenicity and proteolytic stability, purified allergens were used. However, this approchad was proved to be prone to production of erroneous data, since the proteolytic stability of purified proteins was frequently affected by the methodology used for protein purification and the ratio of protens to digestive enzymes used in the assays. Nowadays, the scientific community thrives to establish in vitro digestion protocols that mimic physiological conditions and take into account complex compositon of the food. New studies support this tendency, since it was shown that the presence of various biomolecules in food matrix affects the proteolysis in the simulated gastrointestinal conditions. On top of that, survival of intact proteins upon proteolysis seems not to be necessary, but frequently protein fragments of higher molecular weight with partially preserved structure might be enough to elicit allergic reaction in sensitized individuals.",
publisher = "New York : Nova Science Publishers",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Food Allergens’ Susceptibility to Proteolysis",
volume = "6",
pages = "220",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5726"
}

Prodić, I., Smiljanić, K.,& Radosavljević, J.. (2020). Food Allergens’ Susceptibility to Proteolysis. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publishers., 6, 220.
https://hdl.handle.net/21.15107/rcub_cherry_5726

Prodić I, Smiljanić K, Radosavljević J. Food Allergens’ Susceptibility to Proteolysis. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;6:220.
https://hdl.handle.net/21.15107/rcub_cherry_5726 .

Prodić, Ivana, Smiljanić, Katarina, Radosavljević, Jelena, "Food Allergens’ Susceptibility to Proteolysis" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 6 (2020):220,
https://hdl.handle.net/21.15107/rcub_cherry_5726 .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Simović, Ana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3682
AB  - Resistance to digestion by digestive proteases represents a critical property of many food allergens. Recently, a harmonized INFOGEST protocol was proposed for solid food digestion. The protocol proposes digestion conditions suitable for all kinds of solid and liquid foods. However, peanuts, as a lipid-rich food, represent a challenge for downstream analyses of the digestome. This is particularly reflected in the methodological difficulties in analyzing proteins and peptides in the presence of lipids. Therefore, the removal of the lipids seems to be a prerequisite for the downstream analysis of digestomes of lipid-rich foods. Here, we aimed to compare the digestomes of raw and thermally treated (boiled and roasted) peanuts, resulting from the INFOGEST digestion protocol for solid food, upon defatting the digests in two different manners. The most reproducible results of peanut digests were obtained in downstream analyses on TCA/acetone defatting. Unfortunately, defatting, even with an optimized TCA/acetone procedure, leads to the loss of proteins and peptides. The results of our study reveal that different thermal treatments of peanuts affect protein extraction and gastric/gastrointestinal digestion. Roasting of peanuts seems to enhance the extraction of proteins during intestinal digestion to a notable extent. The increased intestinal digestion is a consequence of the delayed extraction of thermally treated peanut proteins, which are poorly soluble in acidic gastric digestion juice but are easily extracted when the pH of the media is raised as in the subsequent intestinal phase of the digestion. Thermal processing of peanuts impaired the gastrointestinal digestion of the peanut proteins, especially in the case of roasted samples
PB  - MDPI
T2  - Foods
T1  - Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles
VL  - 8
IS  - 10
SP  - 1
EP  - 18
DO  - 10.3390/foods8100463
ER  - 

@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Simović, Ana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Resistance to digestion by digestive proteases represents a critical property of many food allergens. Recently, a harmonized INFOGEST protocol was proposed for solid food digestion. The protocol proposes digestion conditions suitable for all kinds of solid and liquid foods. However, peanuts, as a lipid-rich food, represent a challenge for downstream analyses of the digestome. This is particularly reflected in the methodological difficulties in analyzing proteins and peptides in the presence of lipids. Therefore, the removal of the lipids seems to be a prerequisite for the downstream analysis of digestomes of lipid-rich foods. Here, we aimed to compare the digestomes of raw and thermally treated (boiled and roasted) peanuts, resulting from the INFOGEST digestion protocol for solid food, upon defatting the digests in two different manners. The most reproducible results of peanut digests were obtained in downstream analyses on TCA/acetone defatting. Unfortunately, defatting, even with an optimized TCA/acetone procedure, leads to the loss of proteins and peptides. The results of our study reveal that different thermal treatments of peanuts affect protein extraction and gastric/gastrointestinal digestion. Roasting of peanuts seems to enhance the extraction of proteins during intestinal digestion to a notable extent. The increased intestinal digestion is a consequence of the delayed extraction of thermally treated peanut proteins, which are poorly soluble in acidic gastric digestion juice but are easily extracted when the pH of the media is raised as in the subsequent intestinal phase of the digestion. Thermal processing of peanuts impaired the gastrointestinal digestion of the peanut proteins, especially in the case of roasted samples",
publisher = "MDPI",
journal = "Foods",
title = "Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles",
volume = "8",
number = "10",
pages = "1-18",
doi = "10.3390/foods8100463"
}

Prodić, I., Smiljanić, K., Simović, A., Radosavljević, J.,& Ćirković-Veličković, T.. (2019). Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles. in Foods
MDPI., 8(10), 1-18.
https://doi.org/10.3390/foods8100463

Prodić I, Smiljanić K, Simović A, Radosavljević J, Ćirković-Veličković T. Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles. in Foods. 2019;8(10):1-18.
doi:10.3390/foods8100463 .

Prodić, Ivana, Smiljanić, Katarina, Simović, Ana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles" in Foods, 8, no. 10 (2019):1-18,
https://doi.org/10.3390/foods8100463 . .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5724
AB  - Background: An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been appreciated; hence, little progress has been made within this field. Our aim was to show that in-depth PTM profiling has a great importance and deserves to be explored with renewed and simple method with advanced algorithm.
Method: We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting.
Results: An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA.
Conclusion: Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed that heavy metals are primarily responsible for oxidative stress effects observed in Timothy grass pollen proteome, rather than gaseous pollutants formed during road traffics such as ozone, nitric dioxide or Sulphur di- and/or trioxide.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress
IS  - L7
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5724
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Background: An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been appreciated; hence, little progress has been made within this field. Our aim was to show that in-depth PTM profiling has a great importance and deserves to be explored with renewed and simple method with advanced algorithm.
Method: We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting.
Results: An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA.
Conclusion: Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed that heavy metals are primarily responsible for oxidative stress effects observed in Timothy grass pollen proteome, rather than gaseous pollutants formed during road traffics such as ozone, nitric dioxide or Sulphur di- and/or trioxide.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress",
number = "L7",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5724"
}

Smiljanić, K., Prodić, I., Apostolović, D., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress. in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA.(L7), 13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5724

Smiljanić K, Prodić I, Apostolović D, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress. in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019. 2019;(L7):13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5724 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019, no. L7 (2019):13-13,
https://hdl.handle.net/21.15107/rcub_cherry_5724 .

TY  - THES
AU  - Prodić, Ivana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7705
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22917/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23935753
UR  - https://nardus.mpn.gov.rs/handle/123456789/17617
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4384
AB  - INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije.
AB  - INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17617
ER  - 

@phdthesis{
author = "Prodić, Ivana",
year = "2019",
abstract = "INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije., INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17617"
}

Prodić, I.. (2019). Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_17617

Prodić I. Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_17617 .

Prodić, Ivana, "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_17617 .

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  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5722
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions ranging from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known about their post-translational modifications (PTM) and how they are affected by thermal treatment. PTM profile may differ between raw and thermally treated peanut, which could affect its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software (Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amounts of any of the studied allergens between raw and roasted extracts. Out of the 4 allergens Ara h 6 is modified in the highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw and roasted sample, respectively. Total of 21 modifications were quantified between the two preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and quantity between treated and non-treated extracts. The in silico discovered PTMs could affect protein digestibility and allergenicity. Further investigation is necessary in order to fully understand the impact protein modifications could have on their allergenic potential.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
IS  - 26
EP  - 26
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5722
ER  - 

@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions ranging from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known about their post-translational modifications (PTM) and how they are affected by thermal treatment. PTM profile may differ between raw and thermally treated peanut, which could affect its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software (Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amounts of any of the studied allergens between raw and roasted extracts. Out of the 4 allergens Ara h 6 is modified in the highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw and roasted sample, respectively. Total of 21 modifications were quantified between the two preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and quantity between treated and non-treated extracts. The in silico discovered PTMs could affect protein digestibility and allergenicity. Further investigation is necessary in order to fully understand the impact protein modifications could have on their allergenic potential.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
number = "26",
pages = "26",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5722"
}

Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet.(26).
https://hdl.handle.net/21.15107/rcub_cherry_5722

Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;(26):null-26.
https://hdl.handle.net/21.15107/rcub_cherry_5722 .

Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019, no. 26 (2019),
https://hdl.handle.net/21.15107/rcub_cherry_5722 .