Prodić, Ivana

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  • Prodić, Ivana (19)
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Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu

Prodić, Ivana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - BOOK
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  - http://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
ER  - 
@phdthesis{
author = "Prodić, Ivana",
year = "2019",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=7705, https://fedorabg.bg.ac.rs/fedora/get/o:22917/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23935753, https://nardus.mpn.gov.rs/handle/123456789/17617, http://cherry.chem.bg.ac.rs/handle/123456789/4384",
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"
}
Prodić, I. (2019). Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu.
Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Prodić I. Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. Универзитет у Београду. 2019;
Prodić Ivana, "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu" Универзитет у Београду (2019)

Thermal Processing of Peanut Grains Impairs Their Mimicked Gastrointestinal Digestion While Downstream Defatting Treatments Affect Digestomic Profiles

Prodić, Ivana; Smiljanić, Katarina; Simović, Ana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(MDPI, 2019)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Simović, Ana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://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  - https://doi.org/10.3390/foods8100463
ER  - 
@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Simović, Ana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3682",
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 = "https://doi.org/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.
Foods
MDPI., 8(10), 1-18.
https://doi.org/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. Foods. 2019;8(10):1-18
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" Foods, 8, no. 10 (2019):1-18,
https://doi.org/https://doi.org/10.3390/foods8100463 .
1

In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljković, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Wiley, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljković, 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/123456789/3737
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress
VL  - 74
IS  - supp. 106
SP  - 878
EP  - 878
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljković, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3737",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress",
volume = "74",
number = "supp. 106",
pages = "878-878"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljković, 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 allergome in relation to environmental pollution and oxidative stress.
Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74(supp. 106), 878-878.
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljković Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74(supp. 106):878-878
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Cvetković Anka, Veljković Đorđe, Mutić Jelena, van Hage Marianne, Burazer Lidija M., Ćirković-Veličković Tanja, "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress" Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74, no. supp. 106 (2019):878-878

Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Belgrade : Faculty of Chemistry, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
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/123456789/3742
AB  - 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
determined; hence, little progress has been made within this field.
PB  - Belgrade : Faculty of Chemistry
C3  - 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
T1  - Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments
SP  - 6
EP  - 7
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3742",
abstract = "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
determined; hence, little progress has been made within this field.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia",
title = "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments",
pages = "6-7"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T. (2019). Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments.
1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
Belgrade : Faculty of Chemistry., 6-7.
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia. 2019;:6-7
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Mutić Jelena, van Hage Marianne, Burazer Lidija M., Ćirković-Veličković Tanja, "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments" 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia (2019):6-7

Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
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/123456789/3763
AB  - 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 determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. 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 pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.
C3  - XIV Italian Proteomics Association Annual Meeting with HPS, 2019.
T1  - Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution
SP  - 38
EP  - 38
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3763",
abstract = "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 determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. 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 pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.",
journal = "XIV Italian Proteomics Association Annual Meeting with HPS, 2019.",
title = "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution",
pages = "38-38"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T. (2019). Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution.
XIV Italian Proteomics Association Annual Meeting with HPS, 2019., 38-38.
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. XIV Italian Proteomics Association Annual Meeting with HPS, 2019.. 2019;:38-38
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Mutić Jelena, van Hage Marianne, Burazer Lidija M., Ćirković-Veličković Tanja, "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution" XIV Italian Proteomics Association Annual Meeting with HPS, 2019. (2019):38-38

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
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/123456789/2857
AB  - 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 determined; hence, little progress has been made within this field. 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. 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. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Elsevier
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
VL  - 126
SP  - 644
EP  - 658
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2857",
abstract = "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 determined; hence, little progress has been made within this field. 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. 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. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Elsevier",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
volume = "126",
pages = "644-658",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., 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 allergome in relation to environmental oxidative stress.
Environment International
Elsevier., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. Environment International. 2019;126:644-658
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Cvetković Anka, 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 allergome in relation to environmental oxidative stress" Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 .
2
5
2
4

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3224
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3224",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides.
Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. Clinical and Experimental Allergy. 2018;48(6):731-740
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - BOOK
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3225
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113
ER  - 
@book{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3225",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113.
Clinical and Experimental Allergy
Wiley, Hoboken..
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. Clinical and Experimental Allergy. 2018;
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113" Clinical and Experimental Allergy (2018)

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2155
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2155",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides.
Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. Clinical and Experimental Allergy. 2018;48(6):731-740
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074

Peruško, Marija; Al-Hanish, Ayah; Mihailović-Vesić, Jelena; Minić, Simeon L.; Trifunović, Sara; Prodić, Ivana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - BOOK
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović-Vesić, Jelena
AU  - Minić, Simeon L.
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3027
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074
ER  - 
@book{
author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3027",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074"
}
Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T. (2017). Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074.
Food Chemistry
Elsevier Sci Ltd, Oxford..
Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074. Food Chemistry. 2017;
Peruško Marija, Al-Hanish Ayah, Mihailović-Vesić Jelena, Minić Simeon L., Trifunović Sara, Prodić Ivana, Ćirković-Veličković Tanja, "Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074" Food Chemistry (2017)

Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Mihailović-Vesić, Jelena; Minić, Simeon L.; Trifunović, Sara; Prodić, Ivana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - JOUR
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović-Vesić, Jelena
AU  - Minić, Simeon L.
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2456
AB  - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
VL  - 232
SP  - 744
EP  - 752
DO  - 10.1016/j.foodchem.2017.04.074
ER  - 
@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2456",
abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction",
volume = "232",
pages = "744-752",
doi = "10.1016/j.foodchem.2017.04.074"
}
Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction.
Food Chemistry
Elsevier Sci Ltd, Oxford., 232, 744-752.
https://doi.org/10.1016/j.foodchem.2017.04.074
Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. Food Chemistry. 2017;232:744-752
Peruško Marija, Al-Hanish Ayah, Mihailović-Vesić Jelena, Minić Simeon L., Trifunović Sara, Prodić Ivana, Ćirković-Veličković Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 .
21
19
21

Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - BOOK
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3585
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012
ER  - 
@book{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3585",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford..
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012. Food Hydrocolloids. 2016;
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012" Food Hydrocolloids (2016)

Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2299
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
VL  - 61
SP  - 241
EP  - 250
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 
@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2299",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
volume = "61",
pages = "241-250",
doi = "10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. Food Hydrocolloids. 2016;61:241-250
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 .
2
57
44
56

Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - BOOK
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2905
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040
ER  - 
@book{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2905",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2013). Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040.
Food Chemistry
Elsevier Sci Ltd, Oxford..
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040. Food Chemistry. 2013;
Stojadinović Marija M., Radosavljević Jelena, Ognjenović Jana, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040" Food Chemistry (2013)

Supplementary data for article: Stanić-Vučinić, D.; Prodić, I.; Apostolović, D.; Nikolić, M.; Ćirković-Veličković, T. Structure and Antioxidant Activity of Beta-Lactoglobulin-Glycoconjugates Obtained by High-Intensity-Ultrasound-Induced Maillard Reaction in Aqueous Model Systems under Neutral Conditions. Food Chemistry 2013, 138 (1), 590–599. https://doi.org/10.1016/j.foodchem.2012.10.087

Stanić-Vučinić, Dragana; Prodić, Ivana; Apostolović, Danijela; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - BOOK
AU  - Stanić-Vučinić, Dragana
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3525
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for article: Stanić-Vučinić, D.; Prodić, I.; Apostolović, D.; Nikolić, M.; Ćirković-Veličković, T. Structure and Antioxidant Activity of Beta-Lactoglobulin-Glycoconjugates Obtained by High-Intensity-Ultrasound-Induced Maillard Reaction in Aqueous Model Systems under Neutral Conditions. Food Chemistry 2013, 138 (1), 590–599. https://doi.org/10.1016/j.foodchem.2012.10.087
ER  - 
@book{
author = "Stanić-Vučinić, Dragana and Prodić, Ivana and Apostolović, Danijela and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3525",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for article: Stanić-Vučinić, D.; Prodić, I.; Apostolović, D.; Nikolić, M.; Ćirković-Veličković, T. Structure and Antioxidant Activity of Beta-Lactoglobulin-Glycoconjugates Obtained by High-Intensity-Ultrasound-Induced Maillard Reaction in Aqueous Model Systems under Neutral Conditions. Food Chemistry 2013, 138 (1), 590–599. https://doi.org/10.1016/j.foodchem.2012.10.087"
}
Stanić-Vučinić, D., Prodić, I., Apostolović, D., Nikolić, M.,& Ćirković-Veličković, T. (2013). Supplementary data for article: Stanić-Vučinić, D.; Prodić, I.; Apostolović, D.; Nikolić, M.; Ćirković-Veličković, T. Structure and Antioxidant Activity of Beta-Lactoglobulin-Glycoconjugates Obtained by High-Intensity-Ultrasound-Induced Maillard Reaction in Aqueous Model Systems under Neutral Conditions. Food Chemistry 2013, 138 (1), 590–599. https://doi.org/10.1016/j.foodchem.2012.10.087.
Food Chemistry
Elsevier Sci Ltd, Oxford..
Stanić-Vučinić D, Prodić I, Apostolović D, Nikolić M, Ćirković-Veličković T. Supplementary data for article: Stanić-Vučinić, D.; Prodić, I.; Apostolović, D.; Nikolić, M.; Ćirković-Veličković, T. Structure and Antioxidant Activity of Beta-Lactoglobulin-Glycoconjugates Obtained by High-Intensity-Ultrasound-Induced Maillard Reaction in Aqueous Model Systems under Neutral Conditions. Food Chemistry 2013, 138 (1), 590–599. https://doi.org/10.1016/j.foodchem.2012.10.087. Food Chemistry. 2013;
Stanić-Vučinić Dragana, Prodić Ivana, Apostolović Danijela, Nikolić Milan, Ćirković-Veličković Tanja, "Supplementary data for article: Stanić-Vučinić, D.; Prodić, I.; Apostolović, D.; Nikolić, M.; Ćirković-Veličković, T. Structure and Antioxidant Activity of Beta-Lactoglobulin-Glycoconjugates Obtained by High-Intensity-Ultrasound-Induced Maillard Reaction in Aqueous Model Systems under Neutral Conditions. Food Chemistry 2013, 138 (1), 590–599. https://doi.org/10.1016/j.foodchem.2012.10.087" Food Chemistry (2013)

Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1577
AB  - Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
VL  - 136
IS  - 3-4
SP  - 1263
EP  - 1271
DO  - 10.1016/j.foodchem.2012.09.040
ER  - 
@article{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1577",
abstract = "Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed",
volume = "136",
number = "3-4",
pages = "1263-1271",
doi = "10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2013). Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed.
Food Chemistry
Elsevier Sci Ltd, Oxford., 136(3-4), 1263-1271.
https://doi.org/10.1016/j.foodchem.2012.09.040
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. Food Chemistry. 2013;136(3-4):1263-1271
Stojadinović Marija M., Radosavljević Jelena, Ognjenović Jana, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed" Food Chemistry, 136, no. 3-4 (2013):1263-1271,
https://doi.org/10.1016/j.foodchem.2012.09.040 .
122
106
124

Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions

Stanić-Vučinić, Dragana; Prodić, Ivana; Apostolović, Danijela; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1583
AB  - Sonication is a new processing technology in the dairy industry. The aim of this study was to test glycation of beta-lactoglobulin (BLG) in Maillard reaction (MR) induced by high-intensity ultrasound in aqueous solution under neutral conditions at 10-15 degrees C, which is not favourable for the MR. BLG was sonicated in the presence of glucose, galactose, lactose, fructose, ribose and arabinose. Formation of Maillard reaction products (MRPs) was monitored by mass spectrometry, spectrophotometry and fluorimetry. Ultrasound treatment resulted in formation of MRPs with all tested carbohydrates. Ribose induced the highest degree of modification resulting in 76% of BLG modified and an average of three anhydroribose units attached. Circular dichroism spectra analyses indicated only minor alterations in secondary and tertiary structures. MRP obtained by ultrasound exhibited 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity and possessed increased iron-chelating activity and reducing power. High-intensity ultrasound efficiently promotes BLG-glycoconjugates formation by MR in aqueous solutions under non-denaturing conditions.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions
VL  - 138
IS  - 1
SP  - 590
EP  - 599
DO  - 10.1016/j.foodchem.2012.10.087
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Prodić, Ivana and Apostolović, Danijela and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1583",
abstract = "Sonication is a new processing technology in the dairy industry. The aim of this study was to test glycation of beta-lactoglobulin (BLG) in Maillard reaction (MR) induced by high-intensity ultrasound in aqueous solution under neutral conditions at 10-15 degrees C, which is not favourable for the MR. BLG was sonicated in the presence of glucose, galactose, lactose, fructose, ribose and arabinose. Formation of Maillard reaction products (MRPs) was monitored by mass spectrometry, spectrophotometry and fluorimetry. Ultrasound treatment resulted in formation of MRPs with all tested carbohydrates. Ribose induced the highest degree of modification resulting in 76% of BLG modified and an average of three anhydroribose units attached. Circular dichroism spectra analyses indicated only minor alterations in secondary and tertiary structures. MRP obtained by ultrasound exhibited 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity and possessed increased iron-chelating activity and reducing power. High-intensity ultrasound efficiently promotes BLG-glycoconjugates formation by MR in aqueous solutions under non-denaturing conditions.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions",
volume = "138",
number = "1",
pages = "590-599",
doi = "10.1016/j.foodchem.2012.10.087"
}
Stanić-Vučinić, D., Prodić, I., Apostolović, D., Nikolić, M.,& Ćirković-Veličković, T. (2013). Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions.
Food Chemistry
Elsevier Sci Ltd, Oxford., 138(1), 590-599.
https://doi.org/10.1016/j.foodchem.2012.10.087
Stanić-Vučinić D, Prodić I, Apostolović D, Nikolić M, Ćirković-Veličković T. Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. Food Chemistry. 2013;138(1):590-599
Stanić-Vučinić Dragana, Prodić Ivana, Apostolović Danijela, Nikolić Milan, Ćirković-Veličković Tanja, "Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions" Food Chemistry, 138, no. 1 (2013):590-599,
https://doi.org/10.1016/j.foodchem.2012.10.087 .
75
68
81

Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity

Stojadinović, Marija M.; Ognjenović, J.; Radosavljević, Jelena; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2012)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Ognjenović, J.
AU  - Radosavljević, Jelena
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1527
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity
VL  - 279
SP  - 400
EP  - 400
ER  - 
@conference{
author = "Stojadinović, Marija M. and Ognjenović, J. and Radosavljević, Jelena and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1527",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity",
volume = "279",
pages = "400-400"
}
Stojadinović, M. M., Ognjenović, J., Radosavljević, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2012). Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 279, 400-400.
Stojadinović MM, Ognjenović J, Radosavljević J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity. FEBS Journal / Federation of European of Biochemical Societies. 2012;279:400-400
Stojadinović Marija M., Ognjenović J., Radosavljević Jelena, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity" FEBS Journal / Federation of European of Biochemical Societies, 279 (2012):400-400
2

Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase

Tantoush, Ziyad; Apostolović, Danijela; Kravić, Bojana; Prodić, Ivana; Mihajlovic, Luka; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2012)

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Apostolović, Danijela
AU  - Kravić, Bojana
AU  - Prodić, Ivana
AU  - Mihajlovic, Luka
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1311
AB  - The in vitro gastric digestion of several food allergens (beta-lactoglobulin (BLG), alpha-lactalbumin (LA) and peanut allergens (PE)) in the presence of a catechin-enriched polyphenol extract of green tea (GTC), oxidized polyphenols and phenol oxidase processed food allergens and GTC was investigated. Pepsin-resistant proteins, such as BLG, major peanut allergens, Ara h 1 and Ara h 2, degrade faster in the presence of catechin-enriched green tea polyphenols. Phenol oxidase polymerized GTC affected adversely protein digestion of BLG and LA, but not digestion of PE proteins. Protecting effect of polyphenols correlated well with the ability of proteins to form insoluble complexes with oxidized catechins. Cross-linking of proteins and polyphenols further extended the half-lives of BLG and LA in the in vitro digestion by pepsin. Catechin-enriched green tea polyphenols of food supplements facilitate pepsin digestion of major food allergens, but hamper their digestion if oxidized and polymerized by phenol oxidase. (c) 2012 Elsevier Ltd. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Functional Foods
T1  - Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase
VL  - 4
IS  - 3
SP  - 650
EP  - 660
DO  - 10.1016/j.jff.2012.04.006
ER  - 
@article{
author = "Tantoush, Ziyad and Apostolović, Danijela and Kravić, Bojana and Prodić, Ivana and Mihajlovic, Luka and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1311",
abstract = "The in vitro gastric digestion of several food allergens (beta-lactoglobulin (BLG), alpha-lactalbumin (LA) and peanut allergens (PE)) in the presence of a catechin-enriched polyphenol extract of green tea (GTC), oxidized polyphenols and phenol oxidase processed food allergens and GTC was investigated. Pepsin-resistant proteins, such as BLG, major peanut allergens, Ara h 1 and Ara h 2, degrade faster in the presence of catechin-enriched green tea polyphenols. Phenol oxidase polymerized GTC affected adversely protein digestion of BLG and LA, but not digestion of PE proteins. Protecting effect of polyphenols correlated well with the ability of proteins to form insoluble complexes with oxidized catechins. Cross-linking of proteins and polyphenols further extended the half-lives of BLG and LA in the in vitro digestion by pepsin. Catechin-enriched green tea polyphenols of food supplements facilitate pepsin digestion of major food allergens, but hamper their digestion if oxidized and polymerized by phenol oxidase. (c) 2012 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Functional Foods",
title = "Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase",
volume = "4",
number = "3",
pages = "650-660",
doi = "10.1016/j.jff.2012.04.006"
}
Tantoush, Z., Apostolović, D., Kravić, B., Prodić, I., Mihajlovic, L., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2012). Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase.
Journal of Functional Foods
Elsevier Science Bv, Amsterdam., 4(3), 650-660.
https://doi.org/10.1016/j.jff.2012.04.006
Tantoush Z, Apostolović D, Kravić B, Prodić I, Mihajlovic L, Stanić-Vučinić D, Ćirković-Veličković T. Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase. Journal of Functional Foods. 2012;4(3):650-660
Tantoush Ziyad, Apostolović Danijela, Kravić Bojana, Prodić Ivana, Mihajlovic Luka, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase" Journal of Functional Foods, 4, no. 3 (2012):650-660,
https://doi.org/10.1016/j.jff.2012.04.006 .
36
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