FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics

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FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (en)
Authors

Publications

Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix

Khulal, Urmila; Stojadinović, Marija M.; Prodić, Ivana; Rajković, Andrea; Ćirković-Veličković, Tanja

(Elsevier, 2023)

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

Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating

Radomirović, Mirjana Ž.; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Van Haute, Sam; Rajković, Andreja; Ćirković-Veličković, Tanja

(Elsevier, 2022)

TY  - JOUR
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Van Haute, Sam
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4863
AB  - β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.
PB  - Elsevier
T2  - Food Hydrocolloids
T1  - Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating
VL  - 123
SP  - 107169
DO  - 10.1016/j.foodhyd.2021.107169
ER  - 
@article{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Van Haute, Sam and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.",
publisher = "Elsevier",
journal = "Food Hydrocolloids",
title = "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating",
volume = "123",
pages = "107169",
doi = "10.1016/j.foodhyd.2021.107169"
}
Radomirović, M. Ž., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Van Haute, S., Rajković, A.,& Ćirković-Veličković, T.. (2022). Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids
Elsevier., 123, 107169.
https://doi.org/10.1016/j.foodhyd.2021.107169
Radomirović MŽ, Minić SL, Stanić-Vučinić D, Nikolić M, Van Haute S, Rajković A, Ćirković-Veličković T. Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids. 2022;123:107169.
doi:10.1016/j.foodhyd.2021.107169 .
Radomirović, Mirjana Ž., Minić, Simeon L., Stanić-Vučinić, Dragana, Nikolić, Milan, Van Haute, Sam, Rajković, Andreja, Ćirković-Veličković, Tanja, "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating" in Food Hydrocolloids, 123 (2022):107169,
https://doi.org/10.1016/j.foodhyd.2021.107169 . .
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7
7

Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain

Simović, Ana; Radomirović, Mirjana Ž.; Gligorijević, Nikola; Stanić-Vučinić, Dragana; Minić, Simeon L.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Faculty of Chemistry, Serbian Biochemical Society, 2022)

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Minić, Simeon L.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5520
AB  - The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
T1  - Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain
SP  - 130
EP  - 131
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5520
ER  - 
@conference{
author = "Simović, Ana and Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Minić, Simeon L. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain",
pages = "130-131",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5520"
}
Simović, A., Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Minić, S. L., Nikolić, M.,& Ćirković-Veličković, T.. (2022). Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
Faculty of Chemistry, Serbian Biochemical Society., 130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520
Simović A, Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Minić SL, Nikolić M, Ćirković-Veličković T. Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia. 2022;:130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520 .
Simović, Ana, Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Minić, Simeon L., Nikolić, Milan, Ćirković-Veličković, Tanja, "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain" in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia (2022):130-131,
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting

Đukić, Teodora; Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Apostolović, Danijela; Liu, Shu-Hua; Epstein, Michelle M.; van Hage, Marianne; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5781
AB  - : Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs
PB  - MDPI
T2  - Foods
T1  - Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
VL  - 11
IS  - 24
SP  - 3993
DO  - 10.3390/foods11243993
ER  - 
@article{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = ": Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs",
publisher = "MDPI",
journal = "Foods",
title = "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting",
volume = "11",
number = "24",
pages = "3993",
doi = "10.3390/foods11243993"
}
Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods
MDPI., 11(24), 3993.
https://doi.org/10.3390/foods11243993
Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods. 2022;11(24):3993.
doi:10.3390/foods11243993 .
Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting" in Foods, 11, no. 24 (2022):3993,
https://doi.org/10.3390/foods11243993 . .

Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting

Đukić, Teodora; Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Apostolović, Danijela; Liu, Shu-Hua; Epstein, Michelle M.; van Hage, Marianne; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5702
AB  - Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
PB  - MDPI
T2  - Foods
T1  - Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
VL  - 11
IS  - 24
EP  - 3993
DO  - 10.3390/foods11243993
ER  - 
@article{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.",
publisher = "MDPI",
journal = "Foods",
title = "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting",
volume = "11",
number = "24",
pages = "3993",
doi = "10.3390/foods11243993"
}
Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods
MDPI., 11(24).
https://doi.org/10.3390/foods11243993
Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods. 2022;11(24):null-3993.
doi:10.3390/foods11243993 .
Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting" in Foods, 11, no. 24 (2022),
https://doi.org/10.3390/foods11243993 . .

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

Đukić, Teodora; Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Apostolović, Danijela; Liu, Shu-Hua; Epstein, Michelle M.; van Hage, Marianne; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - DATA
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5708
AB  - Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
PB  - MDPI
T2  - Foods
T1  - Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993
VL  - 11
IS  - 24
EP  - 3993
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5708
ER  - 
@misc{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993",
volume = "11",
number = "24",
pages = "3993",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5708"
}
Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods
MDPI., 11(24).
https://hdl.handle.net/21.15107/rcub_cherry_5708
Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods. 2022;11(24):null-3993.
https://hdl.handle.net/21.15107/rcub_cherry_5708 .
Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993" in Foods, 11, no. 24 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5708 .

Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk

Radosavljević, Jelena; Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Radomirović, Mirjana Ž.; Simović, Ana; Radibratović, Milica; Ćirković-Veličković, Tanja

(Bentham Science, 2022)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4883
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4883
ER  - 
@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4883"
}
Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883
Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883 .
Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4883 .
2
1
1

Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Radomirović, Mirjana Ž.; Simović, Ana; Radibratović, Milica; Ćirković-Veličković, Tanja

(Bentham Science, 2022)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4884
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4884
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4884"
}
Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884
Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884 .
Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4884 .
2
1
1

Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes

Simović, Ana; Combet, Sophie; Ćirković-Veličković, Tanja; Nikolic, Milan; Minic, Simeon

(Sociedade Portuguesa de Química, 2022)

TY  - CONF
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minic, Simeon
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5133
AB  - The high content of vitamins, minerals, antioxidants, and proteins makes red algae Porphyra sp. (Nori) superfood with exceptional health-promoting benefits. Its intense colour originates from R-phycoerythrin (R-PE), phycobiliprotein containing covalently attached tetrapyrrole chromophores: red phycoerythrobilin and orange phycourobilin. The present study aims to characterize the stability of R-PE, a natural colourant with a high potential for application in the food, cosmetic, and pharmaceutical industries. We purified R-PE from dried Nori flakes with a high purity ratio (A560 /A280 ≥5). Far-UV CD spectroscopic showed that α-helix is the dominant secondary structure (75%). The thermal unfolding of α-helix revealed two transitions (Tm1 and Tm2 at 56 and 72°C, respectively), ascribed to the different subunits of R-PE. Absorption measurements showed that high pressure (HP) induces dissociation of R-PE into subunits followed by subunit unfolding. Contrary to temperature, HP treatment showed a significant advantage under applied conditions: the protein unfolding is partly reversible, and the R-PE colour bleaching is minimized. Based on the fluorescence quenching approach, R-PE's binding affinities for Cu2+ and Zn2+ ions were 6.27x105 and 1.71x103 M-1, respectively. Absorption and near-UV/VIS CD spectroscopy suggested conformational changes in protein chromophores upon metal ions binding. Far-UV CD spectroscopy did not reveal that metal binding affects R-PE structure. The obtained results give new insights into the stability of R-PE with a good use-value in replacement of toxic synthetic dyes, preservation of R-PE red colour in fortified food and beverages by HP processing, and as a biosensor for Cu2+ in aquatic life systems.
Acknowledgments: This study was financially supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, Contract number: 451-03-9/2021-14/200168 and the European Commission, under the Horizon2020, FoodEnTwin Project, GA No. 810752.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
T1  - Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes
SP  - 138
EP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5133
ER  - 
@conference{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minic, Simeon",
year = "2022",
abstract = "The high content of vitamins, minerals, antioxidants, and proteins makes red algae Porphyra sp. (Nori) superfood with exceptional health-promoting benefits. Its intense colour originates from R-phycoerythrin (R-PE), phycobiliprotein containing covalently attached tetrapyrrole chromophores: red phycoerythrobilin and orange phycourobilin. The present study aims to characterize the stability of R-PE, a natural colourant with a high potential for application in the food, cosmetic, and pharmaceutical industries. We purified R-PE from dried Nori flakes with a high purity ratio (A560 /A280 ≥5). Far-UV CD spectroscopic showed that α-helix is the dominant secondary structure (75%). The thermal unfolding of α-helix revealed two transitions (Tm1 and Tm2 at 56 and 72°C, respectively), ascribed to the different subunits of R-PE. Absorption measurements showed that high pressure (HP) induces dissociation of R-PE into subunits followed by subunit unfolding. Contrary to temperature, HP treatment showed a significant advantage under applied conditions: the protein unfolding is partly reversible, and the R-PE colour bleaching is minimized. Based on the fluorescence quenching approach, R-PE's binding affinities for Cu2+ and Zn2+ ions were 6.27x105 and 1.71x103 M-1, respectively. Absorption and near-UV/VIS CD spectroscopy suggested conformational changes in protein chromophores upon metal ions binding. Far-UV CD spectroscopy did not reveal that metal binding affects R-PE structure. The obtained results give new insights into the stability of R-PE with a good use-value in replacement of toxic synthetic dyes, preservation of R-PE red colour in fortified food and beverages by HP processing, and as a biosensor for Cu2+ in aquatic life systems.
Acknowledgments: This study was financially supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, Contract number: 451-03-9/2021-14/200168 and the European Commission, under the Horizon2020, FoodEnTwin Project, GA No. 810752.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference",
title = "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes",
pages = "138-138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5133"
}
Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minic, S.. (2022). Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
Sociedade Portuguesa de Química., 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5133
Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minic S. Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5133 .
Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minic, Simeon, "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes" in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5133 .

Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells

Ljujic, Mila; Trifunović, Sara; Smiljanić, Katarina; Solari, Fiorella Andrea; Sickmann, Albert; Divac Rankov, Aleksandra

(European Respiraotory Society (ERS), 2022)

TY  - CONF
AU  - Ljujic, Mila
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Solari, Fiorella Andrea
AU  - Sickmann, Albert
AU  - Divac Rankov, Aleksandra
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5731
AB  - The COVID-19 pandemic caused by the SARS-CoV2 virus poses a global health threat with over 5 million deaths recorded. There is little understanding regarding SARS-CoV2 pathogenesis in the human airways and disease severity increases with age. Neutrophils are white blood cells found in large numbers in the airways of the lungs in severe COVID-19 patients. It is not known whether this influx of neutrophils into the airway has a protective or detrimental effect. We aim to understand the role of neutrophils during COVID-19 pathology, using an experimental infection model of the airway epithelium from the eldelry and children. To do this, we collect nasal airway cells from healthy elderly and children and grow them at air-liquid interface. Once differentiation and ciliation of these cells is reached, we infect the cells with SARS-CoV2 virus and allow neutrophils to migrate from the basolateral (blood) to the apical (air) side of the epithelium, similar to a physiological airway. Using flow cytometric analyses, we measure the expression of activation markers and the number of neutrophils that migrate across the epithelium of different ages in response to SARS-CoV2 infection. Preliminary work shows less viable neutrophils recovered from the elderly epithelium, more activated neutrophils when migrating through the elderly epithelium, as well as increased numbers of neutrophils remaining on the basolateral (blood) side of the elderly epithelium. These findings point to an inflammatory neutrophil phenotype influenced by the damaged elderly epithelium and supports the hypothesis that neutrophils are responsible for the severity of disease.
PB  - European Respiraotory Society (ERS)
C3  - European Respiratory Journal
T1  - Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells
VL  - 60
IS  - 66
SP  - 506
DO  - 10.1183/13993003.congress-2022.506
ER  - 
@conference{
author = "Ljujic, Mila and Trifunović, Sara and Smiljanić, Katarina and Solari, Fiorella Andrea and Sickmann, Albert and Divac Rankov, Aleksandra",
year = "2022",
abstract = "The COVID-19 pandemic caused by the SARS-CoV2 virus poses a global health threat with over 5 million deaths recorded. There is little understanding regarding SARS-CoV2 pathogenesis in the human airways and disease severity increases with age. Neutrophils are white blood cells found in large numbers in the airways of the lungs in severe COVID-19 patients. It is not known whether this influx of neutrophils into the airway has a protective or detrimental effect. We aim to understand the role of neutrophils during COVID-19 pathology, using an experimental infection model of the airway epithelium from the eldelry and children. To do this, we collect nasal airway cells from healthy elderly and children and grow them at air-liquid interface. Once differentiation and ciliation of these cells is reached, we infect the cells with SARS-CoV2 virus and allow neutrophils to migrate from the basolateral (blood) to the apical (air) side of the epithelium, similar to a physiological airway. Using flow cytometric analyses, we measure the expression of activation markers and the number of neutrophils that migrate across the epithelium of different ages in response to SARS-CoV2 infection. Preliminary work shows less viable neutrophils recovered from the elderly epithelium, more activated neutrophils when migrating through the elderly epithelium, as well as increased numbers of neutrophils remaining on the basolateral (blood) side of the elderly epithelium. These findings point to an inflammatory neutrophil phenotype influenced by the damaged elderly epithelium and supports the hypothesis that neutrophils are responsible for the severity of disease.",
publisher = "European Respiraotory Society (ERS)",
journal = "European Respiratory Journal",
title = "Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells",
volume = "60",
number = "66",
pages = "506",
doi = "10.1183/13993003.congress-2022.506"
}
Ljujic, M., Trifunović, S., Smiljanić, K., Solari, F. A., Sickmann, A.,& Divac Rankov, A.. (2022). Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells. in European Respiratory Journal
European Respiraotory Society (ERS)., 60(66), 506.
https://doi.org/10.1183/13993003.congress-2022.506
Ljujic M, Trifunović S, Smiljanić K, Solari FA, Sickmann A, Divac Rankov A. Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells. in European Respiratory Journal. 2022;60(66):506.
doi:10.1183/13993003.congress-2022.506 .
Ljujic, Mila, Trifunović, Sara, Smiljanić, Katarina, Solari, Fiorella Andrea, Sickmann, Albert, Divac Rankov, Aleksandra, "Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells" in European Respiratory Journal, 60, no. 66 (2022):506,
https://doi.org/10.1183/13993003.congress-2022.506 . .

Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu

Bajkanović, Dragana

(2022)

TY  - THES
AU  - Bajkanović, Dragana
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5469
AB  - Cilj ovog rada je bio ispitati regioselektivnost Zr-Wells-Dawson 1:2 polioksometalata (Zr-WD 1:2) na β-laktoglobulinu (BLG) kao model proteinu. Literaturni podaci ukazuju na selektivnost ka kiselim aminokiselinama, kao što su aspartat i glutamat. Kako bismo dobili što pouzdanije rezultate u radu su korišteni nativni BLG (smjesa A i B izoforme), redukovan i alkilovan BLG i pojedinačne izoforme A i B. Rezultati dobijeni reakcijom sa Zr-WD 1:2 ukazuju da dolazi do hidrolize i da je elektroforetski profil različit za sve ispitivane tipove BLG. Zbog uslova reakcije (7 dana na 60 °C) dolazi i do autolize tako da krajnji efekat jeste kombinovani efekat autolize i dejstva Zr-WD 1:2. Bitno za naglasiti jeste to da nakon 24 časa na elektroforetskim profilma se javljaju proizvodi hidrolize, dok autoliza izostaje. Takođe, rezultati su pokazali da Zr-WD 1:2 ne ispoljava isključivu selektivnost ka kiselim aminokiselinama (aspartatu i glutamatu) već dolazi do hidrolize i na drugim aminokiselinama što nije u skladu sa literaturnim podacima u uzorku redukovanog i alkilovanog BLG.
T1  - Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu
SP  - 1
EP  - 67
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5469
ER  - 
@mastersthesis{
author = "Bajkanović, Dragana",
year = "2022",
abstract = "Cilj ovog rada je bio ispitati regioselektivnost Zr-Wells-Dawson 1:2 polioksometalata (Zr-WD 1:2) na β-laktoglobulinu (BLG) kao model proteinu. Literaturni podaci ukazuju na selektivnost ka kiselim aminokiselinama, kao što su aspartat i glutamat. Kako bismo dobili što pouzdanije rezultate u radu su korišteni nativni BLG (smjesa A i B izoforme), redukovan i alkilovan BLG i pojedinačne izoforme A i B. Rezultati dobijeni reakcijom sa Zr-WD 1:2 ukazuju da dolazi do hidrolize i da je elektroforetski profil različit za sve ispitivane tipove BLG. Zbog uslova reakcije (7 dana na 60 °C) dolazi i do autolize tako da krajnji efekat jeste kombinovani efekat autolize i dejstva Zr-WD 1:2. Bitno za naglasiti jeste to da nakon 24 časa na elektroforetskim profilma se javljaju proizvodi hidrolize, dok autoliza izostaje. Takođe, rezultati su pokazali da Zr-WD 1:2 ne ispoljava isključivu selektivnost ka kiselim aminokiselinama (aspartatu i glutamatu) već dolazi do hidrolize i na drugim aminokiselinama što nije u skladu sa literaturnim podacima u uzorku redukovanog i alkilovanog BLG.",
title = "Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu",
pages = "1-67",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5469"
}
Bajkanović, D.. (2022). Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu. , 1-67.
https://hdl.handle.net/21.15107/rcub_cherry_5469
Bajkanović D. Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu. 2022;:1-67.
https://hdl.handle.net/21.15107/rcub_cherry_5469 .
Bajkanović, Dragana, "Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu" (2022):1-67,
https://hdl.handle.net/21.15107/rcub_cherry_5469 .

New applications of advanced instrumental techniques for the characterization of food allergenic proteins

Benedé, Sara; Lozano-Ojalvo, Daniel; Cristobal, Susana; Costa, Joana; D’Auria, Enza; Ćirković-Veličković, Tanja; Garrido-Arandia, María; Karakaya, Sibel; Mafra, Isabel; Mazzucchelli, Gabriel; Picariello, Gianluca; Romero-Sahagun, Alejandro; Villa, Caterina; Roncada, Paola; Molina, Elena

(Taylor & Francis Group, 2022)

TY  - JOUR
AU  - Benedé, Sara
AU  - Lozano-Ojalvo, Daniel
AU  - Cristobal, Susana
AU  - Costa, Joana
AU  - D’Auria, Enza
AU  - Ćirković-Veličković, Tanja
AU  - Garrido-Arandia, María
AU  - Karakaya, Sibel
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Picariello, Gianluca
AU  - Romero-Sahagun, Alejandro
AU  - Villa, Caterina
AU  - Roncada, Paola
AU  - Molina, Elena
PY  - 2022
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4548
AB  - Current approaches based on electrophoretic, chromatographic or immunochemical principles have allowed characterizing multiple allergens, mapping their epitopes, studying their mechanisms of action, developing detection and diagnostic methods and therapeutic strategies for the food and pharmaceutical industry. However, some of the common structural features related to the allergenic potential of food proteins remain unknown, or the pathological mechanism of food allergy is not yet fully understood. In addition, it is also necessary to evaluate new allergens from novel protein sources that may pose a new risk for consumers. Technological development has allowed the expansion of advanced technologies for which their whole potential has not been entirely exploited and could provide novel contributions to still unexplored molecular traits underlying both the structure of food allergens and the mechanisms through which they sensitize or elicit adverse responses in human subjects, as well as improving analytical techniques for their detection. This review presents cutting-edge instrumental techniques recently applied when studying structural and functional aspects of proteins, mechanism of action and interaction between biomolecules. We also exemplify their role in the food allergy research and discuss their new possible applications in several areas of the food allergy field.
PB  - Taylor & Francis Group
T2  - Critical Reviews in Food Science and Nutrition
T1  - New applications of advanced instrumental techniques for the characterization of food allergenic proteins
VL  - 62
IS  - 31
DO  - 10.1080/10408398.2021.1931806
ER  - 
@article{
author = "Benedé, Sara and Lozano-Ojalvo, Daniel and Cristobal, Susana and Costa, Joana and D’Auria, Enza and Ćirković-Veličković, Tanja and Garrido-Arandia, María and Karakaya, Sibel and Mafra, Isabel and Mazzucchelli, Gabriel and Picariello, Gianluca and Romero-Sahagun, Alejandro and Villa, Caterina and Roncada, Paola and Molina, Elena",
year = "2022",
abstract = "Current approaches based on electrophoretic, chromatographic or immunochemical principles have allowed characterizing multiple allergens, mapping their epitopes, studying their mechanisms of action, developing detection and diagnostic methods and therapeutic strategies for the food and pharmaceutical industry. However, some of the common structural features related to the allergenic potential of food proteins remain unknown, or the pathological mechanism of food allergy is not yet fully understood. In addition, it is also necessary to evaluate new allergens from novel protein sources that may pose a new risk for consumers. Technological development has allowed the expansion of advanced technologies for which their whole potential has not been entirely exploited and could provide novel contributions to still unexplored molecular traits underlying both the structure of food allergens and the mechanisms through which they sensitize or elicit adverse responses in human subjects, as well as improving analytical techniques for their detection. This review presents cutting-edge instrumental techniques recently applied when studying structural and functional aspects of proteins, mechanism of action and interaction between biomolecules. We also exemplify their role in the food allergy research and discuss their new possible applications in several areas of the food allergy field.",
publisher = "Taylor & Francis Group",
journal = "Critical Reviews in Food Science and Nutrition",
title = "New applications of advanced instrumental techniques for the characterization of food allergenic proteins",
volume = "62",
number = "31",
doi = "10.1080/10408398.2021.1931806"
}
Benedé, S., Lozano-Ojalvo, D., Cristobal, S., Costa, J., D’Auria, E., Ćirković-Veličković, T., Garrido-Arandia, M., Karakaya, S., Mafra, I., Mazzucchelli, G., Picariello, G., Romero-Sahagun, A., Villa, C., Roncada, P.,& Molina, E.. (2022). New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition
Taylor & Francis Group., 62(31).
https://doi.org/10.1080/10408398.2021.1931806
Benedé S, Lozano-Ojalvo D, Cristobal S, Costa J, D’Auria E, Ćirković-Veličković T, Garrido-Arandia M, Karakaya S, Mafra I, Mazzucchelli G, Picariello G, Romero-Sahagun A, Villa C, Roncada P, Molina E. New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition. 2022;62(31).
doi:10.1080/10408398.2021.1931806 .
Benedé, Sara, Lozano-Ojalvo, Daniel, Cristobal, Susana, Costa, Joana, D’Auria, Enza, Ćirković-Veličković, Tanja, Garrido-Arandia, María, Karakaya, Sibel, Mafra, Isabel, Mazzucchelli, Gabriel, Picariello, Gianluca, Romero-Sahagun, Alejandro, Villa, Caterina, Roncada, Paola, Molina, Elena, "New applications of advanced instrumental techniques for the characterization of food allergenic proteins" in Critical Reviews in Food Science and Nutrition, 62, no. 31 (2022),
https://doi.org/10.1080/10408398.2021.1931806 . .
1
7
2
8

Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells

Trifunović, Sara; Smiljanić, Katarina; Sickmann, Albert; Solari, Fiorella Andrea; Kolarević, Stoimir; Divac Rankov, Aleksandra; Ljujic, Mila

(BMC Springer Nature, 2022)

TY  - JOUR
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Sickmann, Albert
AU  - Solari, Fiorella Andrea
AU  - Kolarević, Stoimir
AU  - Divac Rankov, Aleksandra
AU  - Ljujic, Mila
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5458
AB  - Abstract
Background: Although still considered a safer alternative to classical cigarettes, growing body of work points to
harmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect of
e-cigarettes needs to be investigated in more detail considering their widespread use.
Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, with
and without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-
lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performed
via high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.
Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however it
negatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletion
in total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteins
were upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-
translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data are
available via ProteomeXchange with identifier PXD032071.
Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMs
alterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.
PB  - BMC Springer Nature
T2  - Respiratory Research
T1  - Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells
VL  - 23
IS  - 191
DO  - 10.1186/s12931-022-02102-w
ER  - 
@article{
author = "Trifunović, Sara and Smiljanić, Katarina and Sickmann, Albert and Solari, Fiorella Andrea and Kolarević, Stoimir and Divac Rankov, Aleksandra and Ljujic, Mila",
year = "2022",
abstract = "Abstract
Background: Although still considered a safer alternative to classical cigarettes, growing body of work points to
harmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect of
e-cigarettes needs to be investigated in more detail considering their widespread use.
Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, with
and without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-
lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performed
via high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.
Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however it
negatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletion
in total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteins
were upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-
translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data are
available via ProteomeXchange with identifier PXD032071.
Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMs
alterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.",
publisher = "BMC Springer Nature",
journal = "Respiratory Research",
title = "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells",
volume = "23",
number = "191",
doi = "10.1186/s12931-022-02102-w"
}
Trifunović, S., Smiljanić, K., Sickmann, A., Solari, F. A., Kolarević, S., Divac Rankov, A.,& Ljujic, M.. (2022). Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research
BMC Springer Nature., 23(191).
https://doi.org/10.1186/s12931-022-02102-w
Trifunović S, Smiljanić K, Sickmann A, Solari FA, Kolarević S, Divac Rankov A, Ljujic M. Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research. 2022;23(191).
doi:10.1186/s12931-022-02102-w .
Trifunović, Sara, Smiljanić, Katarina, Sickmann, Albert, Solari, Fiorella Andrea, Kolarević, Stoimir, Divac Rankov, Aleksandra, Ljujic, Mila, "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells" in Respiratory Research, 23, no. 191 (2022),
https://doi.org/10.1186/s12931-022-02102-w . .
9

Ligand binding to fibrinogen influences its structure and function

Gligorijević, Nikola; Minić, Simeon L.; Radomirović, Mirjana Ž.; Lević, Steva M.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(University of Novi Sad - Faculty of Sciences, Department of Biology, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Lević, Steva M.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4862
AB  - Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.
PB  - University of Novi Sad - Faculty of Sciences, Department of Biology
T2  - Biologia Serbica
T1  - Ligand binding to fibrinogen influences its structure and function
VL  - 43
IS  - 1
DO  - 10.5281/zenodo.5512285
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Radomirović, Mirjana Ž. and Lević, Steva M. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2021",
abstract = "Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.",
publisher = "University of Novi Sad - Faculty of Sciences, Department of Biology",
journal = "Biologia Serbica",
title = "Ligand binding to fibrinogen influences its structure and function",
volume = "43",
number = "1",
doi = "10.5281/zenodo.5512285"
}
Gligorijević, N., Minić, S. L., Radomirović, M. Ž., Lević, S. M., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2021). Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica
University of Novi Sad - Faculty of Sciences, Department of Biology., 43(1).
https://doi.org/10.5281/zenodo.5512285
Gligorijević N, Minić SL, Radomirović MŽ, Lević SM, Nikolić M, Ćirković-Veličković T, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica. 2021;43(1).
doi:10.5281/zenodo.5512285 .
Gligorijević, Nikola, Minić, Simeon L., Radomirović, Mirjana Ž., Lević, Steva M., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Ligand binding to fibrinogen influences its structure and function" in Biologia Serbica, 43, no. 1 (2021),
https://doi.org/10.5281/zenodo.5512285 . .

Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli

Đukić, Teodora; Mladenović, Maja; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Smiljanić, Katarina; Sabljić, Ljiljana; Gnjatović, Marija Lj.; Cujić, Danica; Vasović, Tamara; Simović, Ana; Radomirović, Mirjana Ž.; Ćirković-Veličković, Tanja

(2021)

TY  - CONF
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Gnjatović, Marija Lj.
AU  - Cujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5735
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection and for assessment of immunological response after the vaccination. Nucleocapsid (N) protein is the most abundant virus protein and strong immunogen. The aim was develop efficient, low-cost production of N protein large fragment and to characterize it with bottom-up, high-resolution tandem mass spectrometry and immunologically.
SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form and purified by several chromatographic steps and was subjected to SDS-PAGE and in-gel digested with trypsin.
rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower. Identity of rfNP was confirmed with high scores and peptide coverage above 80%. Estimation from the value of areas under ion extracted chromatographic curves is that only up to 0,03% of the total band protein quantity belongs to host proteins, while rfNP share is well above 99,9%, resulting in highly pure nucleocapsid protein preparation.
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli
SP  - 50
EP  - 50
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5735
ER  - 
@conference{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Gnjatović, Marija Lj. and Cujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection and for assessment of immunological response after the vaccination. Nucleocapsid (N) protein is the most abundant virus protein and strong immunogen. The aim was develop efficient, low-cost production of N protein large fragment and to characterize it with bottom-up, high-resolution tandem mass spectrometry and immunologically.
SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form and purified by several chromatographic steps and was subjected to SDS-PAGE and in-gel digested with trypsin.
rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower. Identity of rfNP was confirmed with high scores and peptide coverage above 80%. Estimation from the value of areas under ion extracted chromatographic curves is that only up to 0,03% of the total band protein quantity belongs to host proteins, while rfNP share is well above 99,9%, resulting in highly pure nucleocapsid protein preparation.",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli",
pages = "50-50",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5735"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Gnjatović, M. Lj., Cujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 50-50.
https://hdl.handle.net/21.15107/rcub_cherry_5735
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Gnjatović ML, Cujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:50-50.
https://hdl.handle.net/21.15107/rcub_cherry_5735 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Gnjatović, Marija Lj., Cujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):50-50,
https://hdl.handle.net/21.15107/rcub_cherry_5735 .

Life cycle assessment of edible insects (Protaetia brevitarsis seulensis larvae) as a future protein and fat source

Nikkhah, Amin; Van Haute, Sam; Jovanović, Vesna B.; Jung, Heejung; Dewulf, Jo; Ćirković-Veličković, Tanja; Ghnimi, Sami

(Springer Nature, 2021)

TY  - JOUR
AU  - Nikkhah, Amin
AU  - Van Haute, Sam
AU  - Jovanović, Vesna B.
AU  - Jung, Heejung
AU  - Dewulf, Jo
AU  - Ćirković-Veličković, Tanja
AU  - Ghnimi, Sami
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4584
AB  - Because it is important to develop new sustainable sources of edible protein, insects have been recommended as a new protein source. This study applied Life Cycle Assessment (LCA) to investigate the environmental impact of small-scale edible insect production unit in South Korea. IMPACT 2002 + was applied as the baseline impact assessment (IA) methodology. The CML-IA baseline, EDIP 2003, EDP 2013, ILCD 2011 Midpoint, and ReCiPe midpoint IA methodologies were also used for LCIA methodology sensitivity analysis. The protein, fat contents, and fatty acid profile of the investigated insect (Protaetia brevitarsis seulensis larvae) were analyzed to determine its potential food application. The results revealed that the studied edible insect production system has beneficial environmental effects on various impact categories (ICs), i.e., land occupation, mineral extraction, aquatic and terrestrial ecotoxicity, due to utilization of bio-waste to feed insects. This food production system can mitigate the negative environmental effects of those ICs, but has negative environmental impact on some other ICs such as global warming potential. By managing the consumption of various inputs, edible insects can become an environmentally efficient food production system for human nutrition.
PB  - Springer Nature
T2  - Scientific Reports
T1  - Life cycle assessment of edible insects (Protaetia brevitarsis seulensis larvae) as a future protein and fat source
VL  - 11
IS  - 1
SP  - 14030
DO  - 10.1038/s41598-021-93284-8
ER  - 
@article{
author = "Nikkhah, Amin and Van Haute, Sam and Jovanović, Vesna B. and Jung, Heejung and Dewulf, Jo and Ćirković-Veličković, Tanja and Ghnimi, Sami",
year = "2021",
abstract = "Because it is important to develop new sustainable sources of edible protein, insects have been recommended as a new protein source. This study applied Life Cycle Assessment (LCA) to investigate the environmental impact of small-scale edible insect production unit in South Korea. IMPACT 2002 + was applied as the baseline impact assessment (IA) methodology. The CML-IA baseline, EDIP 2003, EDP 2013, ILCD 2011 Midpoint, and ReCiPe midpoint IA methodologies were also used for LCIA methodology sensitivity analysis. The protein, fat contents, and fatty acid profile of the investigated insect (Protaetia brevitarsis seulensis larvae) were analyzed to determine its potential food application. The results revealed that the studied edible insect production system has beneficial environmental effects on various impact categories (ICs), i.e., land occupation, mineral extraction, aquatic and terrestrial ecotoxicity, due to utilization of bio-waste to feed insects. This food production system can mitigate the negative environmental effects of those ICs, but has negative environmental impact on some other ICs such as global warming potential. By managing the consumption of various inputs, edible insects can become an environmentally efficient food production system for human nutrition.",
publisher = "Springer Nature",
journal = "Scientific Reports",
title = "Life cycle assessment of edible insects (Protaetia brevitarsis seulensis larvae) as a future protein and fat source",
volume = "11",
number = "1",
pages = "14030",
doi = "10.1038/s41598-021-93284-8"
}
Nikkhah, A., Van Haute, S., Jovanović, V. B., Jung, H., Dewulf, J., Ćirković-Veličković, T.,& Ghnimi, S.. (2021). Life cycle assessment of edible insects (Protaetia brevitarsis seulensis larvae) as a future protein and fat source. in Scientific Reports
Springer Nature., 11(1), 14030.
https://doi.org/10.1038/s41598-021-93284-8
Nikkhah A, Van Haute S, Jovanović VB, Jung H, Dewulf J, Ćirković-Veličković T, Ghnimi S. Life cycle assessment of edible insects (Protaetia brevitarsis seulensis larvae) as a future protein and fat source. in Scientific Reports. 2021;11(1):14030.
doi:10.1038/s41598-021-93284-8 .
Nikkhah, Amin, Van Haute, Sam, Jovanović, Vesna B., Jung, Heejung, Dewulf, Jo, Ćirković-Veličković, Tanja, Ghnimi, Sami, "Life cycle assessment of edible insects (Protaetia brevitarsis seulensis larvae) as a future protein and fat source" in Scientific Reports, 11, no. 1 (2021):14030,
https://doi.org/10.1038/s41598-021-93284-8 . .
23
9
2
8

Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)

Nikkhah, Amin; Van Haute, Sam; Jovanović, Vesna B.; Jung, Heejung; Dewulf, Jo; Ćirković-Veličković, Tanja; Ghnimi, Sami

(Springer Nature, 2021)

TY  - JOUR
AU  - Nikkhah, Amin
AU  - Van Haute, Sam
AU  - Jovanović, Vesna B.
AU  - Jung, Heejung
AU  - Dewulf, Jo
AU  - Ćirković-Veličković, Tanja
AU  - Ghnimi, Sami
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4586
AB  - In the original version of this Article, Sam Van Haute and Sami Ghnimi were omitted as corresponding authors.
Correspondence and requests for materials should also be addressed to sam.vanhaute@ghent.ac.kr and sghnimi@
isara.fr.
The original Article has been corrected.
PB  - Springer Nature
T2  - Scientific Reports
T1  - Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)
VL  - 11
IS  - 1
SP  - 14030
DO  - 10.1038/s41598-021-97513-y
ER  - 
@article{
author = "Nikkhah, Amin and Van Haute, Sam and Jovanović, Vesna B. and Jung, Heejung and Dewulf, Jo and Ćirković-Veličković, Tanja and Ghnimi, Sami",
year = "2021",
abstract = "In the original version of this Article, Sam Van Haute and Sami Ghnimi were omitted as corresponding authors.
Correspondence and requests for materials should also be addressed to sam.vanhaute@ghent.ac.kr and sghnimi@
isara.fr.
The original Article has been corrected.",
publisher = "Springer Nature",
journal = "Scientific Reports",
title = "Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)",
volume = "11",
number = "1",
pages = "14030",
doi = "10.1038/s41598-021-97513-y"
}
Nikkhah, A., Van Haute, S., Jovanović, V. B., Jung, H., Dewulf, J., Ćirković-Veličković, T.,& Ghnimi, S.. (2021). Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8). in Scientific Reports
Springer Nature., 11(1), 14030.
https://doi.org/10.1038/s41598-021-97513-y
Nikkhah A, Van Haute S, Jovanović VB, Jung H, Dewulf J, Ćirković-Veličković T, Ghnimi S. Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8). in Scientific Reports. 2021;11(1):14030.
doi:10.1038/s41598-021-97513-y .
Nikkhah, Amin, Van Haute, Sam, Jovanović, Vesna B., Jung, Heejung, Dewulf, Jo, Ćirković-Veličković, Tanja, Ghnimi, Sami, "Correction to:  Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)" in Scientific Reports, 11, no. 1 (2021):14030,
https://doi.org/10.1038/s41598-021-97513-y . .

Supplementary data for the article: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. https://doi.org/10.1038/S41598-021-93284-8).

Nikkhah, Amin; Van Haute, Sam; Jovanović, Vesna B.; Jung, Heejung; Dewulf, Jo; Ćirković-Veličković, Tanja; Ghnimi, Sami

(Springer Nature, 2021)

TY  - DATA
AU  - Nikkhah, Amin
AU  - Van Haute, Sam
AU  - Jovanović, Vesna B.
AU  - Jung, Heejung
AU  - Dewulf, Jo
AU  - Ćirković-Veličković, Tanja
AU  - Ghnimi, Sami
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4587
PB  - Springer Nature
T2  - Scientific Reports
T1  - Supplementary data for the article: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. https://doi.org/10.1038/S41598-021-93284-8).
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4587
ER  - 
@misc{
author = "Nikkhah, Amin and Van Haute, Sam and Jovanović, Vesna B. and Jung, Heejung and Dewulf, Jo and Ćirković-Veličković, Tanja and Ghnimi, Sami",
year = "2021",
publisher = "Springer Nature",
journal = "Scientific Reports",
title = "Supplementary data for the article: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. https://doi.org/10.1038/S41598-021-93284-8).",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4587"
}
Nikkhah, A., Van Haute, S., Jovanović, V. B., Jung, H., Dewulf, J., Ćirković-Veličković, T.,& Ghnimi, S.. (2021). Supplementary data for the article: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. https://doi.org/10.1038/S41598-021-93284-8).. in Scientific Reports
Springer Nature..
https://hdl.handle.net/21.15107/rcub_cherry_4587
Nikkhah A, Van Haute S, Jovanović VB, Jung H, Dewulf J, Ćirković-Veličković T, Ghnimi S. Supplementary data for the article: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. https://doi.org/10.1038/S41598-021-93284-8).. in Scientific Reports. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4587 .
Nikkhah, Amin, Van Haute, Sam, Jovanović, Vesna B., Jung, Heejung, Dewulf, Jo, Ćirković-Veličković, Tanja, Ghnimi, Sami, "Supplementary data for the article: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. https://doi.org/10.1038/S41598-021-93284-8)." in Scientific Reports (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4587 .

Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation

Mutić, Jelena; Jovanović, Vesna B.; Jacxsens, Liesbeth; Tondeleir, Jannes; Ristivojević, Petar; Đurđić, Slađana Z.; Rajković, Andreja; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - JOUR
AU  - Mutić, Jelena
AU  - Jovanović, Vesna B.
AU  - Jacxsens, Liesbeth
AU  - Tondeleir, Jannes
AU  - Ristivojević, Petar
AU  - Đurđić, Slađana Z.
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4825
AB  - Bivalves are a good source of nutrients but also a potential source of environmental contaminants, which could pose a risk for consumers. The aims of this study were: the determination of 16 elements by ICP-MS in 48 samples of five bivalve species purchased from market in Korea; the identification of elements useful for species classification using multivariate analyses; and the benefit-risk evaluation associated to the consumption of these bivalves. The highest difference among content of elements between species was found for Cd, Mn, Ni, Zn, and Fe. Partial last squares discriminant analysis revealed elements with a VIP score >1 which were considered as the most relevant for explaining certain species. As, Cd, Co, and Ni were found as taxonomical markers of V. philippinarum; Mn, Zn, Mg, and Na of A. irradians; and Cd, Ni, and Fe of M. yessoensis. These species could serve as good dietary sources of essential elements. Cd exposure by consumption of Manila clams is not representing a health risk for the Korean population; however, through consumption of Yesso scallops, 5.3% of the Korean population has a potential health risk. Removal of the digestive gland before eating will drastically reduce the amount of Cd ingested.
PB  - MDPI
T2  - Foods
T1  - Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation
VL  - 10
IS  - 11
SP  - 2690
DO  - 10.3390/foods10112690
ER  - 
@article{
author = "Mutić, Jelena and Jovanović, Vesna B. and Jacxsens, Liesbeth and Tondeleir, Jannes and Ristivojević, Petar and Đurđić, Slađana Z. and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Bivalves are a good source of nutrients but also a potential source of environmental contaminants, which could pose a risk for consumers. The aims of this study were: the determination of 16 elements by ICP-MS in 48 samples of five bivalve species purchased from market in Korea; the identification of elements useful for species classification using multivariate analyses; and the benefit-risk evaluation associated to the consumption of these bivalves. The highest difference among content of elements between species was found for Cd, Mn, Ni, Zn, and Fe. Partial last squares discriminant analysis revealed elements with a VIP score >1 which were considered as the most relevant for explaining certain species. As, Cd, Co, and Ni were found as taxonomical markers of V. philippinarum; Mn, Zn, Mg, and Na of A. irradians; and Cd, Ni, and Fe of M. yessoensis. These species could serve as good dietary sources of essential elements. Cd exposure by consumption of Manila clams is not representing a health risk for the Korean population; however, through consumption of Yesso scallops, 5.3% of the Korean population has a potential health risk. Removal of the digestive gland before eating will drastically reduce the amount of Cd ingested.",
publisher = "MDPI",
journal = "Foods",
title = "Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation",
volume = "10",
number = "11",
pages = "2690",
doi = "10.3390/foods10112690"
}
Mutić, J., Jovanović, V. B., Jacxsens, L., Tondeleir, J., Ristivojević, P., Đurđić, S. Z., Rajković, A.,& Ćirković-Veličković, T.. (2021). Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. in Foods
MDPI., 10(11), 2690.
https://doi.org/10.3390/foods10112690
Mutić J, Jovanović VB, Jacxsens L, Tondeleir J, Ristivojević P, Đurđić SZ, Rajković A, Ćirković-Veličković T. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. in Foods. 2021;10(11):2690.
doi:10.3390/foods10112690 .
Mutić, Jelena, Jovanović, Vesna B., Jacxsens, Liesbeth, Tondeleir, Jannes, Ristivojević, Petar, Đurđić, Slađana Z., Rajković, Andreja, Ćirković-Veličković, Tanja, "Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation" in Foods, 10, no. 11 (2021):2690,
https://doi.org/10.3390/foods10112690 . .
1
1

Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.

Mutić, Jelena; Jovanović, Vesna B.; Jacxsens, Liesbeth; Tondeleir, Jannes; Ristivojević, Petar; Đurđić, Slađana Z.; Rajković, Andreja; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - DATA
AU  - Mutić, Jelena
AU  - Jovanović, Vesna B.
AU  - Jacxsens, Liesbeth
AU  - Tondeleir, Jannes
AU  - Ristivojević, Petar
AU  - Đurđić, Slađana Z.
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4826
PB  - MDPI
T2  - Foods
T1  - Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4826
ER  - 
@misc{
author = "Mutić, Jelena and Jovanović, Vesna B. and Jacxsens, Liesbeth and Tondeleir, Jannes and Ristivojević, Petar and Đurđić, Slađana Z. and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4826"
}
Mutić, J., Jovanović, V. B., Jacxsens, L., Tondeleir, J., Ristivojević, P., Đurđić, S. Z., Rajković, A.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.. in Foods
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_4826
Mutić J, Jovanović VB, Jacxsens L, Tondeleir J, Ristivojević P, Đurđić SZ, Rajković A, Ćirković-Veličković T. Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.. in Foods. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4826 .
Mutić, Jelena, Jovanović, Vesna B., Jacxsens, Liesbeth, Tondeleir, Jannes, Ristivojević, Petar, Đurđić, Slađana Z., Rajković, Andreja, Ćirković-Veličković, Tanja, "Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690." in Foods (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4826 .

Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds

Ristivojević, Petar; Jovanović, Vesna B.; Milojković-Opsenica, Dušanka; Park, Jihae; Rollinger, Judith M.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4844
AB  - Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.
PB  - Elsevier
T2  - Food Chemistry
T1  - Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds
VL  - 334
SP  - 127562
DO  - 10.1016/j.foodchem.2020.127562
ER  - 
@article{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds",
volume = "334",
pages = "127562",
doi = "10.1016/j.foodchem.2020.127562"
}
Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry
Elsevier., 334, 127562.
https://doi.org/10.1016/j.foodchem.2020.127562
Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry. 2021;334:127562.
doi:10.1016/j.foodchem.2020.127562 .
Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds" in Food Chemistry, 334 (2021):127562,
https://doi.org/10.1016/j.foodchem.2020.127562 . .
3
12
6
10

Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds

Ristivojević, Petar; Jovanović, Vesna B.; Milojković-Opsenica, Dušanka; Park, Jihae; Rollinger, Judith M.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4844
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4864
AB  - Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.
PB  - Elsevier
T2  - Food Chemistry
T1  - Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds
VL  - 334
SP  - 127562
DO  - 10.1016/j.foodchem.2020.127562
ER  - 
@article{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds",
volume = "334",
pages = "127562",
doi = "10.1016/j.foodchem.2020.127562"
}
Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry
Elsevier., 334, 127562.
https://doi.org/10.1016/j.foodchem.2020.127562
Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry. 2021;334:127562.
doi:10.1016/j.foodchem.2020.127562 .
Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds" in Food Chemistry, 334 (2021):127562,
https://doi.org/10.1016/j.foodchem.2020.127562 . .
3
13
6
10

Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.

Ristivojević, Petar; Jovanović, Vesna B.; Milojković-Opsenica, Dušanka; Park, Jihae; Rollinger, Judith M.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - DATA
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4865
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4865
ER  - 
@misc{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4865"
}
Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4865
Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.. in Food Chemistry. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4865 .
Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562." in Food Chemistry (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4865 .

Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting

Smiljanić, Katarina; Prodić, Ivana; Đukić, Teodora; Vasović, Tamara; Jovanović, Vesna B.; Ćirković-Veličković, Tanja

(2021)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5716
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting
SP  - 71
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5716
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5716"
}
Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 71-71.
https://hdl.handle.net/21.15107/rcub_cherry_5716
Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cherry_5716 .
Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cherry_5716 .

The immunoproteomics reveals novel potential allergens in ark clam seashells, besides abundant tropomyosin

Mladenović, Maja; Apostolović, Danijela; Smiljanić, Katarina; Jovanović, Vesna B.; Ćirković-Veličković, Tanja

(2021)

TY  - CONF
AU  - Mladenović, Maja
AU  - Apostolović, Danijela
AU  - Smiljanić, Katarina
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5734
AB  - Shellfish allergy is one of the most common food allergies with a prevalence of 0.5%-2.5% in the general population. The most common allergen present in shellfish is tropomyosin. Our aim was to probe for the presence potentially novel allergens in two blood cockles, containing hemoglobin, Anadara broughtonii (AB) and Tigellarca granosa (TG), using sera of patients allergic to seashells and shrimps. Seashells estracts were resolved by 1D and 2D-SDS-PAGE, which were in-gel trypsin digested and characterized with nLC-ESI-MS/MS. The presence of tropomyosin was confirmed by commercial tropomyosin standard, by 1D/2D blots with specific antibodies, and by mass spectrometry identification. 1D-immunoblot was used for individual patients' profiling of IgE binding, while 2D-immunoblot was used to asses IgE reactivity with the pool of patients' sera. One third of 69sera of tested patients allergic to seafood or shrimps showed cross-reactivity with blood clamps. 2D-electrophoresis showed that most of proteins are in acidic range with especially in the range 35-50 kDa, with tropomyosin's isoforms presence in majority of spots in both seashells. IgE reactivity of individual patients showed great pattern diversity in 1D-immunoblot. 2D-immunoblots suggests hemoglobin and arginine kinase could be novel allergens. In-depth characterization of proteins causing IgE-mediated allergies is important because it can improve diagnosis and patients' health management.
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 2021, 71-71
T1  - The immunoproteomics reveals novel potential allergens in ark clam seashells, besides abundant tropomyosin
SP  - 59
EP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5734
ER  - 
@conference{
author = "Mladenović, Maja and Apostolović, Danijela and Smiljanić, Katarina and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Shellfish allergy is one of the most common food allergies with a prevalence of 0.5%-2.5% in the general population. The most common allergen present in shellfish is tropomyosin. Our aim was to probe for the presence potentially novel allergens in two blood cockles, containing hemoglobin, Anadara broughtonii (AB) and Tigellarca granosa (TG), using sera of patients allergic to seashells and shrimps. Seashells estracts were resolved by 1D and 2D-SDS-PAGE, which were in-gel trypsin digested and characterized with nLC-ESI-MS/MS. The presence of tropomyosin was confirmed by commercial tropomyosin standard, by 1D/2D blots with specific antibodies, and by mass spectrometry identification. 1D-immunoblot was used for individual patients' profiling of IgE binding, while 2D-immunoblot was used to asses IgE reactivity with the pool of patients' sera. One third of 69sera of tested patients allergic to seafood or shrimps showed cross-reactivity with blood clamps. 2D-electrophoresis showed that most of proteins are in acidic range with especially in the range 35-50 kDa, with tropomyosin's isoforms presence in majority of spots in both seashells. IgE reactivity of individual patients showed great pattern diversity in 1D-immunoblot. 2D-immunoblots suggests hemoglobin and arginine kinase could be novel allergens. In-depth characterization of proteins causing IgE-mediated allergies is important because it can improve diagnosis and patients' health management.",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 2021, 71-71",
title = "The immunoproteomics reveals novel potential allergens in ark clam seashells, besides abundant tropomyosin",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5734"
}
Mladenović, M., Apostolović, D., Smiljanić, K., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). The immunoproteomics reveals novel potential allergens in ark clam seashells, besides abundant tropomyosin. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 2021, 71-71, 59-59.
https://hdl.handle.net/21.15107/rcub_cherry_5734
Mladenović M, Apostolović D, Smiljanić K, Jovanović VB, Ćirković-Veličković T. The immunoproteomics reveals novel potential allergens in ark clam seashells, besides abundant tropomyosin. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 2021, 71-71. 2021;:59-59.
https://hdl.handle.net/21.15107/rcub_cherry_5734 .
Mladenović, Maja, Apostolović, Danijela, Smiljanić, Katarina, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "The immunoproteomics reveals novel potential allergens in ark clam seashells, besides abundant tropomyosin" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 2021, 71-71 (2021):59-59,
https://hdl.handle.net/21.15107/rcub_cherry_5734 .