Ćirković-Veličković, Tanja

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Authority KeyName Variants
orcid::0000-0003-2559-5234
  • Ćirković-Veličković, Tanja (260)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima Swedish Research Council
King Gustaf V 80th Birthday Foundation Magnus Bergvall Foundation
Swedish Asthma and Allergy Associations Research Foundation Swedish Cancer and Allergy Foundation
Swedish Heart-Lung Foundation Stockholm County Council
Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718. Hesselman Foundation
Structure-properties relationships of natural and synthetic molecules and their metal complexes Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance
Karolinska Institutet Serbian Academy of Sciences and Arts GA No. F-26.
COST Action [FA 1005] Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology
Serbian Academy of Sciences and Arts Project F-26. Swedish Association for Allergology
Center for Inflammatory Diseases Application of advanced oxidation processes and nanostructured oxide materials for the removal of pollutants from the environment, development and optimisation of instrumental techniques for efficiency monitoring
CAPSIDO – Developement of the assays for detection of SARS Cov-2 virus capsid proteins in biological fluids of COVID19 patients The Hesselman Foundation.
The King Gustaf V 80th Birthday Foundation. The Konsul Th C Bergh Foundation.
The Magnus Bergvall Foundation. The Swedish Cancer and Allergy Foundation.

Author's Bibliography

INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity

Prodić, Ivana; Smiljanić, Katarina; Nagl, Christoph; Ballmer-Weber, Barbara; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(MDPI, 2022)

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

Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Costa, Joana; Bavaro, Simona Lucia; Benedé, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larré, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martín-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Ćirković-Veličković, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas

(Springer, 2022)

TY  - JOUR
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - https://doi.org/10.1007/s12016-020-08810-9
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4981
AB  - This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
VL  - 62
IS  - 1
SP  - 37
EP  - 63
DO  - 10.1007/s12016-020-08810-9
ER  - 
@article{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
abstract = "This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?",
volume = "62",
number = "1",
pages = "37-63",
doi = "10.1007/s12016-020-08810-9"
}
Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology
Springer., 62(1), 37-63.
https://doi.org/10.1007/s12016-020-08810-9
Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology. 2022;62(1):37-63.
doi:10.1007/s12016-020-08810-9 .
Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?" in Clinical Reviews in Allergy & Immunology, 62, no. 1 (2022):37-63,
https://doi.org/10.1007/s12016-020-08810-9 . .
9
55
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44

Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining

de Guzman, Maria Krishna; Anđelković, Mirjana; Jovanović, Vesna; Jung, Jaehak; Kim, Juyang; Dailey, Lea Ann; Rajković, Andreja; De Meulenaer, Bruno; Ćirković-Veličković, Tanja

(Elsevier, 2022)

TY  - JOUR
AU  - de Guzman, Maria Krishna
AU  - Anđelković, Mirjana
AU  - Jovanović, Vesna
AU  - Jung, Jaehak
AU  - Kim, Juyang
AU  - Dailey, Lea Ann
AU  - Rajković, Andreja
AU  - De Meulenaer, Bruno
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://hdl.handle.net/1854/LU-8759702
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5420
AB  - The accumulation of microplastics in marine organisms is an emerging concern. Due to trophic transfer, the
safety of seafood is under investigation in view of the potential negative effects of microplastics on human health.
In this study, market samples of Manila clams (Ruditapes philippinarum) from South Korea were segregated into
two groups of considerably different size (p < 0.05), namely small clams with shell length of 40.69 ± 3.97 mm,
and large clams of shell length 51.19 ± 2.86 mm. Comparative profiling of the number, size, shape, and polymer
type of microplastics were performed using μFTIR imaging and Nile red staining. Overall, μFTIR detected only
1559 microplastics while 1996 microplastics were counted based on staining from 61 Manila clams (30 small and
31 large), leading to an overestimation of 18 to 75 %. Comparable microplastics concentration, based on μFTIR,
were observed at 2.70 ± 1.66 MP/g or 15.64 ± 9.25 MP/individual for the small samples, and 3.65 ± 1.59 MP/g
or 41.63 ± 16.90 MP/individual for the large ones (p > 0.05). Particle diameters of 20–100 μm was the most
dominant, accounting for 44.6 % and 46.5 % of all microplastics from the small and large groups, respectively.
Particles, with a circularity (resemblance to a circle) value between 0.6 and 1.0, were the most prevalent, fol-
lowed by fragments and fibers. At least 50 % of microplastics from the small and large samples were polystyrene,
making it the most abundant polymer type. Despite the substantial difference in the size of the animals, only a
weak to moderate correlation was observed between microplastics content and the physical attributes of the
clams such as shell length and weight, (soft) tissue weight, and total weight (Spearman's coefficient < 0.5). The
estimated intake of microplastics by the Korean population was 1232 MP/person/year via small clams, 1663 MP/
person/year via large clams, and 1489 MP/person/year via clams independent of size.
PB  - Elsevier
T2  - Marine Pollution Bulletin
T1  - Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining
VL  - n/a
IS  - n/a
DO  - 10.1016/j.marpolbul.2022.113846
ER  - 
@article{
author = "de Guzman, Maria Krishna and Anđelković, Mirjana and Jovanović, Vesna and Jung, Jaehak and Kim, Juyang and Dailey, Lea Ann and Rajković, Andreja and De Meulenaer, Bruno and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The accumulation of microplastics in marine organisms is an emerging concern. Due to trophic transfer, the
safety of seafood is under investigation in view of the potential negative effects of microplastics on human health.
In this study, market samples of Manila clams (Ruditapes philippinarum) from South Korea were segregated into
two groups of considerably different size (p < 0.05), namely small clams with shell length of 40.69 ± 3.97 mm,
and large clams of shell length 51.19 ± 2.86 mm. Comparative profiling of the number, size, shape, and polymer
type of microplastics were performed using μFTIR imaging and Nile red staining. Overall, μFTIR detected only
1559 microplastics while 1996 microplastics were counted based on staining from 61 Manila clams (30 small and
31 large), leading to an overestimation of 18 to 75 %. Comparable microplastics concentration, based on μFTIR,
were observed at 2.70 ± 1.66 MP/g or 15.64 ± 9.25 MP/individual for the small samples, and 3.65 ± 1.59 MP/g
or 41.63 ± 16.90 MP/individual for the large ones (p > 0.05). Particle diameters of 20–100 μm was the most
dominant, accounting for 44.6 % and 46.5 % of all microplastics from the small and large groups, respectively.
Particles, with a circularity (resemblance to a circle) value between 0.6 and 1.0, were the most prevalent, fol-
lowed by fragments and fibers. At least 50 % of microplastics from the small and large samples were polystyrene,
making it the most abundant polymer type. Despite the substantial difference in the size of the animals, only a
weak to moderate correlation was observed between microplastics content and the physical attributes of the
clams such as shell length and weight, (soft) tissue weight, and total weight (Spearman's coefficient < 0.5). The
estimated intake of microplastics by the Korean population was 1232 MP/person/year via small clams, 1663 MP/
person/year via large clams, and 1489 MP/person/year via clams independent of size.",
publisher = "Elsevier",
journal = "Marine Pollution Bulletin",
title = "Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining",
volume = "n/a",
number = "n/a",
doi = "10.1016/j.marpolbul.2022.113846"
}
de Guzman, M. K., Anđelković, M., Jovanović, V., Jung, J., Kim, J., Dailey, L. A., Rajković, A., De Meulenaer, B.,& Ćirković-Veličković, T.. (2022). Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining. in Marine Pollution Bulletin
Elsevier., n/a(n/a).
https://doi.org/10.1016/j.marpolbul.2022.113846
de Guzman MK, Anđelković M, Jovanović V, Jung J, Kim J, Dailey LA, Rajković A, De Meulenaer B, Ćirković-Veličković T. Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining. in Marine Pollution Bulletin. 2022;n/a(n/a).
doi:10.1016/j.marpolbul.2022.113846 .
de Guzman, Maria Krishna, Anđelković, Mirjana, Jovanović, Vesna, Jung, Jaehak, Kim, Juyang, Dailey, Lea Ann, Rajković, Andreja, De Meulenaer, Bruno, Ćirković-Veličković, Tanja, "Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining" in Marine Pollution Bulletin, n/a, no. n/a (2022),
https://doi.org/10.1016/j.marpolbul.2022.113846 . .
3

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

Simović, Ana; Combet, Sophie; Ćirković-Veličković, Tanja; Nikolic, Milan; Minić, Simeon L.

(Elsevier, 2022)

TY  - JOUR
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5002
AB  - This study aimed to characterise the stability of R-phycoerythrin (R-PE), a vivid natural colourant with emerging
potential for application in the food industry. High-quality (A560/A280 ≥ 5), native (α-helix content 75%) R-PE
was purified from commercial dried Nori (Porphyra sp.) flakes. Thermal unfolding revealed two transitions (at 56
and 72 ◦C), ascribed to different protein subunits. Contrary to elevated temperature, high-pressure (HP) treatment showed significant advantages: The R-PE unfolding was partly reversible and the colour bleaching was
minimal. Binding of Cu2+ (6.3 × 105 M− 1
) and Zn2+ (1.7 × 103 M− 1
) influenced conformational changes in the
protein tetrapyrrole chromophore without affecting R-PE structure and stability (colour). The results give new
insights into the stability of R-PE suggesting its usefulness for the replacement of toxic synthetic dyes. Preservation of the red colour of R-PE could be considered in fortified food and beverages by HP processing. R-PE may
act as a biosensor for Cu2+ in aquatic systems.
PB  - Elsevier
T2  - Food Chemistry
T1  - Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes
VL  - 374
IS  - 131780
DO  - 10.1016/j.foodchem.2021.131780
ER  - 
@article{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minić, Simeon L.",
year = "2022",
abstract = "This study aimed to characterise the stability of R-phycoerythrin (R-PE), a vivid natural colourant with emerging
potential for application in the food industry. High-quality (A560/A280 ≥ 5), native (α-helix content 75%) R-PE
was purified from commercial dried Nori (Porphyra sp.) flakes. Thermal unfolding revealed two transitions (at 56
and 72 ◦C), ascribed to different protein subunits. Contrary to elevated temperature, high-pressure (HP) treatment showed significant advantages: The R-PE unfolding was partly reversible and the colour bleaching was
minimal. Binding of Cu2+ (6.3 × 105 M− 1
) and Zn2+ (1.7 × 103 M− 1
) influenced conformational changes in the
protein tetrapyrrole chromophore without affecting R-PE structure and stability (colour). The results give new
insights into the stability of R-PE suggesting its usefulness for the replacement of toxic synthetic dyes. Preservation of the red colour of R-PE could be considered in fortified food and beverages by HP processing. R-PE may
act as a biosensor for Cu2+ in aquatic systems.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes",
volume = "374",
number = "131780",
doi = "10.1016/j.foodchem.2021.131780"
}
Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minić, S. L.. (2022). Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Food Chemistry
Elsevier., 374(131780).
https://doi.org/10.1016/j.foodchem.2021.131780
Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minić SL. Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Food Chemistry. 2022;374(131780).
doi:10.1016/j.foodchem.2021.131780 .
Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minić, Simeon L., "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes" in Food Chemistry, 374, no. 131780 (2022),
https://doi.org/10.1016/j.foodchem.2021.131780 . .
1
2
2

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

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

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
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",
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.
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.
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 (2022),
https://doi.org/10.1080/10408398.2021.1931806 . .
1
7
2
7

Microplastics in food: scoping review on health effects, occurrence, and human exposure

Udovički, Božidar; Anđelković, Mirjana; Ćirković-Veličković, Tanja; Rajković, Andreja

(BMC, 2022)

TY  - JOUR
AU  - Udovički, Božidar
AU  - Anđelković, Mirjana
AU  - Ćirković-Veličković, Tanja
AU  - Rajković, Andreja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5509
AB  - With most of the plastics ever produced now being waste, slowly degrading and fragmenting in the environment, microplastics (MPs) have become an emerging concern regarding their presence in food and influence on human health. While many studies on marine ecotoxicology and the occurrence of MPs in fish and shellfish exist, research on the occurrence of MPs in other foods and their effect on human health is still in early-stage, but the attention is increasing. This review aimed to provide relevant information on the possible health effect of ingested MPs, the occurrence, and levels of MPs contamination in various foods and estimated exposure to MPs through food. Potential toxic consequences from exposure to MPs through food can arise from MPs themselves, diffused monomers and additives but also from sorbed contaminants or microorganisms that colonise MPs. Recent publications have confirmed widespread contamination of our food with MPs including basic and life-essential constituents such as water and salt providing the basis for chronic exposure. Available exposure assessments indicate that we ingest up to several hundred thousand MPs particles yearly.
PB  - BMC
T2  - International Journal of Food Contamination
T1  - Microplastics in food: scoping review on health effects, occurrence, and human exposure
VL  - 9
IS  - 1
DO  - 10.1186/s40550-022-00093-6
ER  - 
@article{
author = "Udovički, Božidar and Anđelković, Mirjana and Ćirković-Veličković, Tanja and Rajković, Andreja",
year = "2022",
abstract = "With most of the plastics ever produced now being waste, slowly degrading and fragmenting in the environment, microplastics (MPs) have become an emerging concern regarding their presence in food and influence on human health. While many studies on marine ecotoxicology and the occurrence of MPs in fish and shellfish exist, research on the occurrence of MPs in other foods and their effect on human health is still in early-stage, but the attention is increasing. This review aimed to provide relevant information on the possible health effect of ingested MPs, the occurrence, and levels of MPs contamination in various foods and estimated exposure to MPs through food. Potential toxic consequences from exposure to MPs through food can arise from MPs themselves, diffused monomers and additives but also from sorbed contaminants or microorganisms that colonise MPs. Recent publications have confirmed widespread contamination of our food with MPs including basic and life-essential constituents such as water and salt providing the basis for chronic exposure. Available exposure assessments indicate that we ingest up to several hundred thousand MPs particles yearly.",
publisher = "BMC",
journal = "International Journal of Food Contamination",
title = "Microplastics in food: scoping review on health effects, occurrence, and human exposure",
volume = "9",
number = "1",
doi = "10.1186/s40550-022-00093-6"
}
Udovički, B., Anđelković, M., Ćirković-Veličković, T.,& Rajković, A.. (2022). Microplastics in food: scoping review on health effects, occurrence, and human exposure. in International Journal of Food Contamination
BMC., 9(1).
https://doi.org/10.1186/s40550-022-00093-6
Udovički B, Anđelković M, Ćirković-Veličković T, Rajković A. Microplastics in food: scoping review on health effects, occurrence, and human exposure. in International Journal of Food Contamination. 2022;9(1).
doi:10.1186/s40550-022-00093-6 .
Udovički, Božidar, Anđelković, Mirjana, Ćirković-Veličković, Tanja, Rajković, Andreja, "Microplastics in food: scoping review on health effects, occurrence, and human exposure" in International Journal of Food Contamination, 9, no. 1 (2022),
https://doi.org/10.1186/s40550-022-00093-6 . .
2
1

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

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

(Faculty of Chemistry, Serbian Biochemical Society, 2022)

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić Vučinić, Dragana
AU  - Minić, Simeon
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 and Gligorijević, Nikola and Stanić Vučinić, Dragana and Minić, Simeon 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., Gligorijević, N., Stanić Vučinić, D., Minić, S., 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 M, Gligorijević N, Stanić Vučinić D, Minić S, 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, Gligorijević, Nikola, Stanić Vučinić, Dragana, Minić, Simeon, 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 .

Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein

Radomirović, Mirjana Z.; Simović, Ana S.; Udovički, Božidar D.; Krstić-Ristivojević, Maja V.; Sabljić, Ljiljana Z.; Lukić, Ivana D.; Glamočlija, Sofija Đ.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana M.; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2022)

TY  - CONF
AU  - Radomirović, Mirjana Z.
AU  - Simović, Ana S.
AU  - Udovički, Božidar D.
AU  - Krstić-Ristivojević, Maja V.
AU  - Sabljić, Ljiljana Z.
AU  - Lukić, Ivana D.
AU  - Glamočlija, Sofija Đ.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana M.
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5362
AB  - Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja zasuzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostimaELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studijeje bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih serumaza rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjamapsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testaproizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima ize evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumivisokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog zaovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adheriranina dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli itekoncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu zakvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jimpoliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe ujespektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikacijuN-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototipELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekcijuN-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u zakvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma.
AB  - The accurate diagnosis of people with suspected infection with the SARS-CoV-2 isessential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can bedetected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens inbiological fluids in ELISA or similar techniques using antibodies developed in animals.The aim of the study was the establishment of a quantitative polyclonal sera-based test forroutine measurement of the concentration of SARS CoV-2 nucleocapsid protein usingabsorbance measurement in a standard 96-well microtiter plate. For the purposes of the testdevelopment, recombinant N protein was produced and used for the production of miceand rabbit antisera. Produced antisera were purified and titer was determined. High-affinitypolyclonal N-protein specific antisera were used for N-protein specific ELISA testdevelopment. The test is based on mice polyclonal sera adhered to microtiter plate bottomfor the capture of the N protein from the specimen. Various concentrations of therecombinant N-protein were used to generate a standard curve for protein quantification.The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera andanti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.We have successfully developed the prototype ELISA for the quantification of N-proteinwith the detection limit being in the range of ng/mL. The average LOD value for theprototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for thedetection of N-protein with affinity and specificity similar to, or better than commercialantibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence forquantification of the N-protein in protein-rich samples, similar to human sera.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein
T1  - Development of SARS-CoV-2 N-protein specific capture ELISA
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5362
ER  - 
@conference{
author = "Radomirović, Mirjana Z. and Simović, Ana S. and Udovički, Božidar D. and Krstić-Ristivojević, Maja V. and Sabljić, Ljiljana Z. and Lukić, Ivana D. and Glamočlija, Sofija Đ. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana M. and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja zasuzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostimaELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studijeje bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih serumaza rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjamapsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testaproizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima ize evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumivisokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog zaovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adheriranina dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli itekoncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu zakvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jimpoliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe ujespektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikacijuN-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototipELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekcijuN-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u zakvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma., The accurate diagnosis of people with suspected infection with the SARS-CoV-2 isessential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can bedetected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens inbiological fluids in ELISA or similar techniques using antibodies developed in animals.The aim of the study was the establishment of a quantitative polyclonal sera-based test forroutine measurement of the concentration of SARS CoV-2 nucleocapsid protein usingabsorbance measurement in a standard 96-well microtiter plate. For the purposes of the testdevelopment, recombinant N protein was produced and used for the production of miceand rabbit antisera. Produced antisera were purified and titer was determined. High-affinitypolyclonal N-protein specific antisera were used for N-protein specific ELISA testdevelopment. The test is based on mice polyclonal sera adhered to microtiter plate bottomfor the capture of the N protein from the specimen. Various concentrations of therecombinant N-protein were used to generate a standard curve for protein quantification.The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera andanti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.We have successfully developed the prototype ELISA for the quantification of N-proteinwith the detection limit being in the range of ng/mL. The average LOD value for theprototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for thedetection of N-protein with affinity and specificity similar to, or better than commercialantibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence forquantification of the N-protein in protein-rich samples, similar to human sera.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein, Development of SARS-CoV-2 N-protein specific capture ELISA",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5362"
}
Radomirović, M. Z., Simović, A. S., Udovički, B. D., Krstić-Ristivojević, M. V., Sabljić, L. Z., Lukić, I. D., Glamočlija, S. Đ., Ćujić, D. R., Gnjatović, M. Lj., Stojanović, M. M., Stanić-Vučinić, D., Radosavljević, J.,& Ćirković-Veličković, T.. (2022). Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo..
https://hdl.handle.net/21.15107/rcub_cherry_5362
Radomirović MZ, Simović AS, Udovički BD, Krstić-Ristivojević MV, Sabljić LZ, Lukić ID, Glamočlija SĐ, Ćujić DR, Gnjatović ML, Stojanović MM, Stanić-Vučinić D, Radosavljević J, Ćirković-Veličković T. Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5362 .
Radomirović, Mirjana Z., Simović, Ana S., Udovički, Božidar D., Krstić-Ristivojević, Maja V., Sabljić, Ljiljana Z., Lukić, Ivana D., Glamočlija, Sofija Đ., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana M., Stanić-Vučinić, Dragana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5362 .

Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein

Radomirović, Mirjana Z.; Simović, Ana S.; Udovički, Božidar D.; Krstić-Ristivojević, Maja V.; Sabljić, Ljiljana Z.; Lukić, Ivana D.; Glamočlija, Sofija Đ.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana M.; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2022)

TY  - CONF
AU  - Radomirović, Mirjana Z.
AU  - Simović, Ana S.
AU  - Udovički, Božidar D.
AU  - Krstić-Ristivojević, Maja V.
AU  - Sabljić, Ljiljana Z.
AU  - Lukić, Ivana D.
AU  - Glamočlija, Sofija Đ.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana M.
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5361
AB  - Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja za
suzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostima
ELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studije
je bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih seruma
za rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjam
apsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testa
proizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima i
ze evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumi
visokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog za
ovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adherirani
na dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli ite
koncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu za
kvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jim
poliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe uje
spektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikaciju
N-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototip
ELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ
10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekciju
N-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.
Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u za
kvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma.
AB  - The accurate diagnosis of people with suspected infection with the SARS-CoV-2 is
essential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can be
detected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens in
biological fluids in ELISA or similar techniques using antibodies developed in animals.
The aim of the study was the establishment of a quantitative polyclonal sera-based test for
routine measurement of the concentration of SARS CoV-2 nucleocapsid protein using
absorbance measurement in a standard 96-well microtiter plate. For the purposes of the test
development, recombinant N protein was produced and used for the production of mice
and rabbit antisera. Produced antisera were purified and titer was determined. High-affinity
polyclonal N-protein specific antisera were used for N-protein specific ELISA test
development. The test is based on mice polyclonal sera adhered to microtiter plate bottom
for the capture of the N protein from the specimen. Various concentrations of the
recombinant N-protein were used to generate a standard curve for protein quantification.
The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera and
anti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.
We have successfully developed the prototype ELISA for the quantification of N-protein
with the detection limit being in the range of ng/mL. The average LOD value for the
prototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was
10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for the
detection of N-protein with affinity and specificity similar to, or better than commercial
antibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence for
quantification of the N-protein in protein-rich samples, similar to human sera.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein
T1  - Development of SARS-CoV-2 N-protein specific capture ELISA
SP  - 65
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5361
ER  - 
@conference{
author = "Radomirović, Mirjana Z. and Simović, Ana S. and Udovički, Božidar D. and Krstić-Ristivojević, Maja V. and Sabljić, Ljiljana Z. and Lukić, Ivana D. and Glamočlija, Sofija Đ. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana M. and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja za
suzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostima
ELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studije
je bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih seruma
za rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjam
apsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testa
proizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima i
ze evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumi
visokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog za
ovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adherirani
na dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli ite
koncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu za
kvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jim
poliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe uje
spektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikaciju
N-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototip
ELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ
10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekciju
N-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.
Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u za
kvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma., The accurate diagnosis of people with suspected infection with the SARS-CoV-2 is
essential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can be
detected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens in
biological fluids in ELISA or similar techniques using antibodies developed in animals.
The aim of the study was the establishment of a quantitative polyclonal sera-based test for
routine measurement of the concentration of SARS CoV-2 nucleocapsid protein using
absorbance measurement in a standard 96-well microtiter plate. For the purposes of the test
development, recombinant N protein was produced and used for the production of mice
and rabbit antisera. Produced antisera were purified and titer was determined. High-affinity
polyclonal N-protein specific antisera were used for N-protein specific ELISA test
development. The test is based on mice polyclonal sera adhered to microtiter plate bottom
for the capture of the N protein from the specimen. Various concentrations of the
recombinant N-protein were used to generate a standard curve for protein quantification.
The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera and
anti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.
We have successfully developed the prototype ELISA for the quantification of N-protein
with the detection limit being in the range of ng/mL. The average LOD value for the
prototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was
10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for the
detection of N-protein with affinity and specificity similar to, or better than commercial
antibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence for
quantification of the N-protein in protein-rich samples, similar to human sera.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein, Development of SARS-CoV-2 N-protein specific capture ELISA",
pages = "65-66",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5361"
}
Radomirović, M. Z., Simović, A. S., Udovički, B. D., Krstić-Ristivojević, M. V., Sabljić, L. Z., Lukić, I. D., Glamočlija, S. Đ., Ćujić, D. R., Gnjatović, M. Lj., Stojanović, M. M., Stanić-Vučinić, D., Radosavljević, J.,& Ćirković-Veličković, T.. (2022). Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo., 65-66.
https://hdl.handle.net/21.15107/rcub_cherry_5361
Radomirović MZ, Simović AS, Udovički BD, Krstić-Ristivojević MV, Sabljić LZ, Lukić ID, Glamočlija SĐ, Ćujić DR, Gnjatović ML, Stojanović MM, Stanić-Vučinić D, Radosavljević J, Ćirković-Veličković T. Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;:65-66.
https://hdl.handle.net/21.15107/rcub_cherry_5361 .
Radomirović, Mirjana Z., Simović, Ana S., Udovički, Božidar D., Krstić-Ristivojević, Maja V., Sabljić, Ljiljana Z., Lukić, Ivana D., Glamočlija, Sofija Đ., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana M., Stanić-Vučinić, Dragana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022):65-66,
https://hdl.handle.net/21.15107/rcub_cherry_5361 .

Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.

Simović, Ana; Combet, Sophie; Ćirković-Veličković, Tanja; Nikolic, Milan; Minić, Simeon L.

(Elsevier, 2022)

TY  - DATA
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5003
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5003
ER  - 
@misc{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minić, Simeon L.",
year = "2022",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5003"
}
Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minić, S. L.. (2022). Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_5003
Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minić SL. Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.. in Food Chemistry. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5003 .
Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minić, Simeon L., "Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780." in Food Chemistry (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5003 .

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 . .
2
6
4

Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.

Costa, Joana; Bavaro, Simona Lucia; Benedé, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larré, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martín-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Ćirković-Veličković, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas

(Springer, 2022)

TY  - DATA
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4982
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4982
ER  - 
@misc{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4982"
}
Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_4982
Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_4982 .
Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9." in Clinical Reviews in Allergy & Immunology (2022),
https://hdl.handle.net/21.15107/rcub_cherry_4982 .

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

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

(Elsevier, 2021)

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna
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 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., 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 V, 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, 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
10
6
8

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

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

(Elsevier, 2021)

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna
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 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., 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 V, 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, 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
10
6
8

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; Milojković-Opsenica, Dušanka; Park, Jihae; Rollinger, Judith M.; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - DATA
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna
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 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., 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 V, 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, 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 .

Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application

Đurđić, Slađana Z.; Stanković, V.; Vlahović, Filip; Ognjanović, Miloš; Kalcher, K.; Ćirković-Veličković, Tanja; Mutić, Jelena; Stanković, Dalibor

(The Electrochemical Society (ECS), 2021)

TY  - JOUR
AU  - Đurđić, Slađana Z.
AU  - Stanković, V.
AU  - Vlahović, Filip
AU  - Ognjanović, Miloš
AU  - Kalcher, K.
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Stanković, Dalibor
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4474
AB  - Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.
PB  - The Electrochemical Society (ECS)
T2  - Journal of The Electrochemical Society
T1  - Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application
VL  - 168
IS  - 3
SP  - 037510
DO  - 10.1149/1945-7111/abeaf2
ER  - 
@article{
author = "Đurđić, Slađana Z. and Stanković, V. and Vlahović, Filip and Ognjanović, Miloš and Kalcher, K. and Ćirković-Veličković, Tanja and Mutić, Jelena and Stanković, Dalibor",
year = "2021",
abstract = "Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.",
publisher = "The Electrochemical Society (ECS)",
journal = "Journal of The Electrochemical Society",
title = "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application",
volume = "168",
number = "3",
pages = "037510",
doi = "10.1149/1945-7111/abeaf2"
}
Đurđić, S. Z., Stanković, V., Vlahović, F., Ognjanović, M., Kalcher, K., Ćirković-Veličković, T., Mutić, J.,& Stanković, D.. (2021). Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society
The Electrochemical Society (ECS)., 168(3), 037510.
https://doi.org/10.1149/1945-7111/abeaf2
Đurđić SZ, Stanković V, Vlahović F, Ognjanović M, Kalcher K, Ćirković-Veličković T, Mutić J, Stanković D. Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society. 2021;168(3):037510.
doi:10.1149/1945-7111/abeaf2 .
Đurđić, Slađana Z., Stanković, V., Vlahović, Filip, Ognjanović, Miloš, Kalcher, K., Ćirković-Veličković, Tanja, Mutić, Jelena, Stanković, Dalibor, "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application" in Journal of The Electrochemical Society, 168, no. 3 (2021):037510,
https://doi.org/10.1149/1945-7111/abeaf2 . .
5
2
5

Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application

Đurđić, Slađana Z.; Stanković, V.; Vlahović, Filip; Ognjanović, Miloš; Kalcher, K.; Ćirković-Veličković, Tanja; Mutić, Jelena; Stanković, Dalibor

(The Electrochemical Society (ECS), 2021)

TY  - JOUR
AU  - Đurđić, Slađana Z.
AU  - Stanković, V.
AU  - Vlahović, Filip
AU  - Ognjanović, Miloš
AU  - Kalcher, K.
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Stanković, Dalibor
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4475
AB  - Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.
PB  - The Electrochemical Society (ECS)
T2  - Journal of The Electrochemical Society
T1  - Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application
VL  - 168
IS  - 3
SP  - 037510
DO  - 10.1149/1945-7111/abeaf2
ER  - 
@article{
author = "Đurđić, Slađana Z. and Stanković, V. and Vlahović, Filip and Ognjanović, Miloš and Kalcher, K. and Ćirković-Veličković, Tanja and Mutić, Jelena and Stanković, Dalibor",
year = "2021",
abstract = "Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.",
publisher = "The Electrochemical Society (ECS)",
journal = "Journal of The Electrochemical Society",
title = "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application",
volume = "168",
number = "3",
pages = "037510",
doi = "10.1149/1945-7111/abeaf2"
}
Đurđić, S. Z., Stanković, V., Vlahović, F., Ognjanović, M., Kalcher, K., Ćirković-Veličković, T., Mutić, J.,& Stanković, D.. (2021). Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society
The Electrochemical Society (ECS)., 168(3), 037510.
https://doi.org/10.1149/1945-7111/abeaf2
Đurđić SZ, Stanković V, Vlahović F, Ognjanović M, Kalcher K, Ćirković-Veličković T, Mutić J, Stanković D. Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society. 2021;168(3):037510.
doi:10.1149/1945-7111/abeaf2 .
Đurđić, Slađana Z., Stanković, V., Vlahović, Filip, Ognjanović, Miloš, Kalcher, K., Ćirković-Veličković, Tanja, Mutić, Jelena, Stanković, Dalibor, "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application" in Journal of The Electrochemical Society, 168, no. 3 (2021):037510,
https://doi.org/10.1149/1945-7111/abeaf2 . .
5
2
5

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

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

(MDPI, 2021)

TY  - JOUR
AU  - Mutić, Jelena
AU  - Jovanović, Vesna
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 &gt;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 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 &gt;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., 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 V, 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, 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; Jacxsens, Liesbeth; Tondeleir, Jannes; Ristivojević, Petar; Đurđić, Slađana Z.; Rajković, Andreja; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - DATA
AU  - Mutić, Jelena
AU  - Jovanović, Vesna
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 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., 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 V, 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, 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 .

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

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

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4330
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.

Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, 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 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.

Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
5
11
8
8

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

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

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4331
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, 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 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
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Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4332
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
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Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4333
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
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