TY  - JOUR
AU  - Khulal, Urmila
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6437
AB  - Meat samples were subjected to thermal processing combined with simulated INFOGEST in vitro gastrointestinal (GI) digestion. Protein modifications (PMs) were screened with commercially available PM-specific antibodies. Specific proteins at 20, 37, 50, and 65 kDa react to more than 3 PM-specific antibodies among meat proteins. Lysine methylation and methionine oxidation were the most prominent PMs in WB. Mass spectrometry confirmed bands at ≈20 kDa as allergenic proteins: sarcoplasmic calcium-binding protein in oyster, 37 kDa as tropomyosin in shrimp, oyster, and abalone. MS-identified PMs of shellfish allergens were aligned to the IgE binding epitopes. GI digestion-resistant peptides of shellfish proteins were identified as paramyosins in oyster and abalone and SBP in shrimp. Our results point to the high susceptibility of immunodominant epitopes of major shellfish allergens to PMs. In TPM, saturation of oxidative modification increases with thermal processing resulting in higher susceptibility of TPM to gastric digestion.
PB  - Elsevier
T2  - Journal of Functional Foods
T1  - Protein modifications screening of raw and thermally treated meat gastrointestinal digesta
VL  - 113
SP  - 106052
DO  - 10.1016/j.jff.2024.106052
ER  - 

@article{
author = "Khulal, Urmila and Đukić, Teodora and Smiljanić, Katarina and Vasović, Tamara and Aćimović, Jelena and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Meat samples were subjected to thermal processing combined with simulated INFOGEST in vitro gastrointestinal (GI) digestion. Protein modifications (PMs) were screened with commercially available PM-specific antibodies. Specific proteins at 20, 37, 50, and 65 kDa react to more than 3 PM-specific antibodies among meat proteins. Lysine methylation and methionine oxidation were the most prominent PMs in WB. Mass spectrometry confirmed bands at ≈20 kDa as allergenic proteins: sarcoplasmic calcium-binding protein in oyster, 37 kDa as tropomyosin in shrimp, oyster, and abalone. MS-identified PMs of shellfish allergens were aligned to the IgE binding epitopes. GI digestion-resistant peptides of shellfish proteins were identified as paramyosins in oyster and abalone and SBP in shrimp. Our results point to the high susceptibility of immunodominant epitopes of major shellfish allergens to PMs. In TPM, saturation of oxidative modification increases with thermal processing resulting in higher susceptibility of TPM to gastric digestion.",
publisher = "Elsevier",
journal = "Journal of Functional Foods",
title = "Protein modifications screening of raw and thermally treated meat gastrointestinal digesta",
volume = "113",
pages = "106052",
doi = "10.1016/j.jff.2024.106052"
}

Khulal, U., Đukić, T., Smiljanić, K., Vasović, T., Aćimović, J., Rajković, A.,& Ćirković-Veličković, T.. (2024). Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods
Elsevier., 113, 106052.
https://doi.org/10.1016/j.jff.2024.106052

Khulal U, Đukić T, Smiljanić K, Vasović T, Aćimović J, Rajković A, Ćirković-Veličković T. Protein modifications screening of raw and thermally treated meat gastrointestinal digesta. in Journal of Functional Foods. 2024;113:106052.
doi:10.1016/j.jff.2024.106052 .

Khulal, Urmila, Đukić, Teodora, Smiljanić, Katarina, Vasović, Tamara, Aćimović, Jelena, Rajković, Andreja, Ćirković-Veličković, Tanja, "Protein modifications screening of raw and thermally treated meat gastrointestinal digesta" in Journal of Functional Foods, 113 (2024):106052,
https://doi.org/10.1016/j.jff.2024.106052 . .

TY  - JOUR
AU  - Mladenović Stokanić, Maja
AU  - Simović, Ana
AU  - Jovanović, Vesna B.
AU  - Radomirović, Mirjana
AU  - Udovićki, Božidar
AU  - Krstić Ristivojević, Maja
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Aćimović, Jelena
AU  - Sabljić, Ljiljana
AU  - Lukić, Ivana
AU  - Kovačević, Ana
AU  - Cujić, Danica
AU  - Gnjatović, Marija
AU  - Smiljanić, Katarina
AU  - Stojadinović, Marija
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojanović, Marijana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6436
AB  - In this study, a cost-effective sandwich ELISA test, based on polyclonal antibodies, for routine quantification SARS-CoV-2 nucleocapsid (N) protein was developed. The recombinant N protein was produced and used for the production of mice and rabbit antisera. Polyclonal N protein-specific antibodies served as capture and detection antibodies. The prototype ELISA has LOD 0.93 ng/mL and LOQ 5.3 ng/mL, with a linear range of 1.52–48.83 ng/mL. N protein heat pretreatment (56 °C, 1 h) decreased, while pretreatment with 1% Triton X-100 increased analytical ELISA sensitivity. The diagnostic specificity of ELISA was 100% (95% CI, 91.19–100.00%) and sensitivity was 52.94% (95% CI, 35.13–70.22%) compared to rtRT-PCR (Ct < 40). Profoundly higher sensitivity was obtained using patient samples mostly containing Wuhan-similar variants (Wuhan, alpha, and delta), 62.50% (95% CI, 40.59 to 81.20%), in comparison to samples mostly containing Wuhan-distant variants (Omicron) 30.00% (6.67–65.25%). The developed product has relatively high diagnostic sensitivity in relation to its analytical sensitivity due to the usage of polyclonal antibodies from two species, providing a wide repertoire of antibodies against multiple N protein epitopes. Moreover, the fast, simple, and inexpensive production of polyclonal antibodies, as the most expensive assay components, would result in affordable antigen tests.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species
VL  - 25
IS  - 1
SP  - 333
DO  - 10.3390/ijms25010333
ER  - 

@article{
author = "Mladenović Stokanić, Maja and Simović, Ana and Jovanović, Vesna B. and Radomirović, Mirjana and Udovićki, Božidar and Krstić Ristivojević, Maja and Đukić, Teodora and Vasović, Tamara and Aćimović, Jelena and Sabljić, Ljiljana and Lukić, Ivana and Kovačević, Ana and Cujić, Danica and Gnjatović, Marija and Smiljanić, Katarina and Stojadinović, Marija and Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojanović, Marijana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "In this study, a cost-effective sandwich ELISA test, based on polyclonal antibodies, for routine quantification SARS-CoV-2 nucleocapsid (N) protein was developed. The recombinant N protein was produced and used for the production of mice and rabbit antisera. Polyclonal N protein-specific antibodies served as capture and detection antibodies. The prototype ELISA has LOD 0.93 ng/mL and LOQ 5.3 ng/mL, with a linear range of 1.52–48.83 ng/mL. N protein heat pretreatment (56 °C, 1 h) decreased, while pretreatment with 1% Triton X-100 increased analytical ELISA sensitivity. The diagnostic specificity of ELISA was 100% (95% CI, 91.19–100.00%) and sensitivity was 52.94% (95% CI, 35.13–70.22%) compared to rtRT-PCR (Ct < 40). Profoundly higher sensitivity was obtained using patient samples mostly containing Wuhan-similar variants (Wuhan, alpha, and delta), 62.50% (95% CI, 40.59 to 81.20%), in comparison to samples mostly containing Wuhan-distant variants (Omicron) 30.00% (6.67–65.25%). The developed product has relatively high diagnostic sensitivity in relation to its analytical sensitivity due to the usage of polyclonal antibodies from two species, providing a wide repertoire of antibodies against multiple N protein epitopes. Moreover, the fast, simple, and inexpensive production of polyclonal antibodies, as the most expensive assay components, would result in affordable antigen tests.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species",
volume = "25",
number = "1",
pages = "333",
doi = "10.3390/ijms25010333"
}

Mladenović Stokanić, M., Simović, A., Jovanović, V. B., Radomirović, M., Udovićki, B., Krstić Ristivojević, M., Đukić, T., Vasović, T., Aćimović, J., Sabljić, L., Lukić, I., Kovačević, A., Cujić, D., Gnjatović, M., Smiljanić, K., Stojadinović, M., Radosavljević, J., Stanić-Vučinić, D., Stojanović, M., Rajković, A.,& Ćirković-Veličković, T.. (2023). Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species. in International Journal of Molecular Sciences
MDPI., 25(1), 333.
https://doi.org/10.3390/ijms25010333

Mladenović Stokanić M, Simović A, Jovanović VB, Radomirović M, Udovićki B, Krstić Ristivojević M, Đukić T, Vasović T, Aćimović J, Sabljić L, Lukić I, Kovačević A, Cujić D, Gnjatović M, Smiljanić K, Stojadinović M, Radosavljević J, Stanić-Vučinić D, Stojanović M, Rajković A, Ćirković-Veličković T. Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species. in International Journal of Molecular Sciences. 2023;25(1):333.
doi:10.3390/ijms25010333 .

Mladenović Stokanić, Maja, Simović, Ana, Jovanović, Vesna B., Radomirović, Mirjana, Udovićki, Božidar, Krstić Ristivojević, Maja, Đukić, Teodora, Vasović, Tamara, Aćimović, Jelena, Sabljić, Ljiljana, Lukić, Ivana, Kovačević, Ana, Cujić, Danica, Gnjatović, Marija, Smiljanić, Katarina, Stojadinović, Marija, Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojanović, Marijana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Sandwich ELISA for the Quantification of Nucleocapsid Protein of SARS-CoV-2 Based on Polyclonal Antibodies from Two Different Species" in International Journal of Molecular Sciences, 25, no. 1 (2023):333,
https://doi.org/10.3390/ijms25010333 . .

TY  - DATA
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6466
AB  - Experimental data for the results shown in the manuscript Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR are given in the attachment.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Research data for: Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences MDPI., 24(20), 15410. https://doi.org/doi.org/10.3390/ ijms242015410
VL  - 24
IS  - 20
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6466
ER  - 

@misc{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Experimental data for the results shown in the manuscript Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR are given in the attachment.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Research data for: Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences MDPI., 24(20), 15410. https://doi.org/doi.org/10.3390/ ijms242015410",
volume = "24",
number = "20",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6466"
}

Radomirović, M., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Research data for: Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences MDPI., 24(20), 15410. https://doi.org/doi.org/10.3390/ ijms242015410. in International Journal of Molecular Sciences
MDPI., 24(20).
https://hdl.handle.net/21.15107/rcub_cherry_6466

Radomirović M, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Research data for: Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences MDPI., 24(20), 15410. https://doi.org/doi.org/10.3390/ ijms242015410. in International Journal of Molecular Sciences. 2023;24(20).
https://hdl.handle.net/21.15107/rcub_cherry_6466 .

Radomirović, Mirjana, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Research data for: Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences MDPI., 24(20), 15410. https://doi.org/doi.org/10.3390/ ijms242015410" in International Journal of Molecular Sciences, 24, no. 20 (2023),
https://hdl.handle.net/21.15107/rcub_cherry_6466 .

TY  - JOUR
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6019
AB  - Tropomyosin is the major and predominant allergen among shellfish. This study developed
an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods.
The method couples sandwich ELISA with the real-time PCR (rtPCR) amplification of marker DNAs. Monoclonal anti-TPM antibody was the capture antibody, polyclonal rabbit anti-shrimp tropomyosin antibody was the detection antibody, while natural shrimp tropomyosin served as the standard. A double-stranded amino-DNA was covalently conjugated to a secondary anti-rabbit antibody and subsequently amplified and quantified via rtPCR. The quantification sensitivity of immuno-PCR was 20-fold higher than analogous ELISA, with LOQ 19.8 pg/mL. The developed immuno-PCR method is highly specific for the detection of crustacean tropomyosin and is highly precise in a broad concentration range. Tropomyosin recovery in the spiked vegetable soup was 87.7–115.6%. Crustacean tropomyosin was also quantified in commercial food products. The reported immuno-PCR assay is the most sensitive method for the quantification of crustacean tropomyosin and is the first immuno-PCR-based assay for the quantification of food allergen and food protein in general. The described method could be easily adapted for the specific and ultrasensitive immuno-PCR-based detection of traces of any food allergen that is currently being quantified with ELISA, which is of critical importance for people with food allergies.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR
VL  - 24
IS  - 20
SP  - 15410
DO  - doi.org/10.3390/ ijms242015410
ER  - 

@article{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Tropomyosin is the major and predominant allergen among shellfish. This study developed
an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods.
The method couples sandwich ELISA with the real-time PCR (rtPCR) amplification of marker DNAs. Monoclonal anti-TPM antibody was the capture antibody, polyclonal rabbit anti-shrimp tropomyosin antibody was the detection antibody, while natural shrimp tropomyosin served as the standard. A double-stranded amino-DNA was covalently conjugated to a secondary anti-rabbit antibody and subsequently amplified and quantified via rtPCR. The quantification sensitivity of immuno-PCR was 20-fold higher than analogous ELISA, with LOQ 19.8 pg/mL. The developed immuno-PCR method is highly specific for the detection of crustacean tropomyosin and is highly precise in a broad concentration range. Tropomyosin recovery in the spiked vegetable soup was 87.7–115.6%. Crustacean tropomyosin was also quantified in commercial food products. The reported immuno-PCR assay is the most sensitive method for the quantification of crustacean tropomyosin and is the first immuno-PCR-based assay for the quantification of food allergen and food protein in general. The described method could be easily adapted for the specific and ultrasensitive immuno-PCR-based detection of traces of any food allergen that is currently being quantified with ELISA, which is of critical importance for people with food allergies.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR",
volume = "24",
number = "20",
pages = "15410",
doi = "doi.org/10.3390/ ijms242015410"
}

Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences
MDPI., 24(20), 15410.
https://doi.org/doi.org/10.3390/ ijms242015410

Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences. 2023;24(20):15410.
doi:doi.org/10.3390/ ijms242015410 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR" in International Journal of Molecular Sciences, 24, no. 20 (2023):15410,
https://doi.org/doi.org/10.3390/ ijms242015410 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Bićanin, Maša
AU  - Udovički, Božidar
AU  - Krstić-Ristivojević, Maja
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6021
AB  - Accurately diagnosing people with suspected SARS-CoV-2 infection is essential to help manage COVID-19. Currently available SARS-CoV-2 diagnostics detect either RNA of the virus by RT-PCR or the presence of viral antigens in biological fluids by ELISA or similar techniques. Low sensitivity of antigen tests could lead to the risk of false negative results. Therefore, this study aimed to develop a highly sensitive immuno-PCR method for quantifying SARS-CoV-2 nucleocapsid (N) protein that combines the specificity of sandwich ELISA with the sensitivity of PCR. Recombinant N protein fragment was produced in E. coli as an expression system and purified using immobilized metal ion affinity chromatography. The antibodies against the N protein were raised in rabbits and mice. High-affinity polyclonal mice and rabbit N protein-specific antisera were purified using ammonium sulfate precipitation and used to develop sandwich ELISA for the quantification of N protein. Mice polyclonal serum was used as a capture for N protein. N
protein bound to mice antibodies was detected with rabbit polyclonal sera. A double-stranded amino-DNA molecule of 77 base pairs was PCR-synthesized, covalently conjugated to a secondary goat anti-rabbit antibody and subsequently amplified and quantified by real-time PCR. The results were compared to analogous sandwich ELISA consisting of alkaline phosphatase-labeled goat anti-rabbit antibody. The sensitivity of immuno-PCR for quantification of N protein was increased by up to 7-fold compared to analogous ELISA, having a limit of detection of 92 pg/mL and a limit of quantification of 840 pg/mL. The developed immuno-PCR method thus has the potential to be used as a new antigen test for COVID-19 and beyond.
PB  - Federation of European Biochemical Societies, Wiley
C3  - The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2
T1  - Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein
SP  - 44
EP  - 44
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6021
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Bićanin, Maša and Udovički, Božidar and Krstić-Ristivojević, Maja and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Accurately diagnosing people with suspected SARS-CoV-2 infection is essential to help manage COVID-19. Currently available SARS-CoV-2 diagnostics detect either RNA of the virus by RT-PCR or the presence of viral antigens in biological fluids by ELISA or similar techniques. Low sensitivity of antigen tests could lead to the risk of false negative results. Therefore, this study aimed to develop a highly sensitive immuno-PCR method for quantifying SARS-CoV-2 nucleocapsid (N) protein that combines the specificity of sandwich ELISA with the sensitivity of PCR. Recombinant N protein fragment was produced in E. coli as an expression system and purified using immobilized metal ion affinity chromatography. The antibodies against the N protein were raised in rabbits and mice. High-affinity polyclonal mice and rabbit N protein-specific antisera were purified using ammonium sulfate precipitation and used to develop sandwich ELISA for the quantification of N protein. Mice polyclonal serum was used as a capture for N protein. N
protein bound to mice antibodies was detected with rabbit polyclonal sera. A double-stranded amino-DNA molecule of 77 base pairs was PCR-synthesized, covalently conjugated to a secondary goat anti-rabbit antibody and subsequently amplified and quantified by real-time PCR. The results were compared to analogous sandwich ELISA consisting of alkaline phosphatase-labeled goat anti-rabbit antibody. The sensitivity of immuno-PCR for quantification of N protein was increased by up to 7-fold compared to analogous ELISA, having a limit of detection of 92 pg/mL and a limit of quantification of 840 pg/mL. The developed immuno-PCR method thus has the potential to be used as a new antigen test for COVID-19 and beyond.",
publisher = "Federation of European Biochemical Societies, Wiley",
journal = "The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2",
title = "Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein",
pages = "44-44",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6021"
}

Radomirović, M. Ž., Bićanin, M., Udovički, B., Krstić-Ristivojević, M., Đukić, T., Vasović, T., Jovanović, V., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein. in The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2
Federation of European Biochemical Societies, Wiley., 44-44.
https://hdl.handle.net/21.15107/rcub_cherry_6021

Radomirović MŽ, Bićanin M, Udovički B, Krstić-Ristivojević M, Đukić T, Vasović T, Jovanović V, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein. in The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2. 2023;:44-44.
https://hdl.handle.net/21.15107/rcub_cherry_6021 .

Radomirović, Mirjana Ž., Bićanin, Maša, Udovički, Božidar, Krstić-Ristivojević, Maja, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Development of immuno-PCR for sensitive quantification of SARS-CoV-2 nucleocapsid protein" in The 47th FEBS Congress, 8th-12th July, 2023. In: FEBS Open Bio, 13: Suppl. 2 (2023):44-44,
https://hdl.handle.net/21.15107/rcub_cherry_6021 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6020
AB  - Tropomyosin has been recognized as one of the most common allergens among shellfish allergens. Sensitive and specific quantification of traces of allergens present in food samples is of critical importance for people with food allergies. This study thus aimed to develop a highly sensitive immuno-PCR method for detecting crustacean tropomyosin in foods. Method couples conventional sandwich ELISA assay with real-time PCR amplification of marker DNA. Monoclonal mouse anti-tropomyosin antibody was used as a capture antibody, while polyclonal rabbit anti-tropomyosin antibody served as a detection antibody in sandwich ELISA. A double-stranded amino-DNA molecule of 77 base pairs was covalently conjugated to a secondary goat anti-rabbit antibody and subsequently amplified and quantified by real-time PCR. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. The sensitivity of immuno-PCR for quantification of tropomyosin was increased by up to 20-fold compared to ELISA, demonstrating accuracy as low as 19.8 pg/mL. Recovery of tropomyosin in vegetable soup as a food matrix was in the 87.7–115.6% range, with relative standard deviations in the 5–24.5% range. Tropomyosin was also quantified in the commercially available food products. Developed immuno-PCR technique thus shows the potential to be a method of choice for specific and ultrasensitive detection of tropomyosin in food samples, with the final aim of reducing risks of accidental food contamination.
PB  - Belgrade : Faculty of Chemistry
PB  - Belgrade : Serbian Biochemical Society
C3  - "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia
T1  - Immuno-PCR for crustacean tropomyosin quantification
SP  - 130
EP  - 130
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6020
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Tropomyosin has been recognized as one of the most common allergens among shellfish allergens. Sensitive and specific quantification of traces of allergens present in food samples is of critical importance for people with food allergies. This study thus aimed to develop a highly sensitive immuno-PCR method for detecting crustacean tropomyosin in foods. Method couples conventional sandwich ELISA assay with real-time PCR amplification of marker DNA. Monoclonal mouse anti-tropomyosin antibody was used as a capture antibody, while polyclonal rabbit anti-tropomyosin antibody served as a detection antibody in sandwich ELISA. A double-stranded amino-DNA molecule of 77 base pairs was covalently conjugated to a secondary goat anti-rabbit antibody and subsequently amplified and quantified by real-time PCR. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. The sensitivity of immuno-PCR for quantification of tropomyosin was increased by up to 20-fold compared to ELISA, demonstrating accuracy as low as 19.8 pg/mL. Recovery of tropomyosin in vegetable soup as a food matrix was in the 87.7–115.6% range, with relative standard deviations in the 5–24.5% range. Tropomyosin was also quantified in the commercially available food products. Developed immuno-PCR technique thus shows the potential to be a method of choice for specific and ultrasensitive detection of tropomyosin in food samples, with the final aim of reducing risks of accidental food contamination.",
publisher = "Belgrade : Faculty of Chemistry, Belgrade : Serbian Biochemical Society",
journal = ""Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia",
title = "Immuno-PCR for crustacean tropomyosin quantification",
pages = "130-130",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6020"
}

Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2023). Immuno-PCR for crustacean tropomyosin quantification. in "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia
Belgrade : Faculty of Chemistry., 130-130.
https://hdl.handle.net/21.15107/rcub_cherry_6020

Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Immuno-PCR for crustacean tropomyosin quantification. in "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia. 2023;:130-130.
https://hdl.handle.net/21.15107/rcub_cherry_6020 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Immuno-PCR for crustacean tropomyosin quantification" in "Biochemistry in Biotechnology", Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia (2023):130-130,
https://hdl.handle.net/21.15107/rcub_cherry_6020 .

TY  - JOUR
AU  - de Guzman, Maria Krishna
AU  - Anđelković, Mirjana
AU  - Jovanović, Vesna B.
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  - 181
SP  - 113846
DO  - 10.1016/j.marpolbul.2022.113846
ER  - 

@article{
author = "de Guzman, Maria Krishna and Anđelković, Mirjana and Jovanović, Vesna B. 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 = "181",
pages = "113846",
doi = "10.1016/j.marpolbul.2022.113846"
}

de Guzman, M. K., Anđelković, M., Jovanović, V. B., 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., 181, 113846.
https://doi.org/10.1016/j.marpolbul.2022.113846

de Guzman MK, Anđelković M, Jovanović VB, 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;181:113846.
doi:10.1016/j.marpolbul.2022.113846 .

de Guzman, Maria Krishna, Anđelković, Mirjana, Jovanović, Vesna B., 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, 181 (2022):113846,
https://doi.org/10.1016/j.marpolbul.2022.113846 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Čolaković, Maša
AU  - Pismestrović, Marina
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6027
AB  - Tropomyosin (TPM) is considered a major allergen among different shellfish species. Therefore, the development of methods for quantifying TPM in food products is crucial for allergic persons. Several extraction buffers were tested for their efficiency in recovering proteins from fresh frozen and cooked razor mud shrimp during 2 and 24 hours of extraction. The protein content was quantified using the Bradford protein assay. SDS-PAGE was used for protein profiling of soluble extracts. Sandwich ELISA was developed and used to quantify TPM content. None of the extraction buffers showed a significant difference in total protein content between 2 and 24 hours of extraction. Significantly fewer proteins were extracted from cooked shrimp compared to the raw shrimp. ELISA quantification showed that phosphate-buffered saline (PBS) containing 1 M NaCl (PBSN) and carbonate buffer, pH 10, extracted approximately 6 times higher amount of tropomyosin in comparison to PBS, highlighting the importance of choosing the appropriate extraction buffer for the precise quantification of TPM. Traditionally used extraction buffer PBS could significantly underestimate shrimp TPM content.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings
T1  - Optimization of extraction conditions of tropomyosin from razor mud shrimp and its quantification by developed ELISA
SP  - 64
EP  - 64
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6027
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Čolaković, Maša and Pismestrović, Marina and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Tropomyosin (TPM) is considered a major allergen among different shellfish species. Therefore, the development of methods for quantifying TPM in food products is crucial for allergic persons. Several extraction buffers were tested for their efficiency in recovering proteins from fresh frozen and cooked razor mud shrimp during 2 and 24 hours of extraction. The protein content was quantified using the Bradford protein assay. SDS-PAGE was used for protein profiling of soluble extracts. Sandwich ELISA was developed and used to quantify TPM content. None of the extraction buffers showed a significant difference in total protein content between 2 and 24 hours of extraction. Significantly fewer proteins were extracted from cooked shrimp compared to the raw shrimp. ELISA quantification showed that phosphate-buffered saline (PBS) containing 1 M NaCl (PBSN) and carbonate buffer, pH 10, extracted approximately 6 times higher amount of tropomyosin in comparison to PBS, highlighting the importance of choosing the appropriate extraction buffer for the precise quantification of TPM. Traditionally used extraction buffer PBS could significantly underestimate shrimp TPM content.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings",
title = "Optimization of extraction conditions of tropomyosin from razor mud shrimp and its quantification by developed ELISA",
pages = "64-64",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6027"
}

Radomirović, M. Ž., Čolaković, M., Pismestrović, M., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2022). Optimization of extraction conditions of tropomyosin from razor mud shrimp and its quantification by developed ELISA. in 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings
Beograd : Srpsko hemijsko društvo., 64-64.
https://hdl.handle.net/21.15107/rcub_cherry_6027

Radomirović MŽ, Čolaković M, Pismestrović M, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Optimization of extraction conditions of tropomyosin from razor mud shrimp and its quantification by developed ELISA. in 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings. 2022;:64-64.
https://hdl.handle.net/21.15107/rcub_cherry_6027 .

Radomirović, Mirjana Ž., Čolaković, Maša, Pismestrović, Marina, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Optimization of extraction conditions of tropomyosin from razor mud shrimp and its quantification by developed ELISA" in 58th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 9th-10th June, 2022. In: Book of Abstracts and Proceedings (2022):64-64,
https://hdl.handle.net/21.15107/rcub_cherry_6027 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6022
AB  - Tropomyosin (TPM) is considered a major allergen among different shellfish species. Developing sensitive, specific, and reliable methods for quantifying TPM in food products is crucial for persons allergic to shellfish. We have previously developed a highly sensitive sandwich ELISA method for quantifying shrimp TPM. Despite high amino acid sequence homology between shrimp and mussels TPM, the method has not been reliable for quantifying TPM from mussels, underestimating its concentration up to three orders of magnitude. Therefore, this work aimed to develop alternative immunological methods for mussel TPM quantification. Western blot, dot blot, and indirect ELISA using monoclonal anti-TPM antibody and alkaline phosphatase-labeled secondary antibody were developed and compared in terms of their sensitivity. Tropomyosin in mussels extracts was quantified using highly purified natural shrimp tropomyosin as standard. The linear range for TPM quantification using dot blot was between 5 and 50 µg/ml, while Western blot has slightly increased sensitivity, with a linear range between 1.25 and 12.5 µg/ml. Indirect ELISA has further improved the sensitivity of TPM quantification, with a 0.04-0.4 µg/ml linear range. Additional work will be performed to enhance the sensitivity of the presented methods, with the final aim of reducing risks of inadvertent food contamination.
PB  - Belgrade : Faculty of Chemistry
PB  - Belgrade : Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference, 22nd-23rd September, 2022. In: Conference Proceedings
T1  - Development and comparison of Western blot, dot blot and ELISA for mussels tropomyosin quantification
SP  - 125
EP  - 125
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6022
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Tropomyosin (TPM) is considered a major allergen among different shellfish species. Developing sensitive, specific, and reliable methods for quantifying TPM in food products is crucial for persons allergic to shellfish. We have previously developed a highly sensitive sandwich ELISA method for quantifying shrimp TPM. Despite high amino acid sequence homology between shrimp and mussels TPM, the method has not been reliable for quantifying TPM from mussels, underestimating its concentration up to three orders of magnitude. Therefore, this work aimed to develop alternative immunological methods for mussel TPM quantification. Western blot, dot blot, and indirect ELISA using monoclonal anti-TPM antibody and alkaline phosphatase-labeled secondary antibody were developed and compared in terms of their sensitivity. Tropomyosin in mussels extracts was quantified using highly purified natural shrimp tropomyosin as standard. The linear range for TPM quantification using dot blot was between 5 and 50 µg/ml, while Western blot has slightly increased sensitivity, with a linear range between 1.25 and 12.5 µg/ml. Indirect ELISA has further improved the sensitivity of TPM quantification, with a 0.04-0.4 µg/ml linear range. Additional work will be performed to enhance the sensitivity of the presented methods, with the final aim of reducing risks of inadvertent food contamination.",
publisher = "Belgrade : Faculty of Chemistry, Belgrade : Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference, 22nd-23rd September, 2022. In: Conference Proceedings",
title = "Development and comparison of Western blot, dot blot and ELISA for mussels tropomyosin quantification",
pages = "125-125",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6022"
}

Radomirović, M. Ž., Gligorijević, N., Rajković, A.,& Ćirković-Veličković, T.. (2022). Development and comparison of Western blot, dot blot and ELISA for mussels tropomyosin quantification. in Serbian Biochemical Society Eleventh Conference, 22nd-23rd September, 2022. In: Conference Proceedings
Belgrade : Faculty of Chemistry., 125-125.
https://hdl.handle.net/21.15107/rcub_cherry_6022

Radomirović MŽ, Gligorijević N, Rajković A, Ćirković-Veličković T. Development and comparison of Western blot, dot blot and ELISA for mussels tropomyosin quantification. in Serbian Biochemical Society Eleventh Conference, 22nd-23rd September, 2022. In: Conference Proceedings. 2022;:125-125.
https://hdl.handle.net/21.15107/rcub_cherry_6022 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Rajković, Andreja, Ćirković-Veličković, Tanja, "Development and comparison of Western blot, dot blot and ELISA for mussels tropomyosin quantification" in Serbian Biochemical Society Eleventh Conference, 22nd-23rd September, 2022. In: Conference Proceedings (2022):125-125,
https://hdl.handle.net/21.15107/rcub_cherry_6022 .

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 . .

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 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6025
AB  - Food allergies affect up to 10% of the general population and represent an important health problem in the field of food safety in industrialized countries. Hence, developing reliable, specific, and sensitive methods for detecting and quantifying allergens in food products is of high importance. Shellfish have been recognized as one of the eight most common sources of allergens, with tropomyosin (TPM) being considered a major heat-stable allergen, having a highly conserved amino acid sequence among different shellfish species. Allergenicity of TPM may change during food processing, such as cooking. The objective of this study was to develop an enzyme-linked immunosorbent assay (ELISA) for the detection and quantification of shellfish tropomyosin in food samples. 
Two different extraction buffers - phosphate-buffered saline (PBS) and PBS containing 1 M sodium-chloride (PBSN), were compared for their ability to recover proteins from pre-cooked frozen Mediterranean mussel (Mytilus galloprovincialis) and fresh frozen razor mud shrimp (Solenocera melantho). The samples were additionally cooked according to the manufacturer's instruction and analyzed as such. The protein content was quantified using Bradford protein assay, and the protein components of soluble extracts were profiled using SDS-PAGE. TPM presence was confirmed using Western blot. Sandwich ELISA was developed using a monoclonal anti-TPM antibody as a capture antibody, while polyclonal anti-TPM antibody served as a detection antibody and was coupled to the biotinylated secondary antibody and streptavidin-alkaline phosphatase conjugate. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. 
The profile of extracted proteins was changed when using PBSN instead of PBS. A higher concentration of proteins was recovered from raw shrimp using PBSN instead of PBS. At the same time, the type of extraction buffer did not affect protein recovery either from heated shrimp or pre-cooked/heated mussels. Significantly fewer proteins were extracted from cooked shrimp sample compared to the raw shrimp, while cooking showed no effect on the extraction of proteins from mussels. Cooking did not affect TPM recognition in Western blot. TPM was quantified in shrimp samples in sandwich ELISA. However, developed ELISA could not quantify mussel's TPM, indicating that this approach may distinguish mussels and shrimp TPM.
PB  - Sociedade Portuguesa de Química, Av. Da República, 45 – 3º Esq, 1050-187 Lisboa – Portugal
C3  - XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts
T1  - Extraction and quantification of tropomyosin in selected samples of shellfish
SP  - 118
EP  - 118
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6025
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Food allergies affect up to 10% of the general population and represent an important health problem in the field of food safety in industrialized countries. Hence, developing reliable, specific, and sensitive methods for detecting and quantifying allergens in food products is of high importance. Shellfish have been recognized as one of the eight most common sources of allergens, with tropomyosin (TPM) being considered a major heat-stable allergen, having a highly conserved amino acid sequence among different shellfish species. Allergenicity of TPM may change during food processing, such as cooking. The objective of this study was to develop an enzyme-linked immunosorbent assay (ELISA) for the detection and quantification of shellfish tropomyosin in food samples. 
Two different extraction buffers - phosphate-buffered saline (PBS) and PBS containing 1 M sodium-chloride (PBSN), were compared for their ability to recover proteins from pre-cooked frozen Mediterranean mussel (Mytilus galloprovincialis) and fresh frozen razor mud shrimp (Solenocera melantho). The samples were additionally cooked according to the manufacturer's instruction and analyzed as such. The protein content was quantified using Bradford protein assay, and the protein components of soluble extracts were profiled using SDS-PAGE. TPM presence was confirmed using Western blot. Sandwich ELISA was developed using a monoclonal anti-TPM antibody as a capture antibody, while polyclonal anti-TPM antibody served as a detection antibody and was coupled to the biotinylated secondary antibody and streptavidin-alkaline phosphatase conjugate. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. 
The profile of extracted proteins was changed when using PBSN instead of PBS. A higher concentration of proteins was recovered from raw shrimp using PBSN instead of PBS. At the same time, the type of extraction buffer did not affect protein recovery either from heated shrimp or pre-cooked/heated mussels. Significantly fewer proteins were extracted from cooked shrimp sample compared to the raw shrimp, while cooking showed no effect on the extraction of proteins from mussels. Cooking did not affect TPM recognition in Western blot. TPM was quantified in shrimp samples in sandwich ELISA. However, developed ELISA could not quantify mussel's TPM, indicating that this approach may distinguish mussels and shrimp TPM.",
publisher = "Sociedade Portuguesa de Química, Av. Da República, 45 – 3º Esq, 1050-187 Lisboa – Portugal",
journal = "XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts",
title = "Extraction and quantification of tropomyosin in selected samples of shellfish",
pages = "118-118",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6025"
}

Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković-Veličković, T.. (2021). Extraction and quantification of tropomyosin in selected samples of shellfish. in XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts
Sociedade Portuguesa de Química, Av. Da República, 45 – 3º Esq, 1050-187 Lisboa – Portugal., 118-118.
https://hdl.handle.net/21.15107/rcub_cherry_6025

Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković-Veličković T. Extraction and quantification of tropomyosin in selected samples of shellfish. in XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts. 2021;:118-118.
https://hdl.handle.net/21.15107/rcub_cherry_6025 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković-Veličković, Tanja, "Extraction and quantification of tropomyosin in selected samples of shellfish" in XXI EuroFoodChem conference, Virtual Congress, 22nd-24th November, 2021. In: Book of Abstracts (2021):118-118,
https://hdl.handle.net/21.15107/rcub_cherry_6025 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6033
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutually protective effect against the free radical-induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very small masking effect of the antioxidative potential of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021
T1  - Resveratrol and fibrinogen interactions
SP  - 15
EP  - 15
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6033
ER  - 

@conference{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, only to be later discovered that the presence of several antioxidants, including resveratrol, are responsible for it. We investigated if resveratrol has a more direct role in protection from harmful oxidation and development of thrombosis, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetric analysis demonstrated binding of resveratrol to fibrinogen, the main protein in the coagulation process, which also has an important application as a food additive in making of fibrin gels. Various spectroscopic methods have demonstrated that binding of resveratrol does not unfold or destabilize fibrinogen since both near and far-UV CD spectra as well as its melting temperature remained unchanged. A mutually protective effect against the free radical-induced oxidation of resveratrol and fibrinogen was found. The presence of fibrinogen caused a very small masking effect of the antioxidative potential of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing potential bioavailability and activity of resveratrol in circulation. By direct interaction and protection of fibrinogen, resveratrol may serve as an important antioxidant for prevention of thrombosis. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021",
title = "Resveratrol and fibrinogen interactions",
pages = "15-15",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6033"
}

Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T.. (2021). Resveratrol and fibrinogen interactions. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021, 15-15.
https://hdl.handle.net/21.15107/rcub_cherry_6033

Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Resveratrol and fibrinogen interactions. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. 2021;:15-15.
https://hdl.handle.net/21.15107/rcub_cherry_6033 .

Gligorijević, Nikola, Radomirović, Mirjana Ž., Rajković, Andreja, Nedić, Olgica, Ćirković-Veličković, Tanja, "Resveratrol and fibrinogen interactions" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021 (2021):15-15,
https://hdl.handle.net/21.15107/rcub_cherry_6033 .

TY  - CONF
AU  - Khulal, Urmila
AU  - Radomirović, Mirjana Ž.
AU  - de Guzman, Maria Krishna
AU  - Mutić, Jelena
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6034
AB  - Tropomyosin (TM) is known to be a major shrimp allergen (e.g., Pen m 1) and considered a cross-reacting panallergen among shellfish/invertebrates. The clam TM is also considered its major allergen but has not been widely studied. The food processing techniques can alter the TM allergenicity. Hence, the objective of this research is to detect and quantify TM in fresh and differentially treated clams collected in Korea via in-house developed sandwich ELISA protocol to evaluate the effect of various real-life processing techniques on TM stability.
Freshly bought live clams (FC), 4 groups of randomly selected equal number of similarly sized clams were differentially treated. Fresh and packaged (FPC), fresh and frozen at -20◦C (FroC). The fresh clams boiled (BC) in boiling water and the marinated clams (MC) suspended in marinade solution for 5 days; soluble protein extracted overnight from 5 samples in PBS buffer with protease inhibitor; BCA assay determined the protein content; capture-detection-enzyme linked secondary antibody in-house ELISA. ELISA was validated with specific antibody based Western blot (WB).
The total soluble protein content of raw clams (FC, FPC, FroC) was between 2.8-4.9 mg/ml. The cooked clams (BC, MC) lost total protein during the cooking and was determined <1 mg/ml. The leaked protein in boiled water (BW) and marinade solution (MS) was confirmed with the protein assay as 0.48 mg/ml and 5.5 mg/ml, respectively. ELISA quantified TM (pg/ml) in FPC =BC (610) >FroC (290) >FC (75) >MC. It (and WB) showed that boiling has no effect on heat stable TM IgG binding, BW contained considerable amount of TM (with pronounced IgG binding). MC, however showed no TM epitope recognition in WB (no band in SDS PAGE) and was not quantified by ELISA nor in MS (<LLOQ). Marination might degrade the TM to significant extent possibly altering the allergenicity.
PB  - Belgrade : Faculty of Chemistry
C3  - FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts
T1  - Detection and quantification of tropomyosin in differentially treated clams from Korea
SP  - 25
EP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6034
ER  - 

@conference{
author = "Khulal, Urmila and Radomirović, Mirjana Ž. and de Guzman, Maria Krishna and Mutić, Jelena and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Tropomyosin (TM) is known to be a major shrimp allergen (e.g., Pen m 1) and considered a cross-reacting panallergen among shellfish/invertebrates. The clam TM is also considered its major allergen but has not been widely studied. The food processing techniques can alter the TM allergenicity. Hence, the objective of this research is to detect and quantify TM in fresh and differentially treated clams collected in Korea via in-house developed sandwich ELISA protocol to evaluate the effect of various real-life processing techniques on TM stability.
Freshly bought live clams (FC), 4 groups of randomly selected equal number of similarly sized clams were differentially treated. Fresh and packaged (FPC), fresh and frozen at -20◦C (FroC). The fresh clams boiled (BC) in boiling water and the marinated clams (MC) suspended in marinade solution for 5 days; soluble protein extracted overnight from 5 samples in PBS buffer with protease inhibitor; BCA assay determined the protein content; capture-detection-enzyme linked secondary antibody in-house ELISA. ELISA was validated with specific antibody based Western blot (WB).
The total soluble protein content of raw clams (FC, FPC, FroC) was between 2.8-4.9 mg/ml. The cooked clams (BC, MC) lost total protein during the cooking and was determined <1 mg/ml. The leaked protein in boiled water (BW) and marinade solution (MS) was confirmed with the protein assay as 0.48 mg/ml and 5.5 mg/ml, respectively. ELISA quantified TM (pg/ml) in FPC =BC (610) >FroC (290) >FC (75) >MC. It (and WB) showed that boiling has no effect on heat stable TM IgG binding, BW contained considerable amount of TM (with pronounced IgG binding). MC, however showed no TM epitope recognition in WB (no band in SDS PAGE) and was not quantified by ELISA nor in MS (<LLOQ). Marination might degrade the TM to significant extent possibly altering the allergenicity.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts",
title = "Detection and quantification of tropomyosin in differentially treated clams from Korea",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6034"
}

Khulal, U., Radomirović, M. Ž., de Guzman, M. K., Mutić, J., Rajković, A.,& Ćirković-Veličković, T.. (2021). Detection and quantification of tropomyosin in differentially treated clams from Korea. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts
Belgrade : Faculty of Chemistry., 25-25.
https://hdl.handle.net/21.15107/rcub_cherry_6034

Khulal U, Radomirović MŽ, de Guzman MK, Mutić J, Rajković A, Ćirković-Veličković T. Detection and quantification of tropomyosin in differentially treated clams from Korea. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts. 2021;:25-25.
https://hdl.handle.net/21.15107/rcub_cherry_6034 .

Khulal, Urmila, Radomirović, Mirjana Ž., de Guzman, Maria Krishna, Mutić, Jelena, Rajković, Andreja, Ćirković-Veličković, Tanja, "Detection and quantification of tropomyosin in differentially treated clams from Korea" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts (2021):25-25,
https://hdl.handle.net/21.15107/rcub_cherry_6034 .

TY  - DATA
AU  - Khulal, Urmila
AU  - Ghnimi, Sami
AU  - Stevanović, Nikola R.
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4747
PB  - Elsevier
T2  - LWT
T1  - Supplementary data for the article: Khulal, U.; Ghnimi, S.; Stevanovic, N.; Rajkovic, A.; Cirkovic Velickovic, T. Aggregability and Digestibility Study of Fruit Juice Fortified Camel Milk Powder Proteins. LWT 2021, 152, 112250. https://doi.org/10.1016/j.lwt.2021.112250.
VL  - 152
SP  - 112250
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4747
ER  - 

@misc{
author = "Khulal, Urmila and Ghnimi, Sami and Stevanović, Nikola R. and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "LWT",
title = "Supplementary data for the article: Khulal, U.; Ghnimi, S.; Stevanovic, N.; Rajkovic, A.; Cirkovic Velickovic, T. Aggregability and Digestibility Study of Fruit Juice Fortified Camel Milk Powder Proteins. LWT 2021, 152, 112250. https://doi.org/10.1016/j.lwt.2021.112250.",
volume = "152",
pages = "112250",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4747"
}

Khulal, U., Ghnimi, S., Stevanović, N. R., Rajković, A.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Khulal, U.; Ghnimi, S.; Stevanovic, N.; Rajkovic, A.; Cirkovic Velickovic, T. Aggregability and Digestibility Study of Fruit Juice Fortified Camel Milk Powder Proteins. LWT 2021, 152, 112250. https://doi.org/10.1016/j.lwt.2021.112250.. in LWT
Elsevier., 152, 112250.
https://hdl.handle.net/21.15107/rcub_cherry_4747

Khulal U, Ghnimi S, Stevanović NR, Rajković A, Ćirković-Veličković T. Supplementary data for the article: Khulal, U.; Ghnimi, S.; Stevanovic, N.; Rajkovic, A.; Cirkovic Velickovic, T. Aggregability and Digestibility Study of Fruit Juice Fortified Camel Milk Powder Proteins. LWT 2021, 152, 112250. https://doi.org/10.1016/j.lwt.2021.112250.. in LWT. 2021;152:112250.
https://hdl.handle.net/21.15107/rcub_cherry_4747 .

Khulal, Urmila, Ghnimi, Sami, Stevanović, Nikola R., Rajković, Andreja, Ćirković-Veličković, Tanja, "Supplementary data for the article: Khulal, U.; Ghnimi, S.; Stevanovic, N.; Rajkovic, A.; Cirkovic Velickovic, T. Aggregability and Digestibility Study of Fruit Juice Fortified Camel Milk Powder Proteins. LWT 2021, 152, 112250. https://doi.org/10.1016/j.lwt.2021.112250." in LWT, 152 (2021):112250,
https://hdl.handle.net/21.15107/rcub_cherry_4747 .

TY  - JOUR
AU  - Mutić, Jelena
AU  - Jovanović, Vesna B.
AU  - Jacxsens, Liesbeth
AU  - Tondeleir, Jannes
AU  - Ristivojević, Petar
AU  - Đurđić, Slađana Z.
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4825
AB  - Bivalves are a good source of nutrients but also a potential source of environmental contaminants, which could pose a risk for consumers. The aims of this study were: the determination of 16 elements by ICP-MS in 48 samples of five bivalve species purchased from market in Korea; the identification of elements useful for species classification using multivariate analyses; and the benefit-risk evaluation associated to the consumption of these bivalves. The highest difference among content of elements between species was found for Cd, Mn, Ni, Zn, and Fe. Partial last squares discriminant analysis revealed elements with a VIP score >1 which were considered as the most relevant for explaining certain species. As, Cd, Co, and Ni were found as taxonomical markers of V. philippinarum; Mn, Zn, Mg, and Na of A. irradians; and Cd, Ni, and Fe of M. yessoensis. These species could serve as good dietary sources of essential elements. Cd exposure by consumption of Manila clams is not representing a health risk for the Korean population; however, through consumption of Yesso scallops, 5.3% of the Korean population has a potential health risk. Removal of the digestive gland before eating will drastically reduce the amount of Cd ingested.
PB  - MDPI
T2  - Foods
T1  - Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation
VL  - 10
IS  - 11
SP  - 2690
DO  - 10.3390/foods10112690
ER  - 

@article{
author = "Mutić, Jelena and Jovanović, Vesna B. and Jacxsens, Liesbeth and Tondeleir, Jannes and Ristivojević, Petar and Đurđić, Slađana Z. and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Bivalves are a good source of nutrients but also a potential source of environmental contaminants, which could pose a risk for consumers. The aims of this study were: the determination of 16 elements by ICP-MS in 48 samples of five bivalve species purchased from market in Korea; the identification of elements useful for species classification using multivariate analyses; and the benefit-risk evaluation associated to the consumption of these bivalves. The highest difference among content of elements between species was found for Cd, Mn, Ni, Zn, and Fe. Partial last squares discriminant analysis revealed elements with a VIP score >1 which were considered as the most relevant for explaining certain species. As, Cd, Co, and Ni were found as taxonomical markers of V. philippinarum; Mn, Zn, Mg, and Na of A. irradians; and Cd, Ni, and Fe of M. yessoensis. These species could serve as good dietary sources of essential elements. Cd exposure by consumption of Manila clams is not representing a health risk for the Korean population; however, through consumption of Yesso scallops, 5.3% of the Korean population has a potential health risk. Removal of the digestive gland before eating will drastically reduce the amount of Cd ingested.",
publisher = "MDPI",
journal = "Foods",
title = "Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation",
volume = "10",
number = "11",
pages = "2690",
doi = "10.3390/foods10112690"
}

Mutić, J., Jovanović, V. B., Jacxsens, L., Tondeleir, J., Ristivojević, P., Đurđić, S. Z., Rajković, A.,& Ćirković-Veličković, T.. (2021). Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. in Foods
MDPI., 10(11), 2690.
https://doi.org/10.3390/foods10112690

Mutić J, Jovanović VB, Jacxsens L, Tondeleir J, Ristivojević P, Đurđić SZ, Rajković A, Ćirković-Veličković T. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. in Foods. 2021;10(11):2690.
doi:10.3390/foods10112690 .

Mutić, Jelena, Jovanović, Vesna B., Jacxsens, Liesbeth, Tondeleir, Jannes, Ristivojević, Petar, Đurđić, Slađana Z., Rajković, Andreja, Ćirković-Veličković, Tanja, "Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation" in Foods, 10, no. 11 (2021):2690,
https://doi.org/10.3390/foods10112690 . .

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

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

Mutić, J., Jovanović, V. B., Jacxsens, L., Tondeleir, J., Ristivojević, P., Đurđić, S. Z., Rajković, A.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.. in Foods
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_4826

Mutić J, Jovanović VB, Jacxsens L, Tondeleir J, Ristivojević P, Đurđić SZ, Rajković A, Ćirković-Veličković T. Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690.. in Foods. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4826 .

Mutić, Jelena, Jovanović, Vesna B., Jacxsens, Liesbeth, Tondeleir, Jannes, Ristivojević, Petar, Đurđić, Slađana Z., Rajković, Andreja, Ćirković-Veličković, Tanja, "Supplementary data for the article: Mutić, J.; Jovanović, V.; Jacxsens, L.; Tondeleir, J.; Ristivojević, P.; Djurdjić, S.; Rajković, A.; Veličković, T. Ć. Chemical Content of Five Molluscan Bivalve Species Collected from South Korea: Multivariate Study and Safety Evaluation. Foods 2021, 10 (11), 2690. https://doi.org/10.3390/foods10112690." in Foods (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4826 .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Ghnimi, Sami
AU  - Stevanović, Nikola R.
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4746
AB  - In this work, we observed the effect of grape juice (% concentrated juice/% concentrated camel milk: GJ20/80, GJ50/50) and pomegranate juice (PJ20/80, PJ40/60) fortification on camel milk (CM) protein solubility and digestibility. Proteins were dissolved in sodium phosphate buffer to 50 mg/ml and defatted prior Bradford assay of protein concentration, then analyzed by Size Exclusion-Ultra High-Performance Liquid chromatography (SE-UHPLC). The CM protein aggregation and their stability were further monitored at different pH 2.0, 4.0, and 7.5 via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Freeze dried CM (FDCM) was the reference sample and our results showed that GJ50/50 and PJ40/60 with the highest fruit juice ratio had the lowest protein content in the supernatant, hence the decreased solubility. SE-UHPLC of supernatants showed a slight decrease in retention times of 11 kDa and 62 kDa proteins for GJ50/50 and PJ40/60 suggesting a possibility of adduct formation due to fortification leading to higher molecular weight. The simulated static in vitro gastrointestinal digestion of samples revealed that most soluble proteins were readily digested by pepsin, trypsin and chymotrypsin enzymes leading to small peptides. However, the SDS PAGE of pellets showed the partial resistance of casein and α-lactalbumin against peptic digestion.
PB  - Elsevier
T2  - LWT
T1  - Aggregability and digestibility study of fruit juice fortified camel milk powder proteins
VL  - 152
SP  - 112250
DO  - 10.1016/j.lwt.2021.112250
ER  - 

@article{
author = "Khulal, Urmila and Ghnimi, Sami and Stevanović, Nikola R. and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "In this work, we observed the effect of grape juice (% concentrated juice/% concentrated camel milk: GJ20/80, GJ50/50) and pomegranate juice (PJ20/80, PJ40/60) fortification on camel milk (CM) protein solubility and digestibility. Proteins were dissolved in sodium phosphate buffer to 50 mg/ml and defatted prior Bradford assay of protein concentration, then analyzed by Size Exclusion-Ultra High-Performance Liquid chromatography (SE-UHPLC). The CM protein aggregation and their stability were further monitored at different pH 2.0, 4.0, and 7.5 via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Freeze dried CM (FDCM) was the reference sample and our results showed that GJ50/50 and PJ40/60 with the highest fruit juice ratio had the lowest protein content in the supernatant, hence the decreased solubility. SE-UHPLC of supernatants showed a slight decrease in retention times of 11 kDa and 62 kDa proteins for GJ50/50 and PJ40/60 suggesting a possibility of adduct formation due to fortification leading to higher molecular weight. The simulated static in vitro gastrointestinal digestion of samples revealed that most soluble proteins were readily digested by pepsin, trypsin and chymotrypsin enzymes leading to small peptides. However, the SDS PAGE of pellets showed the partial resistance of casein and α-lactalbumin against peptic digestion.",
publisher = "Elsevier",
journal = "LWT",
title = "Aggregability and digestibility study of fruit juice fortified camel milk powder proteins",
volume = "152",
pages = "112250",
doi = "10.1016/j.lwt.2021.112250"
}

Khulal, U., Ghnimi, S., Stevanović, N. R., Rajković, A.,& Ćirković-Veličković, T.. (2021). Aggregability and digestibility study of fruit juice fortified camel milk powder proteins. in LWT
Elsevier., 152, 112250.
https://doi.org/10.1016/j.lwt.2021.112250

Khulal U, Ghnimi S, Stevanović NR, Rajković A, Ćirković-Veličković T. Aggregability and digestibility study of fruit juice fortified camel milk powder proteins. in LWT. 2021;152:112250.
doi:10.1016/j.lwt.2021.112250 .

Khulal, Urmila, Ghnimi, Sami, Stevanović, Nikola R., Rajković, Andreja, Ćirković-Veličković, Tanja, "Aggregability and digestibility study of fruit juice fortified camel milk powder proteins" in LWT, 152 (2021):112250,
https://doi.org/10.1016/j.lwt.2021.112250 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
AU  - Rajković, Andreja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6036
AB  - Food allergies represent important health problem in industrialized countries, with seafood being recognized as one of the 8 most common sources of allergens. While there are several proteins that have been linked to shellfish allergy, tropomyosin accounts for majority of diagnozed ingestion-related shellfish allergies. Presence of even traces of allergens in food can be a serious health hazard to consumers, which is why proper labeling of food products by food manufacturers is of critical importance for sensitized persons. On the other hand, development of reliable, specific and sensitive methods for detection and quantification of allergens in food products is of the high importance as well. The objective of this study was to develop highly sensitive immuno-polymerase chain reaction (immuno PCR) method for the detection and quantification of shellfish tropomyosin in food samples. Immuno PCR method couples standard sandwich enzyme-linked immunosorbent assay (ELISA) format with real time PCR. Monoclonal antibody was used as capture antibody, while biotinylated polyclonal antibody served as detection antibody. Reporter biotinylated DNA was coupled to detection antibody via streptavidin and subsequently amplified and quantified by real time PCR. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. The results were compared to standard sandwich ELISA.
PB  - University of Vienna
C3  - 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts
T1  - Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin
SP  - S4
EP  - S4
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6036
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja and Rajković, Andreja",
year = "2020",
abstract = "Food allergies represent important health problem in industrialized countries, with seafood being recognized as one of the 8 most common sources of allergens. While there are several proteins that have been linked to shellfish allergy, tropomyosin accounts for majority of diagnozed ingestion-related shellfish allergies. Presence of even traces of allergens in food can be a serious health hazard to consumers, which is why proper labeling of food products by food manufacturers is of critical importance for sensitized persons. On the other hand, development of reliable, specific and sensitive methods for detection and quantification of allergens in food products is of the high importance as well. The objective of this study was to develop highly sensitive immuno-polymerase chain reaction (immuno PCR) method for the detection and quantification of shellfish tropomyosin in food samples. Immuno PCR method couples standard sandwich enzyme-linked immunosorbent assay (ELISA) format with real time PCR. Monoclonal antibody was used as capture antibody, while biotinylated polyclonal antibody served as detection antibody. Reporter biotinylated DNA was coupled to detection antibody via streptavidin and subsequently amplified and quantified by real time PCR. Tropomyosin was quantified using highly purified natural shrimp tropomyosin as standard. The results were compared to standard sandwich ELISA.",
publisher = "University of Vienna",
journal = "2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts",
title = "Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin",
pages = "S4-S4",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6036"
}

Radomirović, M. Ž., Ćirković-Veličković, T.,& Rajković, A.. (2020). Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin. in 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts
University of Vienna., S4-S4.
https://hdl.handle.net/21.15107/rcub_cherry_6036

Radomirović MŽ, Ćirković-Veličković T, Rajković A. Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin. in 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts. 2020;:S4-S4.
https://hdl.handle.net/21.15107/rcub_cherry_6036 .

Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, Rajković, Andreja, "Development of an immuno-polymerase chain reaction for detection and quantification of shellfish tropomyosin" in 2nd FoodEnTwin Workshop “Experimental animal models for food and environment”, Vienna, Austria, 3rd-4th February, 2020. In: Book of Abstracts (2020):S4-S4,
https://hdl.handle.net/21.15107/rcub_cherry_6036 .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4235
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Foods
T1  - Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation
VL  - 9
IS  - 6
SP  - 780
DO  - 10.3390/foods9060780
ER  - 

@article{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Foods",
title = "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation",
volume = "9",
number = "6",
pages = "780",
doi = "10.3390/foods9060780"
}

Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T.. (2020). Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods
Multidisciplinary Digital Publishing Institute (MDPI)., 9(6), 780.
https://doi.org/10.3390/foods9060780

Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods. 2020;9(6):780.
doi:10.3390/foods9060780 .

Gligorijević, Nikola, Radomirović, Mirjana Ž., Rajković, Andreja, Nedić, Olgica, Ćirković-Veličković, Tanja, "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation" in Foods, 9, no. 6 (2020):780,
https://doi.org/10.3390/foods9060780 . .