TY  - CONF
AU  - Jovanović, Vesna
AU  - Radomirović, Mirjana Ž.
AU  - Krstić-Ristivojević, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6023
AB  - In the last several decades, the trend of seafood consumption has significantly increased not only in the countries with a tradition of seafood consumption, but also in other ones [1]. The increase in the world's population and the awareness of healthy food, the globalization of markets, and the development of aquaculture are some of the factors that have led to this trend. The aquaculture of shellfish like clams, mussels, oysters and scallops has been very developed all around the world and the food products based on them have become part of the daily diet for many consumers. In addition, these food products are considered healthy food because of the high content of proteins and essential fatty acids, but their consumption may carry some risks of food allergy. Tropomyosin from shellfish (TPM) is the major allergen responsible for the development of anaphylaxis in persons with food allergy. The content of TPM in shellfish and its bioavailability from food products can have potential influence on the sensitization of consumers to TPM. It is known that food processing can change the bioavailability of food allergens [2]. The main goal of this study was the investigation of how processing and packaging of shellfish samples can affect the content of TPM in them.
For this study, clam Venerupis philippinarum was chosen as the species with the highest world aquaculture production [1]. After the purchasing of live clams, the animals were separated into 5 groups for the next treatments: fresh live (control group), freshly removed inner content was kept at +4°C for 3 days (three days` shelf-life), frozen in a plastic bag and kept at -20 °C during 7 days, marinated and kept in a glass jar at room temperature during 8 days and freshly boiled. After processing and packaging of samples, the total protein extracts were prepared in 10 mM sodium phosphate buffer pH 7.4 1M NaCl, 1 mM PMSF and the concentration of total proteins was determined by BCA method. The concentration of TPM in the total protein extracts was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) using in-house prepared clams` TPM standard. The content of TPM (μg) in the samples was expressed per mg of extracted soluble proteins, individual animal and grams of soft wet tissue.
The cooked samples have significantly higher TPM content expressed per gram of soft wet tissue compared to all other treatments. Food processing such as freezing, marinating, or extending the shelf-life at 4°C by 3 days has very little effect on the change in TPM content per gram of soft wet tissue compared to the fresh samples. The processing of clams, like cooking or marinating, caused the content of total soluble extracted proteins to be three to four times lower compared to the other three treatments. In these samples the obtained ratio of the total TPM/ total soluble extracted proteins ratio was the highest. This result can be explained by the fact that TPM is thermostable and stays soluble after cooking, while other proteins become insoluble because of denaturation. The lower ratio of TPM/ total soluble extracted proteins was found in marinated samples compared to the cooked samples. The lowest total tropomyosin/ total soluble extracted proteins ratio was found in 3 days’ shelf-life. Treatments like cooking, marinating and keeping the inner content of the shell at +4°C can significantly affect extractability of proteins, particularly affecting the ratio of major allergen TPM in the total protein extracts. Further studies are needed to examine bioaccessibility of TPM in different biologically relevant fluids (gastric/intestinal) and during digestion in relation to the processing conditions.
PB  - Beograd : Srpsko hemijsko društvo
C3  - XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.
T1  - The effect of food processing and packaging of clams on the content of tropomyosin
SP  - 240
EP  - 240
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6023
ER  - 

@conference{
author = "Jovanović, Vesna and Radomirović, Mirjana Ž. and Krstić-Ristivojević, Maja and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "In the last several decades, the trend of seafood consumption has significantly increased not only in the countries with a tradition of seafood consumption, but also in other ones [1]. The increase in the world's population and the awareness of healthy food, the globalization of markets, and the development of aquaculture are some of the factors that have led to this trend. The aquaculture of shellfish like clams, mussels, oysters and scallops has been very developed all around the world and the food products based on them have become part of the daily diet for many consumers. In addition, these food products are considered healthy food because of the high content of proteins and essential fatty acids, but their consumption may carry some risks of food allergy. Tropomyosin from shellfish (TPM) is the major allergen responsible for the development of anaphylaxis in persons with food allergy. The content of TPM in shellfish and its bioavailability from food products can have potential influence on the sensitization of consumers to TPM. It is known that food processing can change the bioavailability of food allergens [2]. The main goal of this study was the investigation of how processing and packaging of shellfish samples can affect the content of TPM in them.
For this study, clam Venerupis philippinarum was chosen as the species with the highest world aquaculture production [1]. After the purchasing of live clams, the animals were separated into 5 groups for the next treatments: fresh live (control group), freshly removed inner content was kept at +4°C for 3 days (three days` shelf-life), frozen in a plastic bag and kept at -20 °C during 7 days, marinated and kept in a glass jar at room temperature during 8 days and freshly boiled. After processing and packaging of samples, the total protein extracts were prepared in 10 mM sodium phosphate buffer pH 7.4 1M NaCl, 1 mM PMSF and the concentration of total proteins was determined by BCA method. The concentration of TPM in the total protein extracts was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) using in-house prepared clams` TPM standard. The content of TPM (μg) in the samples was expressed per mg of extracted soluble proteins, individual animal and grams of soft wet tissue.
The cooked samples have significantly higher TPM content expressed per gram of soft wet tissue compared to all other treatments. Food processing such as freezing, marinating, or extending the shelf-life at 4°C by 3 days has very little effect on the change in TPM content per gram of soft wet tissue compared to the fresh samples. The processing of clams, like cooking or marinating, caused the content of total soluble extracted proteins to be three to four times lower compared to the other three treatments. In these samples the obtained ratio of the total TPM/ total soluble extracted proteins ratio was the highest. This result can be explained by the fact that TPM is thermostable and stays soluble after cooking, while other proteins become insoluble because of denaturation. The lower ratio of TPM/ total soluble extracted proteins was found in marinated samples compared to the cooked samples. The lowest total tropomyosin/ total soluble extracted proteins ratio was found in 3 days’ shelf-life. Treatments like cooking, marinating and keeping the inner content of the shell at +4°C can significantly affect extractability of proteins, particularly affecting the ratio of major allergen TPM in the total protein extracts. Further studies are needed to examine bioaccessibility of TPM in different biologically relevant fluids (gastric/intestinal) and during digestion in relation to the processing conditions.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.",
title = "The effect of food processing and packaging of clams on the content of tropomyosin",
pages = "240-240",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6023"
}

Jovanović, V., Radomirović, M. Ž., Krstić-Ristivojević, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2023). The effect of food processing and packaging of clams on the content of tropomyosin. in XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.
Beograd : Srpsko hemijsko društvo., 240-240.
https://hdl.handle.net/21.15107/rcub_cherry_6023

Jovanović V, Radomirović MŽ, Krstić-Ristivojević M, Stanić-Vučinić D, Ćirković-Veličković T. The effect of food processing and packaging of clams on the content of tropomyosin. in XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.. 2023;:240-240.
https://hdl.handle.net/21.15107/rcub_cherry_6023 .

Jovanović, Vesna, Radomirović, Mirjana Ž., Krstić-Ristivojević, Maja, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "The effect of food processing and packaging of clams on the content of tropomyosin" in XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023. (2023):240-240,
https://hdl.handle.net/21.15107/rcub_cherry_6023 .

TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Jovanović, Vesna
AU  - Radomirović, Mirjana Ž.
AU  - Trifunović, Olga
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6024
AB  - In the last 50 years, the annual per capita consumption of seafood products worldwide has more than doubled, from almost 10 kg in 1960 to over 20 kg in 2014. Seafood protein is an essential part of the diet in many countries, particularly where total protein intake is low [1]. However, as defined by the European Community, fish, and shellfish tropomyosins (TPM) are major allergens and major causes of anaphylaxis [2]. The increasing prevalence of food allergies is consistent with the increasing pollution of soil and water with plastic particles. To investigate the potential link between increasing plastic pollution and increasing food allergy prevalence, we aim to develop methods for precise and accurate monitoring of allergens and plastic in real seafood samples.
TPM was isolated from shrimp (Litopenaeus vannamei), clams (Venerupis philippinarum), and mussels (Mytilus galloprovincialis). The obtained in-house TPM proteins from three different sources were resolved using two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The concentration of TPM in seashell samples from different geographical origin was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) with prior optimization of adequate TPM standard curve using commercial and non-commercial in-house prepared TPM standards.
TPM standards resolved via 2D-PAGE revealed the presence of two isoforms of shrimp and mussels TPM standard, one dominant and one less abundant isoform. Two isoforms from both seafood sources, shrimp and mussels, are slightly different in molecular weight and pI value. As for the TPM standard obtained from clams, the 2D electrophoregram showed possibly eight isoforms with small differences in mass and pI values. Furthermore, the presence of three dominant isoforms can be observed that differ slightly in molecular mass, while other isoforms also differ in pI value. The ELISA results, regarding TPM standard curve optimization, showed that in both the commercial shrimp TPM and in-house shrimp TPM standards, sigmoidal concentration dependence is present in a range of 50 to 0.05 ng/ml, using serial double dilutions. On the other hand, TPM standards isolated from mussels and clams show sigmoidal concentration dependence in the range of 45 to 0.044 μg/ml with using the identical combination of capture and detection antibodies and serial double dilutions. TPM concentrations in clams and mussel samples extrapolated from standard curves of commercial shrimp TPM standard and corresponding in-house TPM standards are presented in Table 1.
Differences in TPM concentration of the same sample using different TPM standards differ from 40 to 600 times, which strongly indicates that the right choice of TPM standard is a critical step for accurate and precise determination of TPM concentration in seafood samples.
PB  - Beograd : Srpsko hemijsko društvo
C3  - XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts
T1  - Tropomyosin quantification in seafood samples-right choice of standard makes a difference
SP  - 132
EP  - 132
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6024
ER  - 

@conference{
author = "Krstić-Ristivojević, Maja and Jovanović, Vesna and Radomirović, Mirjana Ž. and Trifunović, Olga and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "In the last 50 years, the annual per capita consumption of seafood products worldwide has more than doubled, from almost 10 kg in 1960 to over 20 kg in 2014. Seafood protein is an essential part of the diet in many countries, particularly where total protein intake is low [1]. However, as defined by the European Community, fish, and shellfish tropomyosins (TPM) are major allergens and major causes of anaphylaxis [2]. The increasing prevalence of food allergies is consistent with the increasing pollution of soil and water with plastic particles. To investigate the potential link between increasing plastic pollution and increasing food allergy prevalence, we aim to develop methods for precise and accurate monitoring of allergens and plastic in real seafood samples.
TPM was isolated from shrimp (Litopenaeus vannamei), clams (Venerupis philippinarum), and mussels (Mytilus galloprovincialis). The obtained in-house TPM proteins from three different sources were resolved using two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The concentration of TPM in seashell samples from different geographical origin was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) with prior optimization of adequate TPM standard curve using commercial and non-commercial in-house prepared TPM standards.
TPM standards resolved via 2D-PAGE revealed the presence of two isoforms of shrimp and mussels TPM standard, one dominant and one less abundant isoform. Two isoforms from both seafood sources, shrimp and mussels, are slightly different in molecular weight and pI value. As for the TPM standard obtained from clams, the 2D electrophoregram showed possibly eight isoforms with small differences in mass and pI values. Furthermore, the presence of three dominant isoforms can be observed that differ slightly in molecular mass, while other isoforms also differ in pI value. The ELISA results, regarding TPM standard curve optimization, showed that in both the commercial shrimp TPM and in-house shrimp TPM standards, sigmoidal concentration dependence is present in a range of 50 to 0.05 ng/ml, using serial double dilutions. On the other hand, TPM standards isolated from mussels and clams show sigmoidal concentration dependence in the range of 45 to 0.044 μg/ml with using the identical combination of capture and detection antibodies and serial double dilutions. TPM concentrations in clams and mussel samples extrapolated from standard curves of commercial shrimp TPM standard and corresponding in-house TPM standards are presented in Table 1.
Differences in TPM concentration of the same sample using different TPM standards differ from 40 to 600 times, which strongly indicates that the right choice of TPM standard is a critical step for accurate and precise determination of TPM concentration in seafood samples.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts",
title = "Tropomyosin quantification in seafood samples-right choice of standard makes a difference",
pages = "132-132",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6024"
}

Krstić-Ristivojević, M., Jovanović, V., Radomirović, M. Ž., Trifunović, O., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2023). Tropomyosin quantification in seafood samples-right choice of standard makes a difference. in XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts
Beograd : Srpsko hemijsko društvo., 132-132.
https://hdl.handle.net/21.15107/rcub_cherry_6024

Krstić-Ristivojević M, Jovanović V, Radomirović MŽ, Trifunović O, Stanić-Vučinić D, Ćirković-Veličković T. Tropomyosin quantification in seafood samples-right choice of standard makes a difference. in XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts. 2023;:132-132.
https://hdl.handle.net/21.15107/rcub_cherry_6024 .

Krstić-Ristivojević, Maja, Jovanović, Vesna, Radomirović, Mirjana Ž., Trifunović, Olga, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Tropomyosin quantification in seafood samples-right choice of standard makes a difference" in XXII EuroFoodChem conference, 14th-16th June, 2023. In: Book of Abstracts (2023):132-132,
https://hdl.handle.net/21.15107/rcub_cherry_6024 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6032
AB  - Phycobiliproteins (PBP) have been employed in numerous fluorescence-based techniques owing to highly fluorescent, covalently bound tetrapyrrole chromophores. So far, only entire PBPs have been utilized as fluorescent probes. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), to potentially any protein, is proposed, relying on the ability of PCB to be attached to sulfhydryl groups of proteins. Traut’s reagent (TR, 2-iminothiolane) was exploited for introduction of sulfhydryl groups in the model protein, bovine serum albumin (BSA), by modifying its primary amines. Introduced sulfhydryl groups were then targeted for modification by PCB. All tested molar ratios of TR per mole of protein were successful in modification of BSA. Near-UV and far-UV circular dichroism spectroscopy revealed that a higher degree of modification by TR induces more profound alterations of BSA structure, leading at the same time to minor changes in BSA oligomerization and aggregation profile. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio of TR. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal ratio for balancing between the effect on protein structure and the degree of labeling and thus fluorescent signal obtained. The proposed method could be used for labeling of virtually any protein, as means of either obtaining fluorescent probes for application in fluorescent techniques or functionalization of, for example, food proteins through covalent attachment of bioactive PCB.
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  - Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin
SP  - 37
EP  - 37
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6032
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Phycobiliproteins (PBP) have been employed in numerous fluorescence-based techniques owing to highly fluorescent, covalently bound tetrapyrrole chromophores. So far, only entire PBPs have been utilized as fluorescent probes. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), to potentially any protein, is proposed, relying on the ability of PCB to be attached to sulfhydryl groups of proteins. Traut’s reagent (TR, 2-iminothiolane) was exploited for introduction of sulfhydryl groups in the model protein, bovine serum albumin (BSA), by modifying its primary amines. Introduced sulfhydryl groups were then targeted for modification by PCB. All tested molar ratios of TR per mole of protein were successful in modification of BSA. Near-UV and far-UV circular dichroism spectroscopy revealed that a higher degree of modification by TR induces more profound alterations of BSA structure, leading at the same time to minor changes in BSA oligomerization and aggregation profile. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio of TR. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA, most significantly observed starting from 50-fold and higher TR ratios. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal ratio for balancing between the effect on protein structure and the degree of labeling and thus fluorescent signal obtained. The proposed method could be used for labeling of virtually any protein, as means of either obtaining fluorescent probes for application in fluorescent techniques or functionalization of, for example, food proteins through covalent attachment of bioactive PCB.",
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 = "Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin",
pages = "37-37",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6032"
}

Radomirović, M. Ž., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin. 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., 37-37.
https://hdl.handle.net/21.15107/rcub_cherry_6032

Radomirović MŽ, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin. in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts. 2021;:37-37.
https://hdl.handle.net/21.15107/rcub_cherry_6032 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Traut’s reagent application in fluorescent labeling of bovine serum albumin with phycocyanobilin" in FoodEnTwin Symposium “Novel analytical approaches in food and environmental sciences”, Belgrade, Serbia, 16th-18th June, 2021. In: Book of Abstracts (2021):37-37,
https://hdl.handle.net/21.15107/rcub_cherry_6032 .

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  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6039
AB  - Phycobiliproteins (PBP) are extensively used as fluorescent probes due to highly fluorescent, covalently bound, tetrapyrrole chromophores. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), is proposed. We exploited Traut’s reagent (TR) to introduce sulfhydryl groups in the bovine serum albumin (BSA), by modifying its lysine residues. TR successfully modified BSA under all tested molar ratios of reagent per mole of BSA. The higher degree of modification by TR induces more profound alterations of BSA structure. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice for balancing between a satisfactory level of signal amplification and the adverse effect on protein structure. The method could be used for labeling virtually any protein.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings
T1  - Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent
SP  - 71
EP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6039
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Phycobiliproteins (PBP) are extensively used as fluorescent probes due to highly fluorescent, covalently bound, tetrapyrrole chromophores. A new method for covalent attachment of phycocyanin’s chromophore, phycocyanobilin (PCB), is proposed. We exploited Traut’s reagent (TR) to introduce sulfhydryl groups in the bovine serum albumin (BSA), by modifying its lysine residues. TR successfully modified BSA under all tested molar ratios of reagent per mole of BSA. The higher degree of modification by TR induces more profound alterations of BSA structure. PCB was covalently attached to introduced sulfhydryl groups at pH 9 at 20–fold ratio. An increase in the molar ratio of TR per mole of BSA leads to amplification of fluorescent signal of PCB-modified BSA. Using BSA as a model protein, a 50-fold molar excess of TR seems to be the optimal choice for balancing between a satisfactory level of signal amplification and the adverse effect on protein structure. The method could be used for labeling virtually any protein.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings",
title = "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6039"
}

Radomirović, M. Ž., Gligorijević, N., Minić, S., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent. in 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings
Beograd : Srpsko hemijsko društvo., 71-71.
https://hdl.handle.net/21.15107/rcub_cherry_6039

Radomirović MŽ, Gligorijević N, Minić S, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent. in 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_cherry_6039 .

Radomirović, Mirjana Ž., Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Fluorescent labeling of bovine serum albumin with phycocyanobilin using Traut’s reagent" in 57th Meeting of the Serbian Chemical Society, Kragujevac, Serbia, 18th-19th June, 2021. In: Book of Abstracts and Proceedings (2021):71-71,
https://hdl.handle.net/21.15107/rcub_cherry_6039 .