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 .