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

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

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .

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  - Gligorijeviž, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Nedić, Olgica
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4784
AB  - The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention
VL  - 22
IS  - 22
SP  - 12385
DO  - 10.3390/ijms222212385
ER  - 

@article{
author = "Gligorijeviž, Nikola and Radomirović, Mirjana Ž. and Nedić, Olgica and Stojadinović, Marija M. and Khulal, Urmila and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention",
volume = "22",
number = "22",
pages = "12385",
doi = "10.3390/ijms222212385"
}

Gligorijeviž, N., Radomirović, M. Ž., Nedić, O., Stojadinović, M. M., Khulal, U., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences
MDPI., 22(22), 12385.
https://doi.org/10.3390/ijms222212385

Gligorijeviž N, Radomirović MŽ, Nedić O, Stojadinović MM, Khulal U, Stanić-Vučinić D, Ćirković-Veličković T. Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences. 2021;22(22):12385.
doi:10.3390/ijms222212385 .

Gligorijeviž, Nikola, Radomirović, Mirjana Ž., Nedić, Olgica, Stojadinović, Marija M., Khulal, Urmila, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention" in International Journal of Molecular Sciences, 22, no. 22 (2021):12385,
https://doi.org/10.3390/ijms222212385 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://www.mdpi.com/1420-3049/26/10/2834
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4552
AB  - Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.
PB  - MDPI
T2  - Molecules
T1  - Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability
VL  - 26
IS  - 10
SP  - 2834
DO  - 10.3390/molecules26102834
ER  - 

@article{
author = "Gligorijević, Nikola and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Stojadinović, Marija M. and Khulal, Urmila and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.",
publisher = "MDPI",
journal = "Molecules",
title = "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability",
volume = "26",
number = "10",
pages = "2834",
doi = "10.3390/molecules26102834"
}

Gligorijević, N., Stanić-Vučinić, D., Radomirović, M. Ž., Stojadinović, M. M., Khulal, U., Nedić, O.,& Ćirković-Veličković, T.. (2021). Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules
MDPI., 26(10), 2834.
https://doi.org/10.3390/molecules26102834

Gligorijević N, Stanić-Vučinić D, Radomirović MŽ, Stojadinović MM, Khulal U, Nedić O, Ćirković-Veličković T. Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules. 2021;26(10):2834.
doi:10.3390/molecules26102834 .

Gligorijević, Nikola, Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Stojadinović, Marija M., Khulal, Urmila, Nedić, Olgica, Ćirković-Veličković, Tanja, "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability" in Molecules, 26, no. 10 (2021):2834,
https://doi.org/10.3390/molecules26102834 . .

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  - Khulal, Urmila
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3779
AB  - Shellfish, is a highly nutritive food resource in the world, but also among the eight allergic food groups accounting for approximately 90% of all immunoglobulin E food allergies worldwide [1]. This work focuses on the only well-recognized major allergen muscle protein tropomyosin(TM) that is responsible for cross reactivity between shellfish and other invertebrates [2]. By contrary, TM of vertebrates (chicken, pig, cow) is not a prominent allergen. The stability of food allergens to digestion is an important factor contributing to their allergenicity. Most in vitro digestibility studies are based on the protein extract rather than whole food matrix thus overlooking its effect on TM stability [3]. Our objective was to primarily test the pepsin digestibility of invertebrates and vertebrates (raw and thermally treated based on their real life consumption modes) mimicking the gastric digestion under standardized conditions. To closely observe and compare the vertebrates’ and invertebrates’ TM stability, we aimed to perform the specific antibody based western blot analysis with two primary antibodies; ❶Rabbit anti shrimp TM antibody (invertebrates), and ❷ Rabbit anti human TM antibody (species reactivity to vertebrates).
Methods: Thermal treatment of selected samples to compare TM heat stability, Standardized static in vitro methods of simulated gastric digestion[4] for the evaluation and comparison of TM resistance to pepsin, Sodium Dodecyl Sulfate-Polyacryl amide Gel Electrophoresis (SDS-PAGE) of digesta supernatant under reducing and non-reducing conditions to quantify proteins and compare thermally treated invertebrates and vertebrates protein profiles focusing on TM, specific antibody based semi dry Western blot analysis.
Results and discussions: SDS-PAGE analysis of vertebrates and invertebrates’ samples showed a range of proteins in varied amounts between 10-250 kDa. Depending upon samples, varied numbers of prominent protein bands were observed including the distinct bands corresponding with the molecular weights of TM(37-39kDa). In agreement with publications, TM was, indeed, resistant against pepsin digestion as well as thermal treatment prominently in case of invertebrates. This was confirmed upon Ab based Western blot analysis. Our results show that, upon thermal treatment, TM is partially degraded as is observed in case of raw and cooked beef electrophoretic profile as well as WB analysis. Significantly, upon pepsin digestion, TM (allergen) is completely degraded in vertebrates in contrast to the invertebrates’ TM (which is pepsin resistant and heat stable).
This result provides an insight on the differences in digestibility of allergenic versus non-allergenic TM in real food matrix and upon thermal treatments of solid food samples. Methods: Thermal treatment of selected samples to compare TM heat stability, Standardized static in vitro methods of simulated gastric digestion[4] for the evaluation and comparison of TM resistance to pepsin, Sodium Dodecyl Sulfate-Polyacryl amide Gel Electrophoresis (SDS-PAGE) of digesta supernatant under reducing and non-reducing conditions to quantify proteins and compare thermally treated invertebrates and vertebrates protein profiles focusing on TM, specific antibody based semi dry Western blot analysis.
Results and discussions: SDS-PAGE analysis of vertebrates and invertebrates’ samples showed a range of proteins in varied amounts between 10-250 kDa. Depending upon samples, varied numbers of prominent protein bands were observed including the distinct bands corresponding with the molecular weights of TM(37-39kDa). In agreement with publications, TM was, indeed, resistant against pepsin digestion as well as thermal treatment prominently in case of invertebrates. This was confirmed upon Ab based Western blot analysis. Our results show that, upon thermal treatment, TM is partially degraded as is observed in case of raw and cooked beef electrophoretic profile as well as WB analysis. Significantly, upon pepsin digestion, TM (allergen) is completely degraded in vertebrates in contrast to the invertebrates’ TM (which is pepsin resistant and heat stable).
This result provides an insight on the differences in digestibility of allergenic versus non-allergenic TM in real food matrix and upon thermal treatments of solid food samples.
PB  - Portugal : Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XX EuroFoodChem Congress
T1  - Comparative digestomics of Tropomyosin of vertebrates and invertebrates in real food matrix
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3779
ER  - 

@conference{
author = "Khulal, Urmila and Jovanović, Vesna B. and Ćirković-Veličković, Tanja and Mutić, Jelena",
year = "2019",
abstract = "Shellfish, is a highly nutritive food resource in the world, but also among the eight allergic food groups accounting for approximately 90% of all immunoglobulin E food allergies worldwide [1]. This work focuses on the only well-recognized major allergen muscle protein tropomyosin(TM) that is responsible for cross reactivity between shellfish and other invertebrates [2]. By contrary, TM of vertebrates (chicken, pig, cow) is not a prominent allergen. The stability of food allergens to digestion is an important factor contributing to their allergenicity. Most in vitro digestibility studies are based on the protein extract rather than whole food matrix thus overlooking its effect on TM stability [3]. Our objective was to primarily test the pepsin digestibility of invertebrates and vertebrates (raw and thermally treated based on their real life consumption modes) mimicking the gastric digestion under standardized conditions. To closely observe and compare the vertebrates’ and invertebrates’ TM stability, we aimed to perform the specific antibody based western blot analysis with two primary antibodies; ❶Rabbit anti shrimp TM antibody (invertebrates), and ❷ Rabbit anti human TM antibody (species reactivity to vertebrates).
Methods: Thermal treatment of selected samples to compare TM heat stability, Standardized static in vitro methods of simulated gastric digestion[4] for the evaluation and comparison of TM resistance to pepsin, Sodium Dodecyl Sulfate-Polyacryl amide Gel Electrophoresis (SDS-PAGE) of digesta supernatant under reducing and non-reducing conditions to quantify proteins and compare thermally treated invertebrates and vertebrates protein profiles focusing on TM, specific antibody based semi dry Western blot analysis.
Results and discussions: SDS-PAGE analysis of vertebrates and invertebrates’ samples showed a range of proteins in varied amounts between 10-250 kDa. Depending upon samples, varied numbers of prominent protein bands were observed including the distinct bands corresponding with the molecular weights of TM(37-39kDa). In agreement with publications, TM was, indeed, resistant against pepsin digestion as well as thermal treatment prominently in case of invertebrates. This was confirmed upon Ab based Western blot analysis. Our results show that, upon thermal treatment, TM is partially degraded as is observed in case of raw and cooked beef electrophoretic profile as well as WB analysis. Significantly, upon pepsin digestion, TM (allergen) is completely degraded in vertebrates in contrast to the invertebrates’ TM (which is pepsin resistant and heat stable).
This result provides an insight on the differences in digestibility of allergenic versus non-allergenic TM in real food matrix and upon thermal treatments of solid food samples. Methods: Thermal treatment of selected samples to compare TM heat stability, Standardized static in vitro methods of simulated gastric digestion[4] for the evaluation and comparison of TM resistance to pepsin, Sodium Dodecyl Sulfate-Polyacryl amide Gel Electrophoresis (SDS-PAGE) of digesta supernatant under reducing and non-reducing conditions to quantify proteins and compare thermally treated invertebrates and vertebrates protein profiles focusing on TM, specific antibody based semi dry Western blot analysis.
Results and discussions: SDS-PAGE analysis of vertebrates and invertebrates’ samples showed a range of proteins in varied amounts between 10-250 kDa. Depending upon samples, varied numbers of prominent protein bands were observed including the distinct bands corresponding with the molecular weights of TM(37-39kDa). In agreement with publications, TM was, indeed, resistant against pepsin digestion as well as thermal treatment prominently in case of invertebrates. This was confirmed upon Ab based Western blot analysis. Our results show that, upon thermal treatment, TM is partially degraded as is observed in case of raw and cooked beef electrophoretic profile as well as WB analysis. Significantly, upon pepsin digestion, TM (allergen) is completely degraded in vertebrates in contrast to the invertebrates’ TM (which is pepsin resistant and heat stable).
This result provides an insight on the differences in digestibility of allergenic versus non-allergenic TM in real food matrix and upon thermal treatments of solid food samples.",
publisher = "Portugal : Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XX EuroFoodChem Congress",
title = "Comparative digestomics of Tropomyosin of vertebrates and invertebrates in real food matrix",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3779"
}

Khulal, U., Jovanović, V. B., Ćirković-Veličković, T.,& Mutić, J.. (2019). Comparative digestomics of Tropomyosin of vertebrates and invertebrates in real food matrix. in Book of Abstracts of the XX EuroFoodChem Congress
Portugal : Sociedade Portuguesa de Química..
https://hdl.handle.net/21.15107/rcub_cherry_3779

Khulal U, Jovanović VB, Ćirković-Veličković T, Mutić J. Comparative digestomics of Tropomyosin of vertebrates and invertebrates in real food matrix. in Book of Abstracts of the XX EuroFoodChem Congress. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3779 .

Khulal, Urmila, Jovanović, Vesna B., Ćirković-Veličković, Tanja, Mutić, Jelena, "Comparative digestomics of Tropomyosin of vertebrates and invertebrates in real food matrix" in Book of Abstracts of the XX EuroFoodChem Congress (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3779 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Khulal, Urmila
AU  - Mutić, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5710
AB  - Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highly
nutritive food resource in the world, but also among the eight allergic food groups accounting for
approximately 90% of all immunoglobulin E food allergies worldwide. The general objective of our
research is to comprehensively investigate stability and structures of pepsin-resistant allergens, of
their larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsin
digestion of whole raw and extract of shellfish, under standardized and physiologically relevant
gastric conditions.
Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),
were pepsin digested according to standardized static digestion protocol. Controls were treated in a
same manner without adding pepsin. Supernatant of samples and its counterpart controls were
precipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-
PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed by
ncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQ
algorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,
Canada.
Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed a
range of proteins in varied concentrations between 10-250 kDa. In extracted and whole raw
shellfish, approximately 22 prominent protein bands were observed including the distinct bands
corresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-
39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,
specifically around the low molecular weight protein bands. The smearing could possibly be due to
the breakdown products and the glycation. There were slight differences between the protein
profiles under reducing and non-reducing conditions as well. Nevertheless, there was the retention
of a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stable
tropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di
1), with 90% of sequence homology with main tropomyosin allergens from seafood.
Scientific impact and relevance: The results will highlight effects of food matrix on shellfish
allergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will be
obtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in the
real food matrix.
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Digestomics of Japanese abalone in real food matrix
SP  - 10
EP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5710
ER  - 

@conference{
author = "Prodić, Ivana and Khulal, Urmila and Mutić, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highly
nutritive food resource in the world, but also among the eight allergic food groups accounting for
approximately 90% of all immunoglobulin E food allergies worldwide. The general objective of our
research is to comprehensively investigate stability and structures of pepsin-resistant allergens, of
their larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsin
digestion of whole raw and extract of shellfish, under standardized and physiologically relevant
gastric conditions.
Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),
were pepsin digested according to standardized static digestion protocol. Controls were treated in a
same manner without adding pepsin. Supernatant of samples and its counterpart controls were
precipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-
PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed by
ncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQ
algorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,
Canada.
Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed a
range of proteins in varied concentrations between 10-250 kDa. In extracted and whole raw
shellfish, approximately 22 prominent protein bands were observed including the distinct bands
corresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-
39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,
specifically around the low molecular weight protein bands. The smearing could possibly be due to
the breakdown products and the glycation. There were slight differences between the protein
profiles under reducing and non-reducing conditions as well. Nevertheless, there was the retention
of a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stable
tropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di
1), with 90% of sequence homology with main tropomyosin allergens from seafood.
Scientific impact and relevance: The results will highlight effects of food matrix on shellfish
allergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will be
obtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in the
real food matrix.",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Digestomics of Japanese abalone in real food matrix",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5710"
}

Prodić, I., Khulal, U., Mutić, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 10-10.
https://hdl.handle.net/21.15107/rcub_cherry_5710

Prodić I, Khulal U, Mutić J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:10-10.
https://hdl.handle.net/21.15107/rcub_cherry_5710 .

Prodić, Ivana, Khulal, Urmila, Mutić, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Digestomics of Japanese abalone in real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):10-10,
https://hdl.handle.net/21.15107/rcub_cherry_5710 .