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

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

Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091

Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .

Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .

TY  - DATA
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4334
PB  - Elsevier
T2  - LWT
T1  - Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4334
ER  - 

@misc{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "LWT",
title = "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4334"
}

Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4334

Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4334 .

Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091." in LWT (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4334 .

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

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

Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091

Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .

Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4844
AB  - Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.
PB  - Elsevier
T2  - Food Chemistry
T1  - Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds
VL  - 334
SP  - 127562
DO  - 10.1016/j.foodchem.2020.127562
ER  - 

@article{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds",
volume = "334",
pages = "127562",
doi = "10.1016/j.foodchem.2020.127562"
}

Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry
Elsevier., 334, 127562.
https://doi.org/10.1016/j.foodchem.2020.127562

Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry. 2021;334:127562.
doi:10.1016/j.foodchem.2020.127562 .

Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds" in Food Chemistry, 334 (2021):127562,
https://doi.org/10.1016/j.foodchem.2020.127562 . .

TY  - JOUR
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4844
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4864
AB  - Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.
PB  - Elsevier
T2  - Food Chemistry
T1  - Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds
VL  - 334
SP  - 127562
DO  - 10.1016/j.foodchem.2020.127562
ER  - 

@article{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Brown seaweeds are traditionally used as food in Asian countries, and they are a valuable source of bioactive compounds. Herein, a novel high-throughput methodological approach was developed for the tracing of compounds with radical scavenging and antimicrobial activities in Saccharina japonica and Undaria pinnatifida methanol extracts. The seaweed metabolites were separated by a novel high-performance thin-layer chromatography method, the bioactive bands were identified by bioautography assays. The bioactive compounds were characterized with ultra-high-performance liquid chromatography coupled with linear trap quadrupole tandem mass spectrometry. Stearidonic, eicosapentaenoic, and arachidonic acids were identified as major components having radical scavenging and antimicrobial activities. The suggested method provides a fast identification and quantification of bioactive compounds in multicomponent biological samples.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds",
volume = "334",
pages = "127562",
doi = "10.1016/j.foodchem.2020.127562"
}

Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry
Elsevier., 334, 127562.
https://doi.org/10.1016/j.foodchem.2020.127562

Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds. in Food Chemistry. 2021;334:127562.
doi:10.1016/j.foodchem.2020.127562 .

Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Rapid analytical approach for bioprofiling compounds with radical scavenging and antimicrobial activities from seaweeds" in Food Chemistry, 334 (2021):127562,
https://doi.org/10.1016/j.foodchem.2020.127562 . .

TY  - DATA
AU  - Ristivojević, Petar
AU  - Jovanović, Vesna B.
AU  - Milojković-Opsenica, Dušanka
AU  - Park, Jihae
AU  - Rollinger, Judith M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4865
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4865
ER  - 

@misc{
author = "Ristivojević, Petar and Jovanović, Vesna B. and Milojković-Opsenica, Dušanka and Park, Jihae and Rollinger, Judith M. and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4865"
}

Ristivojević, P., Jovanović, V. B., Milojković-Opsenica, D., Park, J., Rollinger, J. M.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4865

Ristivojević P, Jovanović VB, Milojković-Opsenica D, Park J, Rollinger JM, Ćirković-Veličković T. Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562.. in Food Chemistry. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4865 .

Ristivojević, Petar, Jovanović, Vesna B., Milojković-Opsenica, Dušanka, Park, Jihae, Rollinger, Judith M., Ćirković-Veličković, Tanja, "Supplementary data for the article: Ristivojević, P.; Jovanović, V.; Milojković-Opsenica, D.; Park, J.; Rollinger, J. M.; Ćirković-Veličković, T. Rapid Analytical Approach for Bioprofiling Compounds with Radical Scavenging and Antimicrobial Activities from Seaweeds. Food Chemistry 2021, 334, 127562. https://doi.org/10.1016/j.foodchem.2020.127562." in Food Chemistry (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4865 .

TY  - CHAP
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5728
AB  - Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. 
A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.
PB  - New York : Nova Science Publisher
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications
VL  - 4
SP  - 158
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5728
ER  - 

@inbook{
author = "Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. 
A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.",
publisher = "New York : Nova Science Publisher",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications",
volume = "4",
pages = "158",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5728"
}

Smiljanić, K., Mihailović, J., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2020). Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publisher., 4, 158.
https://hdl.handle.net/21.15107/rcub_cherry_5728

Smiljanić K, Mihailović J, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;4:158.
https://hdl.handle.net/21.15107/rcub_cherry_5728 .

Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 4 (2020):158,
https://hdl.handle.net/21.15107/rcub_cherry_5728 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5724
AB  - Background: An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been appreciated; hence, little progress has been made within this field. Our aim was to show that in-depth PTM profiling has a great importance and deserves to be explored with renewed and simple method with advanced algorithm.
Method: We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting.
Results: An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA.
Conclusion: Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed that heavy metals are primarily responsible for oxidative stress effects observed in Timothy grass pollen proteome, rather than gaseous pollutants formed during road traffics such as ozone, nitric dioxide or Sulphur di- and/or trioxide.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress
IS  - L7
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5724
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Background: An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been appreciated; hence, little progress has been made within this field. Our aim was to show that in-depth PTM profiling has a great importance and deserves to be explored with renewed and simple method with advanced algorithm.
Method: We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting.
Results: An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA.
Conclusion: Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed that heavy metals are primarily responsible for oxidative stress effects observed in Timothy grass pollen proteome, rather than gaseous pollutants formed during road traffics such as ozone, nitric dioxide or Sulphur di- and/or trioxide.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress",
number = "L7",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5724"
}

Smiljanić, K., Prodić, I., Apostolović, D., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress. in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA.(L7), 13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5724

Smiljanić K, Prodić I, Apostolović D, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress. in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019. 2019;(L7):13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5724 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019, no. L7 (2019):13-13,
https://hdl.handle.net/21.15107/rcub_cherry_5724 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5721
AB  - Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.
Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.
Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.
Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a
11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products
SP  - 25
EP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5721
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Mihailović, Jelena and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.
Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.
Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.
Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a
11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5721"
}

Prodić, I., Smiljanić, K., Mihailović, J., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2019). Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet., 25-25.
https://hdl.handle.net/21.15107/rcub_cherry_5721

Prodić I, Smiljanić K, Mihailović J, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;:25-25.
https://hdl.handle.net/21.15107/rcub_cherry_5721 .

Prodić, Ivana, Smiljanić, Katarina, Mihailović, Jelena, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019 (2019):25-25,
https://hdl.handle.net/21.15107/rcub_cherry_5721 .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5722
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions ranging from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known about their post-translational modifications (PTM) and how they are affected by thermal treatment. PTM profile may differ between raw and thermally treated peanut, which could affect its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software (Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amounts of any of the studied allergens between raw and roasted extracts. Out of the 4 allergens Ara h 6 is modified in the highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw and roasted sample, respectively. Total of 21 modifications were quantified between the two preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and quantity between treated and non-treated extracts. The in silico discovered PTMs could affect protein digestibility and allergenicity. Further investigation is necessary in order to fully understand the impact protein modifications could have on their allergenic potential.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
IS  - 26
EP  - 26
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5722
ER  - 

@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions ranging from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known about their post-translational modifications (PTM) and how they are affected by thermal treatment. PTM profile may differ between raw and thermally treated peanut, which could affect its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software (Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amounts of any of the studied allergens between raw and roasted extracts. Out of the 4 allergens Ara h 6 is modified in the highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw and roasted sample, respectively. Total of 21 modifications were quantified between the two preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and quantity between treated and non-treated extracts. The in silico discovered PTMs could affect protein digestibility and allergenicity. Further investigation is necessary in order to fully understand the impact protein modifications could have on their allergenic potential.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
number = "26",
pages = "26",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5722"
}

Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet.(26).
https://hdl.handle.net/21.15107/rcub_cherry_5722

Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;(26):null-26.
https://hdl.handle.net/21.15107/rcub_cherry_5722 .

Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Investigation of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019, no. 26 (2019),
https://hdl.handle.net/21.15107/rcub_cherry_5722 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
AU  - Mihailović, Jelena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5723
AB  - Introduction
Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usu-
ally digestion experiments are carried out on purified proteins or protein extracts; however, use of
solid food is far closer to the in vivo situation, taking into account food protein interactions with other
food components, such as polyphenols and lipids.
Objective
The aim of this study was to investigate and compare digestion stability and allergenicity of large
and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under
standardized and physiologically relevant in vitro conditions.
Methodology
In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted
hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE,
2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic
patients’ sera and specific antibodies for Cor a 8.
Main findings
Several important hazelnut seed storage digestion resistant proteins and peptides have been identi-
fied and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance,
acidic and basic chains of Cor a 9, and Cor a 11. Digestion-resistant peptides of Cor a 11 and Cor
a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis.
Conclusion
To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE
response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial
extraction and digestion of Cor a 11 and Cor a 9 into digestion-resistant peptides with preserved
IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut
allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion
and retained their allergenicity.
PB  - INFOGEST Cost action FA1402
C3  - Proceedings of the 6th International Conference on Food Digestion 2019
T1  - Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products
SP  - 191
EP  - 191
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5723
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja and Mihailović, Jelena",
year = "2019",
abstract = "Introduction
Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usu-
ally digestion experiments are carried out on purified proteins or protein extracts; however, use of
solid food is far closer to the in vivo situation, taking into account food protein interactions with other
food components, such as polyphenols and lipids.
Objective
The aim of this study was to investigate and compare digestion stability and allergenicity of large
and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under
standardized and physiologically relevant in vitro conditions.
Methodology
In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted
hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE,
2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic
patients’ sera and specific antibodies for Cor a 8.
Main findings
Several important hazelnut seed storage digestion resistant proteins and peptides have been identi-
fied and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance,
acidic and basic chains of Cor a 9, and Cor a 11. Digestion-resistant peptides of Cor a 11 and Cor
a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis.
Conclusion
To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE
response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial
extraction and digestion of Cor a 11 and Cor a 9 into digestion-resistant peptides with preserved
IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut
allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion
and retained their allergenicity.",
publisher = "INFOGEST Cost action FA1402",
journal = "Proceedings of the 6th International Conference on Food Digestion 2019",
title = "Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products",
pages = "191-191",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5723"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K., Ćirković-Veličković, T.,& Mihailović, J.. (2019). Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products. in Proceedings of the 6th International Conference on Food Digestion 2019
INFOGEST Cost action FA1402., 191-191.
https://hdl.handle.net/21.15107/rcub_cherry_5723

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T, Mihailović J. Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products. in Proceedings of the 6th International Conference on Food Digestion 2019. 2019;:191-191.
https://hdl.handle.net/21.15107/rcub_cherry_5723 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, Mihailović, Jelena, "Digestomics of raw and roasted hazelnut according to harmonized static digestion method suitable for solid food and characterization of gastric-phase products" in Proceedings of the 6th International Conference on Food Digestion 2019 (2019):191-191,
https://hdl.handle.net/21.15107/rcub_cherry_5723 .

TY  - CONF
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5725
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions ranging
from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known
about their post-translational modifications (PTM) and how they are affected by thermal
treatment. PTM profile may differ between raw and thermally treated peanut, which could affect
its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,
Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up
proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested
in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo
Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and
Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software
(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune
Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amountsof any of the
studied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in the
highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw
and roasted sample, respectively. Total of 21 modifications were quantified between the two
preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest
number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and
quantity between treated and non-treated extracts. The in silico discovered PTMs could affect
protein digestibility and allergenicity. Further investigation is necessary in order to fully understand
the impact protein modifications could have on their allergenic potential.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
T1  - Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
SP  - 16/L10
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5725
ER  - 

@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions ranging
from mild to severe. Major peanut allergen IgE epitopes are well characterized but little is known
about their post-translational modifications (PTM) and how they are affected by thermal
treatment. PTM profile may differ between raw and thermally treated peanut, which could affect
its allergic potential depending on type, size and position of modifications.
Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,
Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-up
proteomics methods.
Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digested
in gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (Thermo
Fisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 and
Ara h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software
(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the Immune
Epitope Database (IEDB www.iedb.org).
Main findings. LFQ results show that there is no significant change in the amountsof any of the
studied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in the
highest portion, with respect to the protein size: 15% and 12% of its positions are modified in raw
and roasted sample, respectively. Total of 21 modifications were quantified between the two
preparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largest
number of peptides.
Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern and
quantity between treated and non-treated extracts. The in silico discovered PTMs could affect
protein digestibility and allergenicity. Further investigation is necessary in order to fully understand
the impact protein modifications could have on their allergenic potential.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019",
title = "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
pages = "16/L10",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5725"
}

Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA., 16/L10.
https://hdl.handle.net/21.15107/rcub_cherry_5725

Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019. 2019;:16/L10.
https://hdl.handle.net/21.15107/rcub_cherry_5725 .

Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019 (2019):16/L10,
https://hdl.handle.net/21.15107/rcub_cherry_5725 .