TY  - JOUR
AU  - de Guzman, Maria Krishna
AU  - Anđelković, Mirjana
AU  - Jovanović, Vesna B.
AU  - Jung, Jaehak
AU  - Kim, Juyang
AU  - Dailey, Lea Ann
AU  - Rajković, Andreja
AU  - De Meulenaer, Bruno
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://hdl.handle.net/1854/LU-8759702
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5420
AB  - The accumulation of microplastics in marine organisms is an emerging concern. Due to trophic transfer, the
safety of seafood is under investigation in view of the potential negative effects of microplastics on human health.
In this study, market samples of Manila clams (Ruditapes philippinarum) from South Korea were segregated into
two groups of considerably different size (p < 0.05), namely small clams with shell length of 40.69 ± 3.97 mm,
and large clams of shell length 51.19 ± 2.86 mm. Comparative profiling of the number, size, shape, and polymer
type of microplastics were performed using μFTIR imaging and Nile red staining. Overall, μFTIR detected only
1559 microplastics while 1996 microplastics were counted based on staining from 61 Manila clams (30 small and
31 large), leading to an overestimation of 18 to 75 %. Comparable microplastics concentration, based on μFTIR,
were observed at 2.70 ± 1.66 MP/g or 15.64 ± 9.25 MP/individual for the small samples, and 3.65 ± 1.59 MP/g
or 41.63 ± 16.90 MP/individual for the large ones (p > 0.05). Particle diameters of 20–100 μm was the most
dominant, accounting for 44.6 % and 46.5 % of all microplastics from the small and large groups, respectively.
Particles, with a circularity (resemblance to a circle) value between 0.6 and 1.0, were the most prevalent, fol-
lowed by fragments and fibers. At least 50 % of microplastics from the small and large samples were polystyrene,
making it the most abundant polymer type. Despite the substantial difference in the size of the animals, only a
weak to moderate correlation was observed between microplastics content and the physical attributes of the
clams such as shell length and weight, (soft) tissue weight, and total weight (Spearman's coefficient < 0.5). The
estimated intake of microplastics by the Korean population was 1232 MP/person/year via small clams, 1663 MP/
person/year via large clams, and 1489 MP/person/year via clams independent of size.
PB  - Elsevier
T2  - Marine Pollution Bulletin
T1  - Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining
VL  - 181
SP  - 113846
DO  - 10.1016/j.marpolbul.2022.113846
ER  - 

@article{
author = "de Guzman, Maria Krishna and Anđelković, Mirjana and Jovanović, Vesna B. and Jung, Jaehak and Kim, Juyang and Dailey, Lea Ann and Rajković, Andreja and De Meulenaer, Bruno and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The accumulation of microplastics in marine organisms is an emerging concern. Due to trophic transfer, the
safety of seafood is under investigation in view of the potential negative effects of microplastics on human health.
In this study, market samples of Manila clams (Ruditapes philippinarum) from South Korea were segregated into
two groups of considerably different size (p < 0.05), namely small clams with shell length of 40.69 ± 3.97 mm,
and large clams of shell length 51.19 ± 2.86 mm. Comparative profiling of the number, size, shape, and polymer
type of microplastics were performed using μFTIR imaging and Nile red staining. Overall, μFTIR detected only
1559 microplastics while 1996 microplastics were counted based on staining from 61 Manila clams (30 small and
31 large), leading to an overestimation of 18 to 75 %. Comparable microplastics concentration, based on μFTIR,
were observed at 2.70 ± 1.66 MP/g or 15.64 ± 9.25 MP/individual for the small samples, and 3.65 ± 1.59 MP/g
or 41.63 ± 16.90 MP/individual for the large ones (p > 0.05). Particle diameters of 20–100 μm was the most
dominant, accounting for 44.6 % and 46.5 % of all microplastics from the small and large groups, respectively.
Particles, with a circularity (resemblance to a circle) value between 0.6 and 1.0, were the most prevalent, fol-
lowed by fragments and fibers. At least 50 % of microplastics from the small and large samples were polystyrene,
making it the most abundant polymer type. Despite the substantial difference in the size of the animals, only a
weak to moderate correlation was observed between microplastics content and the physical attributes of the
clams such as shell length and weight, (soft) tissue weight, and total weight (Spearman's coefficient < 0.5). The
estimated intake of microplastics by the Korean population was 1232 MP/person/year via small clams, 1663 MP/
person/year via large clams, and 1489 MP/person/year via clams independent of size.",
publisher = "Elsevier",
journal = "Marine Pollution Bulletin",
title = "Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining",
volume = "181",
pages = "113846",
doi = "10.1016/j.marpolbul.2022.113846"
}

de Guzman, M. K., Anđelković, M., Jovanović, V. B., Jung, J., Kim, J., Dailey, L. A., Rajković, A., De Meulenaer, B.,& Ćirković-Veličković, T.. (2022). Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining. in Marine Pollution Bulletin
Elsevier., 181, 113846.
https://doi.org/10.1016/j.marpolbul.2022.113846

de Guzman MK, Anđelković M, Jovanović VB, Jung J, Kim J, Dailey LA, Rajković A, De Meulenaer B, Ćirković-Veličković T. Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining. in Marine Pollution Bulletin. 2022;181:113846.
doi:10.1016/j.marpolbul.2022.113846 .

de Guzman, Maria Krishna, Anđelković, Mirjana, Jovanović, Vesna B., Jung, Jaehak, Kim, Juyang, Dailey, Lea Ann, Rajković, Andreja, De Meulenaer, Bruno, Ćirković-Veličković, Tanja, "Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining" in Marine Pollution Bulletin, 181 (2022):113846,
https://doi.org/10.1016/j.marpolbul.2022.113846 . .

TY  - 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  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5730
AB  - Cor a 9 is one of the most common hazelnut allergen, a non-glycosylated protein, consisting of two subunits, an acidic (ranging between 35-40 kDa) and a basic subunit (ranging between 20-25 kDa). Very important fact is that the acid chain carries the immunoreactivity, according to literature. The survival of large fragments of Cor a 9 is necessary for its ability to sensitize individual. The aim of this study was to investigate Cor a 9, and to compare the digestive stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut grains in standardized and physiologically relevant in vitro conditions, after heat treatment (roasting as the most abundant type of heat treatment). In vitro simulated phases of oral and gastric digestion were performed with ground raw and roasted hazelnut kernels according to the 1.0 INFOGEST protocol. After digestion proteins were extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE test was examined in the sera of allergic patients using ELISA and 2D immunoblot. The focus of the research was on the analysis of the 2DE map by Image 2D Master Platinum 7.0 software, comparing region of acid and basic Cor a 9 from raw and roasted hazelnut. Cor a 9 peptides are resistant to gastric digestion, and are able to bind IgE patients. Roasted hazelnuts are more prone to digestion in the stomach than the raw sample and cause a milder IgE response in patients. The gastric digestion phase of raw and roasted hazelnut grains resulted in partial extraction and digestion of Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results show significant resistance of Cor a 9 raw and roasted hazelnuts to digestion in the stomach, as they remained mostly intact after 2 hours of gastric (pepsin) phase and retained their allergenicity.
PB  - Belgrade : University of Belgrade
C3  - Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021
T1  - Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion
SP  - 142
EP  - 142
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5730
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 9 is one of the most common hazelnut allergen, a non-glycosylated protein, consisting of two subunits, an acidic (ranging between 35-40 kDa) and a basic subunit (ranging between 20-25 kDa). Very important fact is that the acid chain carries the immunoreactivity, according to literature. The survival of large fragments of Cor a 9 is necessary for its ability to sensitize individual. The aim of this study was to investigate Cor a 9, and to compare the digestive stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut grains in standardized and physiologically relevant in vitro conditions, after heat treatment (roasting as the most abundant type of heat treatment). In vitro simulated phases of oral and gastric digestion were performed with ground raw and roasted hazelnut kernels according to the 1.0 INFOGEST protocol. After digestion proteins were extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE test was examined in the sera of allergic patients using ELISA and 2D immunoblot. The focus of the research was on the analysis of the 2DE map by Image 2D Master Platinum 7.0 software, comparing region of acid and basic Cor a 9 from raw and roasted hazelnut. Cor a 9 peptides are resistant to gastric digestion, and are able to bind IgE patients. Roasted hazelnuts are more prone to digestion in the stomach than the raw sample and cause a milder IgE response in patients. The gastric digestion phase of raw and roasted hazelnut grains resulted in partial extraction and digestion of Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results show significant resistance of Cor a 9 raw and roasted hazelnuts to digestion in the stomach, as they remained mostly intact after 2 hours of gastric (pepsin) phase and retained their allergenicity.",
publisher = "Belgrade : University of Belgrade",
journal = "Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021",
title = "Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion",
pages = "142-142",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5730"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion. in Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021
Belgrade : University of Belgrade., 142-142.
https://hdl.handle.net/21.15107/rcub_cherry_5730

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion. in Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021. 2021;:142-142.
https://hdl.handle.net/21.15107/rcub_cherry_5730 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Influence of immune activity of Cor a 9 from raw and roasted hazelnuts after gastric digestion" in Book of Abstracts: Unifood conference, Belgrade, September 24-25, 2021 (2021):142-142,
https://hdl.handle.net/21.15107/rcub_cherry_5730 .

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  - JOUR
AU  - Krstić-Ristivojević, Maja
AU  - Grundström, Jeanette
AU  - Apostolović, Danijela
AU  - Radomirović, Mirjana Ž.
AU  - Jovanović, Vesna B.
AU  - Radoi, Vlad
AU  - Kiewiet, M. B. Gea
AU  - Vukojević, Vladana
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4866
AB  - Transepithelial transport of proteins is an important step in the immune response to food allergens. Mammalian meat allergy is characterized by an IgE response against the carbohydrate moiety galactosyl-α-1,3-galactose (α-Gal) present on mammalian glycoproteins and glycolipids, which causes severe allergic reactions several hours after red meat consumption. The delayed reaction may be related to the processing of α-Gal carrying proteins in the gastrointestinal tract. The aim of this study was to investigate how protein glycosylation by α-Gal affects the susceptibility to gastric digestion and transport through the Caco-2 cell monolayer. We found that α-Gal glycosylation altered protein susceptibility to gastric digestion, where large protein fragments bearing the α-Gal epitope remained for up to 2 h of digestion. Furthermore, α-Gal glycosylation of the protein hampered transcytosis of the protein through the Caco-2 monolayer. α-Gal epitope on the intact protein could be detected in the endosomal fraction obtained by differential centrifugation of Caco-2 cell lysates. Furthermore, the level of galectin-3 in Caco-2 cells was not affected by the presence of α-Gal glycosylated BSA (bovine serum albumin) (BSA-α-Gal). Taken together, our data add new knowledge and shed light on the digestion and transport of α-Gal glycosylated proteins.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer
VL  - 21
IS  - 16
SP  - 5742
DO  - 10.3390/ijms21165742
ER  - 

@article{
author = "Krstić-Ristivojević, Maja and Grundström, Jeanette and Apostolović, Danijela and Radomirović, Mirjana Ž. and Jovanović, Vesna B. and Radoi, Vlad and Kiewiet, M. B. Gea and Vukojević, Vladana and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2020",
abstract = "Transepithelial transport of proteins is an important step in the immune response to food allergens. Mammalian meat allergy is characterized by an IgE response against the carbohydrate moiety galactosyl-α-1,3-galactose (α-Gal) present on mammalian glycoproteins and glycolipids, which causes severe allergic reactions several hours after red meat consumption. The delayed reaction may be related to the processing of α-Gal carrying proteins in the gastrointestinal tract. The aim of this study was to investigate how protein glycosylation by α-Gal affects the susceptibility to gastric digestion and transport through the Caco-2 cell monolayer. We found that α-Gal glycosylation altered protein susceptibility to gastric digestion, where large protein fragments bearing the α-Gal epitope remained for up to 2 h of digestion. Furthermore, α-Gal glycosylation of the protein hampered transcytosis of the protein through the Caco-2 monolayer. α-Gal epitope on the intact protein could be detected in the endosomal fraction obtained by differential centrifugation of Caco-2 cell lysates. Furthermore, the level of galectin-3 in Caco-2 cells was not affected by the presence of α-Gal glycosylated BSA (bovine serum albumin) (BSA-α-Gal). Taken together, our data add new knowledge and shed light on the digestion and transport of α-Gal glycosylated proteins.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer",
volume = "21",
number = "16",
pages = "5742",
doi = "10.3390/ijms21165742"
}

Krstić-Ristivojević, M., Grundström, J., Apostolović, D., Radomirović, M. Ž., Jovanović, V. B., Radoi, V., Kiewiet, M. B. G., Vukojević, V., Ćirković-Veličković, T.,& van Hage, M.. (2020). Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer. in International Journal of Molecular Sciences
MDPI., 21(16), 5742.
https://doi.org/10.3390/ijms21165742

Krstić-Ristivojević M, Grundström J, Apostolović D, Radomirović MŽ, Jovanović VB, Radoi V, Kiewiet MBG, Vukojević V, Ćirković-Veličković T, van Hage M. Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer. in International Journal of Molecular Sciences. 2020;21(16):5742.
doi:10.3390/ijms21165742 .

Krstić-Ristivojević, Maja, Grundström, Jeanette, Apostolović, Danijela, Radomirović, Mirjana Ž., Jovanović, Vesna B., Radoi, Vlad, Kiewiet, M. B. Gea, Vukojević, Vladana, Ćirković-Veličković, Tanja, van Hage, Marianne, "Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer" in International Journal of Molecular Sciences, 21, no. 16 (2020):5742,
https://doi.org/10.3390/ijms21165742 . .

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  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3742
AB  - 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
determined; hence, little progress has been made within this field.
PB  - Belgrade : Faculty of Chemistry
C3  - 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
T1  - Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments
SP  - 6
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3742
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "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
determined; hence, little progress has been made within this field.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia",
title = "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments",
pages = "6-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3742"
}

Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
Belgrade : Faculty of Chemistry., 6-7.
https://hdl.handle.net/21.15107/rcub_cherry_3742

Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia. 2019;:6-7.
https://hdl.handle.net/21.15107/rcub_cherry_3742 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments" in 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia (2019):6-7,
https://hdl.handle.net/21.15107/rcub_cherry_3742 .