Peruško, Marija

Link to this page

Authority KeyName Variants
orcid::0000-0002-2079-750X
  • Peruško, Marija (24)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics
Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718.
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200288 (Innovation Center of the Faculty of Chemistry) Serbian Academy of Sciences and Arts Project F-26.
COST Action [FA 1005] COST Action [FA1402]
Serbian Academy of Sciences and Arts; Grant/Award Number: GA No. F-26 Austrian Federal Ministry of Economy
Austrian Research Promotion Agency (FFG Project) [822768] EU H2020 project FoodEnTwin grant GA810752
Eva and Oscar Ahrén’s Foundation Karolinska Institutet Research Foundation
Laura Bassi Centers of Expertise program ore Nilsons Foundation for Medical Research
Region Stockholm (ALF‐project). Swedish Asthma and Allergy Association’s Research Foundation
Swedish Heart-Lung Foundation (MVH); The Hesselman Foundation Swedish Research Council grants 2019-01060 (MVH)
The Hesselman Foundation. The King Gustaf V 80th Birthday Foundation.
The Konsul Th C Bergh Foundation (DA) The Magnus Bergvall Foundation
The Swedish Asthma and Allergy Association's Research Foundation (Astmaoch Allergiförbundet). The Swedish Cancer and Allergy Foundation
The Swedish Cancer and Allergy Foundation (Insamlingsstiftelsen Canceroch Allergifonden). The Swedish Heart‐Lung Foundation (Hjärt‐Lungfonden).
The Swedish Medical Society The Swedish Research Council (grant number 2014‐03274, 2019‐01060).

Author's Bibliography

Th2-skewed T cells correlate with B cell response to α-Gal and tick antigens in α-Gal syndrome

Apostolović, Danijela; Grundström, Jeanette; Kiewiet, Mensiena B. Gea; Peruško, Marija; Hamsten, Carl; Starkhammar, Maria; Paulie, Staffan; Hage, Marianne van

(American Society for Clinical Investigation, 2023)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Grundström, Jeanette
AU  - Kiewiet, Mensiena B. Gea
AU  - Peruško, Marija
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Paulie, Staffan
AU  - Hage, Marianne van
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6244
AB  - Tick bites have been shown to transmit a novel form of severe food allergy, the galactose-α-1,3-galactose (α-Gal) syndrome (AGS). Cellular responses to α-Gal in patients with AGS have, to date, not been thoroughly scrutinized. Therefore, we investigated T and B cell proliferation, activation, and cytokine profiles in response to tick protein extract (TE) and α-Gal-free TE in patients with AGS and in healthy controls. T and B cells from both patients and controls proliferated in response to TE, but significantly more in patients with AGS. B cell proliferation, but not T cell proliferation, in patients with AGS was reduced by removing α-Gal from the TE. In addition, TE induced a clear Th2 cytokine profile in patients with AGS. Expression of CD23 by B cells correlated only to T cell proliferation. However, both B cell proliferation and CD23 expression were reduced when CD40L and IL-4 were blocked. A large portion of the IgG1 and IgE antibodies binding TE in patients with AGS were directed against the α-Gal epitope. We have, for what we believe to be the first time, investigated T and B cell responses to α-Gal carrying tick proteins in patients with AGS, which will be essential for the understanding of the immune response against an allergenic carbohydrate transmitted by ticks.
PB  - American Society for Clinical Investigation
T2  - The Journal of Clinical Investigation
T1  - Th2-skewed T cells correlate with B cell response to α-Gal and tick antigens in α-Gal syndrome
VL  - 133
IS  - 6
DO  - 10.1172/JCI158357
ER  - 
@article{
author = "Apostolović, Danijela and Grundström, Jeanette and Kiewiet, Mensiena B. Gea and Peruško, Marija and Hamsten, Carl and Starkhammar, Maria and Paulie, Staffan and Hage, Marianne van",
year = "2023",
abstract = "Tick bites have been shown to transmit a novel form of severe food allergy, the galactose-α-1,3-galactose (α-Gal) syndrome (AGS). Cellular responses to α-Gal in patients with AGS have, to date, not been thoroughly scrutinized. Therefore, we investigated T and B cell proliferation, activation, and cytokine profiles in response to tick protein extract (TE) and α-Gal-free TE in patients with AGS and in healthy controls. T and B cells from both patients and controls proliferated in response to TE, but significantly more in patients with AGS. B cell proliferation, but not T cell proliferation, in patients with AGS was reduced by removing α-Gal from the TE. In addition, TE induced a clear Th2 cytokine profile in patients with AGS. Expression of CD23 by B cells correlated only to T cell proliferation. However, both B cell proliferation and CD23 expression were reduced when CD40L and IL-4 were blocked. A large portion of the IgG1 and IgE antibodies binding TE in patients with AGS were directed against the α-Gal epitope. We have, for what we believe to be the first time, investigated T and B cell responses to α-Gal carrying tick proteins in patients with AGS, which will be essential for the understanding of the immune response against an allergenic carbohydrate transmitted by ticks.",
publisher = "American Society for Clinical Investigation",
journal = "The Journal of Clinical Investigation",
title = "Th2-skewed T cells correlate with B cell response to α-Gal and tick antigens in α-Gal syndrome",
volume = "133",
number = "6",
doi = "10.1172/JCI158357"
}
Apostolović, D., Grundström, J., Kiewiet, M. B. G., Peruško, M., Hamsten, C., Starkhammar, M., Paulie, S.,& Hage, M. v.. (2023). Th2-skewed T cells correlate with B cell response to α-Gal and tick antigens in α-Gal syndrome. in The Journal of Clinical Investigation
American Society for Clinical Investigation., 133(6).
https://doi.org/10.1172/JCI158357
Apostolović D, Grundström J, Kiewiet MBG, Peruško M, Hamsten C, Starkhammar M, Paulie S, Hage MV. Th2-skewed T cells correlate with B cell response to α-Gal and tick antigens in α-Gal syndrome. in The Journal of Clinical Investigation. 2023;133(6).
doi:10.1172/JCI158357 .
Apostolović, Danijela, Grundström, Jeanette, Kiewiet, Mensiena B. Gea, Peruško, Marija, Hamsten, Carl, Starkhammar, Maria, Paulie, Staffan, Hage, Marianne van, "Th2-skewed T cells correlate with B cell response to α-Gal and tick antigens in α-Gal syndrome" in The Journal of Clinical Investigation, 133, no. 6 (2023),
https://doi.org/10.1172/JCI158357 . .
11
2
2

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

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

(Elsevier, 2021)

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 . .
1
16
2
17
13

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.

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

(Elsevier, 2021)

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 .

Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.

Peruško, Marija; Apostolović, Danijela; Kiewiet, Mensiena Berentje Geertje; Grundström, Jeanette; Hamsten, Carl; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hage, Marianne van

(Blackwell Publishing Ltd, 2021)

TY  - DATA
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4447
PB  - Blackwell Publishing Ltd
T2  - Allergy
T2  - Allergy
T1  - Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4447
ER  - 
@misc{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
year = "2021",
publisher = "Blackwell Publishing Ltd",
journal = "Allergy, Allergy",
title = "Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4447"
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.. (2021). Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.. in Allergy
Blackwell Publishing Ltd..
https://hdl.handle.net/21.15107/rcub_cherry_4447
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.. in Allergy. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4447 .
Peruško, Marija, Apostolović, Danijela, Kiewiet, Mensiena Berentje Geertje, Grundström, Jeanette, Hamsten, Carl, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hage, Marianne van, "Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889." in Allergy (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4447 .

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

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

(Elsevier, 2021)

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 . .
1
16
2
17
13

Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome

Peruško, Marija; Apostolović, Danijela; Kiewiet, Mensiena Berentje Geertje; Grundström, Jeanette; Hamsten, Carl; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hage, Marianne van

(Wiley, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
PY  - 2021
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4446
AB  - Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.
PB  - Wiley
T2  - Allergy
T2  - Allergy
T1  - Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome
VL  - 76
IS  - 12
SP  - 3766
EP  - 3775
DO  - 10.1111/all.14889
ER  - 
@article{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
year = "2021",
abstract = "Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.",
publisher = "Wiley",
journal = "Allergy, Allergy",
title = "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome",
volume = "76",
number = "12",
pages = "3766-3775",
doi = "10.1111/all.14889"
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.. (2021). Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. in Allergy
Wiley., 76(12), 3766-3775.
https://doi.org/10.1111/all.14889
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. in Allergy. 2021;76(12):3766-3775.
doi:10.1111/all.14889 .
Peruško, Marija, Apostolović, Danijela, Kiewiet, Mensiena Berentje Geertje, Grundström, Jeanette, Hamsten, Carl, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hage, Marianne van, "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome" in Allergy, 76, no. 12 (2021):3766-3775,
https://doi.org/10.1111/all.14889 . .
24
13
13
7

Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients

Apostolović, Danijela; Grundström, Jeanette; Peruško, Marija; Kiewiet, M. B. Gea; Hamsten, Carl; Starkhammar, Maria; van Hage, Marianne

(Wiley, 2021)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Grundström, Jeanette
AU  - Peruško, Marija
AU  - Kiewiet, M. B. Gea
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - van Hage, Marianne
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4839
PB  - Wiley
T2  - Clinical and Translational Allergy
T2  - Clinical and Translational AllergyClin Transl Allergy
T1  - Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients
VL  - 11
IS  - 10
SP  - e12087
DO  - 10.1002/clt2.12087
ER  - 
@article{
author = "Apostolović, Danijela and Grundström, Jeanette and Peruško, Marija and Kiewiet, M. B. Gea and Hamsten, Carl and Starkhammar, Maria and van Hage, Marianne",
year = "2021",
publisher = "Wiley",
journal = "Clinical and Translational Allergy, Clinical and Translational AllergyClin Transl Allergy",
title = "Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients",
volume = "11",
number = "10",
pages = "e12087",
doi = "10.1002/clt2.12087"
}
Apostolović, D., Grundström, J., Peruško, M., Kiewiet, M. B. G., Hamsten, C., Starkhammar, M.,& van Hage, M.. (2021). Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients. in Clinical and Translational Allergy
Wiley., 11(10), e12087.
https://doi.org/10.1002/clt2.12087
Apostolović D, Grundström J, Peruško M, Kiewiet MBG, Hamsten C, Starkhammar M, van Hage M. Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients. in Clinical and Translational Allergy. 2021;11(10):e12087.
doi:10.1002/clt2.12087 .
Apostolović, Danijela, Grundström, Jeanette, Peruško, Marija, Kiewiet, M. B. Gea, Hamsten, Carl, Starkhammar, Maria, van Hage, Marianne, "Course of IgE to α-Gal in a Swedish population of α-Gal syndrome patients" in Clinical and Translational Allergy, 11, no. 10 (2021):e12087,
https://doi.org/10.1002/clt2.12087 . .
7
4

Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins

Peruško, Marija; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Smiljanić, Katarina; Stanić-Vučinić, Dragana; Ghnimi, Sami; Ćirković-Veličković, Tanja

(2020)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Smiljanić, Katarina
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5130
AB  - Objective. Camel milk is highly nutritious food with many health benefits proposed. Demand for camel milk has increased worldwide. Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we examined the effect of freeze/spray drying treatment for camel milk powder production, on physiochemical and functional properties of camel milk proteins.
Material and Methods. Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic and spectroscopic techniques. Structural and functional properties of camel milk proteins such as Maillard reaction products formation, antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated attachement of lactose moieties to NH2-group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis showed formation of intermediate Maillard reaction products (increased absorbance at 294 nm) and no detectable late Maillard reaction products formation. Higher inlet temperatures (230°C - 250°C) resulted in higher protein carbonyls formation and lower content of free amino groups as a result of Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Antioxidant activity and protein solubility were increased with increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promotes non-enzymatic glycation of camel milk proteins and exert significant effects on the techno-functional properties of CM powder such as nutritional value and shelf life. Thus, optimization of spray drying parametars is essential for production of high quality camel milk powders.
Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752.
C3  - 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria
T1  - Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins
SP  - 6
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5130
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Smiljanić, Katarina and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Objective. Camel milk is highly nutritious food with many health benefits proposed. Demand for camel milk has increased worldwide. Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we examined the effect of freeze/spray drying treatment for camel milk powder production, on physiochemical and functional properties of camel milk proteins.
Material and Methods. Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic and spectroscopic techniques. Structural and functional properties of camel milk proteins such as Maillard reaction products formation, antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated attachement of lactose moieties to NH2-group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis showed formation of intermediate Maillard reaction products (increased absorbance at 294 nm) and no detectable late Maillard reaction products formation. Higher inlet temperatures (230°C - 250°C) resulted in higher protein carbonyls formation and lower content of free amino groups as a result of Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Antioxidant activity and protein solubility were increased with increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promotes non-enzymatic glycation of camel milk proteins and exert significant effects on the techno-functional properties of CM powder such as nutritional value and shelf life. Thus, optimization of spray drying parametars is essential for production of high quality camel milk powders.
Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752.",
journal = "2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria",
title = "Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins",
pages = "6-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5130"
}
Peruško, M., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Smiljanić, K., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2020). Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins. in 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria, 6-7.
https://hdl.handle.net/21.15107/rcub_cherry_5130
Peruško M, Simović A, Stevanović NR, Radomirović MŽ, Smiljanić K, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins. in 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria. 2020;:6-7.
https://hdl.handle.net/21.15107/rcub_cherry_5130 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Smiljanić, Katarina, Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Higher degree of Maillard reaction induced by spray drying at high temperatures increases antioxidant activity of camel milk proteins" in 2nd FoodEnTwin Workshop Experimental anlimal models for food and environment, February 3-4, 2020, Vienna, Austria (2020):6-7,
https://hdl.handle.net/21.15107/rcub_cherry_5130 .

Novel insights into the allergenic relationship between red meat and bovine milk

Peruško, Marija; Apostolović, Danijela; Starkhammar, Maria; Ćirković-Veličković, Tanja; van Hage, Marianne

(Wiley, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3735
AB  - Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - Novel insights into the allergenic relationship between red meat and bovine milk
VL  - 74
VL  - supp. 106
SP  - 596
EP  - 596
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3735
ER  - 
@conference{
author = "Peruško, Marija and Apostolović, Danijela and Starkhammar, Maria and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2019",
abstract = "Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "Novel insights into the allergenic relationship between red meat and bovine milk",
volume = "74, supp. 106",
pages = "596-596",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3735"
}
Peruško, M., Apostolović, D., Starkhammar, M., Ćirković-Veličković, T.,& van Hage, M.. (2019). Novel insights into the allergenic relationship between red meat and bovine milk. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74, 596-596.
https://hdl.handle.net/21.15107/rcub_cherry_3735
Peruško M, Apostolović D, Starkhammar M, Ćirković-Veličković T, van Hage M. Novel insights into the allergenic relationship between red meat and bovine milk. in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74:596-596.
https://hdl.handle.net/21.15107/rcub_cherry_3735 .
Peruško, Marija, Apostolović, Danijela, Starkhammar, Maria, Ćirković-Veličković, Tanja, van Hage, Marianne, "Novel insights into the allergenic relationship between red meat and bovine milk" in Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74 (2019):596-596,
https://hdl.handle.net/21.15107/rcub_cherry_3735 .

Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures

Peruško, Marija; Simović, Ana; Stevanović, Nikola R.; Smiljanić, Katarina; Radomirović, Mirjana Ž.; Stanić-Vučinić, Dragana; Ghnimi, Sami; Ćirković-Veličković, Tanja

(2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Smiljanić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5131
AB  - Objective. Camel milk is highly nutritious food with numerous health benefits
proposed. Demand for camel milk has increased worldwide. Production of camel milk
powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive
for various food products. In this study we characterized proteins of soluble fraction of
freeze/spray dried camel milk powders.
Material and Methods. Whole camel milk powders were prepared by spray drying
treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The
soluble protein fractions upon the treatments were analysed by combination of
electrophoretic and spectroscopic techniques. Functional properties, such as
antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while
native electrophoresis revealed non-uniform decrease in pI values with increased inlet
temperature of spray drying. That indicated attachement of lactose moieties to NH2-
group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis
showed formation of intermediate Maillard reaction products (increased absorbance at
294 nm) and no detectable late Maillard reaction products formation. Far-UV circular
dichroism spectra showed no differences in secondary structures between freeze and
spray dried samples. Antioxidant activity and protein solubility were increased with
increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promoted non-enzymatic
glycation of camel milk proteins. Glycation of food proteins affects their technofunctional
properties, shelf-life and nutritional value. Thus, optimization of spray
drying parametars is essential for production of high quality camel milk powders.
Acknowledgements: This research work was funded the Ministry of Education and Science of the Republic
of Serbia, GA No. OI172024, Ghent University Global Campus, Belgian Special Research Fund BOF StG No.
01N01718, Serbian Academy of Sciences and Arts Project F-26. The project leading to this application
has received funding from the European Union's Horizon 2020 research and innovation programme under
grant agreement No 810752.
C3  - 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia
T1  - Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures
SP  - 27
EP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5131
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola R. and Smiljanić, Katarina and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Objective. Camel milk is highly nutritious food with numerous health benefits
proposed. Demand for camel milk has increased worldwide. Production of camel milk
powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive
for various food products. In this study we characterized proteins of soluble fraction of
freeze/spray dried camel milk powders.
Material and Methods. Whole camel milk powders were prepared by spray drying
treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The
soluble protein fractions upon the treatments were analysed by combination of
electrophoretic and spectroscopic techniques. Functional properties, such as
antioxidant activity and protein solubility were assessed.
Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while
native electrophoresis revealed non-uniform decrease in pI values with increased inlet
temperature of spray drying. That indicated attachement of lactose moieties to NH2-
group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis
showed formation of intermediate Maillard reaction products (increased absorbance at
294 nm) and no detectable late Maillard reaction products formation. Far-UV circular
dichroism spectra showed no differences in secondary structures between freeze and
spray dried samples. Antioxidant activity and protein solubility were increased with
increase in inlet temperature.
Conclusions. Our results showed that spray drying treatment promoted non-enzymatic
glycation of camel milk proteins. Glycation of food proteins affects their technofunctional
properties, shelf-life and nutritional value. Thus, optimization of spray
drying parametars is essential for production of high quality camel milk powders.
Acknowledgements: This research work was funded the Ministry of Education and Science of the Republic
of Serbia, GA No. OI172024, Ghent University Global Campus, Belgian Special Research Fund BOF StG No.
01N01718, Serbian Academy of Sciences and Arts Project F-26. The project leading to this application
has received funding from the European Union's Horizon 2020 research and innovation programme under
grant agreement No 810752.",
journal = "1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia",
title = "Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5131"
}
Peruško, M., Simović, A., Stevanović, N. R., Smiljanić, K., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures. in 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia, 27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5131
Peruško M, Simović A, Stevanović NR, Smiljanić K, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures. in 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia. 2019;:27-27.
https://hdl.handle.net/21.15107/rcub_cherry_5131 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola R., Smiljanić, Katarina, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures" in 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Book of Abstracts, June 20-21, 2019, Belgrade, Serbia (2019):27-27,
https://hdl.handle.net/21.15107/rcub_cherry_5131 .

Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment

Peruško, Marija; Simović, Ana; Stevanović, Nikola; Smiljanić, Katarina; Radomirović, Mirjana Ž.; Stanić-Vučinić, Dragana; Ghnimi, Sami; Ćirković-Veličković, Tanja

(The Faculty of Sciences, University of Novi Sad, Serbian proteomic association, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola
AU  - Smiljanić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5129
AB  - Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand
for camel milk has increased worldwide.Production of camel milk powders facilitate its transport,
prolonge shelf-life, and also offer an attractive additive for various food products. In this study we
characterized proteins of soluble fraction of freeze/spray dried camel milk powders.
Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six
different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon
the treatments were analysed by combination of electrophoretic techniques and circular dichroism.
Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.
Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native
electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of
spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra
showed no differences in secondary structures between freeze and spray dried samples. Mass
spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1
(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum
albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne
(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on
immunoglobulin heavy chain.
Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray
drying treatment which further may affect techno-functional properties of camel milk powders,
their shelf-life and nutritional value.
Acknowledgments: This work was supported by the Ministry of Education, Science and
Technological Development of the Republic of Serbia, grant number 172024. The project leading to
this application has received funding from the European Union's Horizon 2020 research and
innovation programme under grant agreement No 810752.
PB  - The Faculty of Sciences, University of Novi Sad, Serbian proteomic association
C3  - The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia
T1  - Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment
SP  - 7
EP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5129
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola and Smiljanić, Katarina and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand
for camel milk has increased worldwide.Production of camel milk powders facilitate its transport,
prolonge shelf-life, and also offer an attractive additive for various food products. In this study we
characterized proteins of soluble fraction of freeze/spray dried camel milk powders.
Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six
different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon
the treatments were analysed by combination of electrophoretic techniques and circular dichroism.
Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.
Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native
electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of
spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra
showed no differences in secondary structures between freeze and spray dried samples. Mass
spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1
(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum
albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne
(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on
immunoglobulin heavy chain.
Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray
drying treatment which further may affect techno-functional properties of camel milk powders,
their shelf-life and nutritional value.
Acknowledgments: This work was supported by the Ministry of Education, Science and
Technological Development of the Republic of Serbia, grant number 172024. The project leading to
this application has received funding from the European Union's Horizon 2020 research and
innovation programme under grant agreement No 810752.",
publisher = "The Faculty of Sciences, University of Novi Sad, Serbian proteomic association",
journal = "The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia",
title = "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment",
pages = "7-7",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5129"
}
Peruško, M., Simović, A., Stevanović, N., Smiljanić, K., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia
The Faculty of Sciences, University of Novi Sad, Serbian proteomic association., 7-7.
https://hdl.handle.net/21.15107/rcub_cherry_5129
Peruško M, Simović A, Stevanović N, Smiljanić K, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia. 2019;:7-7.
https://hdl.handle.net/21.15107/rcub_cherry_5129 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola, Smiljanić, Katarina, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment" in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia (2019):7-7,
https://hdl.handle.net/21.15107/rcub_cherry_5129 .

Spray drying of camel milk induces protein aggregates and Maillard reaction products formation

Peruško, Marija; Stevanović, Nikola; Simović, Ana; Radomirović, Mirjana Ž.; Stanić-Vučinić, Dragana; Ghnimi, Sami; Ćirković-Veličković, Tanja

(Serbian Chemical Society, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Stevanović, Nikola
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5126
AB  - Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development.
PB  - Serbian Chemical Society
C3  - 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia
T1  - Spray drying of camel milk induces protein aggregates and Maillard reaction products formation
SP  - 73
EP  - 73
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5126
ER  - 
@conference{
author = "Peruško, Marija and Stevanović, Nikola and Simović, Ana and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development.",
publisher = "Serbian Chemical Society",
journal = "56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia",
title = "Spray drying of camel milk induces protein aggregates and Maillard reaction products formation",
pages = "73-73",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5126"
}
Peruško, M., Stevanović, N., Simović, A., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Spray drying of camel milk induces protein aggregates and Maillard reaction products formation. in 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia
Serbian Chemical Society., 73-73.
https://hdl.handle.net/21.15107/rcub_cherry_5126
Peruško M, Stevanović N, Simović A, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Spray drying of camel milk induces protein aggregates and Maillard reaction products formation. in 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia. 2019;:73-73.
https://hdl.handle.net/21.15107/rcub_cherry_5126 .
Peruško, Marija, Stevanović, Nikola, Simović, Ana, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Spray drying of camel milk induces protein aggregates and Maillard reaction products formation" in 56th meeting of the Serbian chemical society, Book of Abstracts, June 7-8, 2019, Niš, Serbia (2019):73-73,
https://hdl.handle.net/21.15107/rcub_cherry_5126 .

Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji

Peruško, Marija

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Peruško, Marija
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7689
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22883/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=24283145
UR  - https://nardus.mpn.gov.rs/handle/123456789/17612
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4385
AB  - Majarova reakcija (MR) je spontana reakcija izmeĊu karbonilne i amino grupe iod velikog je znaĉaja u hemiji hrane. Proteini modifikovani u MR imaju poboljšanetehno-funkcionalne osobine i nalaze primenu u prehrambenoj industriji. TakoĊe,strukture Majarovih proizvoda modifikovanih proteina imaju brojne efekte naalergenost proteina hrane.Predmet rada ove disertacije bilo je ispitivanje efekata MR indukovaneultrazvukom ili sušenjem raspršivanjem na fiziĉko-hemijske i tehno-funkcionalneosobine kravlje surutke i kamiljeg mleka, kao i efekata intenzivnog glikovanja u MR naimunološke osobine glavnog alergena kravljeg mleka, β-laktoglobulina (BLG).Kombinovana primena ultrazvuka i makromolekulskog nagomilavanja jeznaĉajnije ubrzala MR i glikovanje proteina nego sam ultrazvuĉni tretman.Makromolekulsko nagomilavanje, preko ubrzavanja MR, povećava oksidativnepromene na proteinima i formiranje struktura sliĉnih amiloidima. Visoko glikovaniproteini surutke su pokazali poboljšanu rastvorljivost u širokom pH i temperaturnomopsegu, kao i povećanu antioksidativnu moć.U kamiljem mleku u prahu sušenom raspršivanjem više temperature (230 °C –250 °C) su rezultirale većim stepenom MR u odnosu na niže temperature sušenja (190°C – 210 °C). Poboljšanje tehno-funkcionalnih osobina proteina kamiljeg mleka uprahu, kao što su antioksidativna moć i rastvorljivost, je pozitivno koreliralo sastepenom MR.Glikovanje BLG u MR, dovelo je do njegovog smanjenog transporta kroz modelsistem intestinalne barijere, povećanog preuzimanja od strane dendritskih ćelija,smanjenog luĉenja citokina u mešovitoj kulturi dendritskih ćelija sa CD4+ T-ćelijama, ido smanjene aktivacije bazofila, ukazujući da modifikovanje BLG u MR znaĉajnomenja njegovu sudbinu u procesima koji odreĊuju alergenost proteina mleka.
AB  - Maillard reaction (MR) is a spontaneous reaction between carbonil and aminogroup, and it is of high importance in food chemistry. Proteins modified in MR possessimproved techno-functional properties and they have application in food industry. MRproducts of food proteins exert numerous effects on food proteins allergenicity.The subject of this doctoral dissertation was to examine the effects of MRinduced by ultrasound or spray-drying on phisyco-chemical and techno-functionalproperties of cow whey proteins and camel milk proteins, as well as the effects of MRon immunologic properties of major cow milk allergen, β-lactoglobulin (BLG).Combined application of ultrasound and macromolecular crowding enhancedMR to a greater extent than ultrasound treatment alone. Macromolecular crowdingindirectly, by enhancing MR, intensified oxidative modifications of whey proteins andformation of amyloid-like structures. Highly glycated proteins exhibited improvedsolubility in wide pH range, thermal stability and antioxidative power.Upon spray-drying treatment of camel milk, higher temperatures (230 °C – 250°C) induced higher degree of MR compared to lower drying temperatures (190 °C – 210°C). Improvement of techno-functional properties of camel milk proteins, such asantioxidative power and solubility, strongly correlated with the degree of MR.Intensive glycation of BLG in MR reduced its transport through the modelsystem of intestinal barrier, increased uptake by dendritic cells and decreased cytokineproduction in dendritic cells/CD4+ T-cells coculture, as well as reduced basophilactivation, indicating that modification of BLG in MR alters its fate in processescrucially involved in allergenicity of milk proteins.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji
UR  - https://hdl.handle.net/21.15107/rcub_nardus_17612
ER  - 
@phdthesis{
author = "Peruško, Marija",
year = "2019",
abstract = "Majarova reakcija (MR) je spontana reakcija izmeĊu karbonilne i amino grupe iod velikog je znaĉaja u hemiji hrane. Proteini modifikovani u MR imaju poboljšanetehno-funkcionalne osobine i nalaze primenu u prehrambenoj industriji. TakoĊe,strukture Majarovih proizvoda modifikovanih proteina imaju brojne efekte naalergenost proteina hrane.Predmet rada ove disertacije bilo je ispitivanje efekata MR indukovaneultrazvukom ili sušenjem raspršivanjem na fiziĉko-hemijske i tehno-funkcionalneosobine kravlje surutke i kamiljeg mleka, kao i efekata intenzivnog glikovanja u MR naimunološke osobine glavnog alergena kravljeg mleka, β-laktoglobulina (BLG).Kombinovana primena ultrazvuka i makromolekulskog nagomilavanja jeznaĉajnije ubrzala MR i glikovanje proteina nego sam ultrazvuĉni tretman.Makromolekulsko nagomilavanje, preko ubrzavanja MR, povećava oksidativnepromene na proteinima i formiranje struktura sliĉnih amiloidima. Visoko glikovaniproteini surutke su pokazali poboljšanu rastvorljivost u širokom pH i temperaturnomopsegu, kao i povećanu antioksidativnu moć.U kamiljem mleku u prahu sušenom raspršivanjem više temperature (230 °C –250 °C) su rezultirale većim stepenom MR u odnosu na niže temperature sušenja (190°C – 210 °C). Poboljšanje tehno-funkcionalnih osobina proteina kamiljeg mleka uprahu, kao što su antioksidativna moć i rastvorljivost, je pozitivno koreliralo sastepenom MR.Glikovanje BLG u MR, dovelo je do njegovog smanjenog transporta kroz modelsistem intestinalne barijere, povećanog preuzimanja od strane dendritskih ćelija,smanjenog luĉenja citokina u mešovitoj kulturi dendritskih ćelija sa CD4+ T-ćelijama, ido smanjene aktivacije bazofila, ukazujući da modifikovanje BLG u MR znaĉajnomenja njegovu sudbinu u procesima koji odreĊuju alergenost proteina mleka., Maillard reaction (MR) is a spontaneous reaction between carbonil and aminogroup, and it is of high importance in food chemistry. Proteins modified in MR possessimproved techno-functional properties and they have application in food industry. MRproducts of food proteins exert numerous effects on food proteins allergenicity.The subject of this doctoral dissertation was to examine the effects of MRinduced by ultrasound or spray-drying on phisyco-chemical and techno-functionalproperties of cow whey proteins and camel milk proteins, as well as the effects of MRon immunologic properties of major cow milk allergen, β-lactoglobulin (BLG).Combined application of ultrasound and macromolecular crowding enhancedMR to a greater extent than ultrasound treatment alone. Macromolecular crowdingindirectly, by enhancing MR, intensified oxidative modifications of whey proteins andformation of amyloid-like structures. Highly glycated proteins exhibited improvedsolubility in wide pH range, thermal stability and antioxidative power.Upon spray-drying treatment of camel milk, higher temperatures (230 °C – 250°C) induced higher degree of MR compared to lower drying temperatures (190 °C – 210°C). Improvement of techno-functional properties of camel milk proteins, such asantioxidative power and solubility, strongly correlated with the degree of MR.Intensive glycation of BLG in MR reduced its transport through the modelsystem of intestinal barrier, increased uptake by dendritic cells and decreased cytokineproduction in dendritic cells/CD4+ T-cells coculture, as well as reduced basophilactivation, indicating that modification of BLG in MR alters its fate in processescrucially involved in allergenicity of milk proteins.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji",
url = "https://hdl.handle.net/21.15107/rcub_nardus_17612"
}
Peruško, M.. (2019). Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_17612
Peruško M. Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_nardus_17612 .
Peruško, Marija, "Struktura i funkcija proteina mleka modifikovanih u Majarovoj reakciji" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_nardus_17612 .

Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - DATA
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3205
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3205
ER  - 
@misc{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3205"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J.. (2018). Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341. in Molecular Nutrition and Food Research
Wiley, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3205
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341. in Molecular Nutrition and Food Research. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3205 .
Peruško, Marija, van Roest, Manon, Stanić-Vučinić, Dragana, Simons, Peter J., Pieters, Raymond, Ćirković-Veličković, Tanja, Smit, Joost, "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341" in Molecular Nutrition and Food Research (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3205 .

New insights into allergenic relationship between red meat and cow's milk

Peruško, Marija; Apostolović, Danijela; Ćirković-Veličković, Tanja; van Hage, Marianne

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2177
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - New insights into allergenic relationship between red meat and cow's milk
VL  - 8
SP  - 279
EP  - 279
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2177
ER  - 
@conference{
author = "Peruško, Marija and Apostolović, Danijela and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "New insights into allergenic relationship between red meat and cow's milk",
volume = "8",
pages = "279-279",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2177"
}
Peruško, M., Apostolović, D., Ćirković-Veličković, T.,& van Hage, M.. (2018). New insights into allergenic relationship between red meat and cow's milk. in FEBS OPEN BIO
Wiley, Hoboken., 8, 279-279.
https://hdl.handle.net/21.15107/rcub_cherry_2177
Peruško M, Apostolović D, Ćirković-Veličković T, van Hage M. New insights into allergenic relationship between red meat and cow's milk. in FEBS OPEN BIO. 2018;8:279-279.
https://hdl.handle.net/21.15107/rcub_cherry_2177 .
Peruško, Marija, Apostolović, Danijela, Ćirković-Veličković, Tanja, van Hage, Marianne, "New insights into allergenic relationship between red meat and cow's milk" in FEBS OPEN BIO, 8 (2018):279-279,
https://hdl.handle.net/21.15107/rcub_cherry_2177 .

Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2212
AB  - Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation
VL  - 62
IS  - 17
DO  - 10.1002/mnfr.201800341
ER  - 
@article{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
abstract = "Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation",
volume = "62",
number = "17",
doi = "10.1002/mnfr.201800341"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J.. (2018). Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. in Molecular Nutrition and Food Research
Wiley, Hoboken., 62(17).
https://doi.org/10.1002/mnfr.201800341
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. in Molecular Nutrition and Food Research. 2018;62(17).
doi:10.1002/mnfr.201800341 .
Peruško, Marija, van Roest, Manon, Stanić-Vučinić, Dragana, Simons, Peter J., Pieters, Raymond, Ćirković-Veličković, Tanja, Smit, Joost, "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation" in Molecular Nutrition and Food Research, 62, no. 17 (2018),
https://doi.org/10.1002/mnfr.201800341 . .
1
46
20
41
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Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, Snežana S.; Ognjenović, J.; Peruško, Marija; Mihajlović, Luka; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3126
AB  - Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
VL  - 47
IS  - 6
SP  - 815
EP  - 828
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
volume = "47",
number = "6",
pages = "815-828",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Wiley, Hoboken., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović L, Burazer LM, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .
2
24
15
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23

Supplementary data for article: Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, Snežana S.; Ognjenović, J.; Peruško, Marija; Mihajlović, Luka; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - DATA
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3127
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3127
ER  - 
@misc{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3127"
}
Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2017). Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874. in Clinical and Experimental Allergy
Wiley, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3127
Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović L, Burazer LM, van Hage M, Ćirković-Veličković T. Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874. in Clinical and Experimental Allergy. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3127 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874" in Clinical and Experimental Allergy (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3127 .

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, Snežana S.; Ognjenović, J.; Peruško, Marija; Mihajlović, Luka; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2468
AB  - Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
VL  - 47
IS  - 6
SP  - 815
EP  - 828
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
volume = "47",
number = "6",
pages = "815-828",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Wiley, Hoboken., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović L, Burazer LM, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .
2
24
15
21
23

Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Mihailović-Vesić, Jelena; Minić, Simeon L.; Trifunović, Sara; Prodić, Ivana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - JOUR
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović-Vesić, Jelena
AU  - Minić, Simeon L.
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2456
AB  - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
VL  - 232
SP  - 744
EP  - 752
DO  - 10.1016/j.foodchem.2017.04.074
ER  - 
@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction",
volume = "232",
pages = "744-752",
doi = "10.1016/j.foodchem.2017.04.074"
}
Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T.. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 232, 744-752.
https://doi.org/10.1016/j.foodchem.2017.04.074
Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry. 2017;232:744-752.
doi:10.1016/j.foodchem.2017.04.074 .
Peruško, Marija, Al-Hanish, Ayah, Mihailović-Vesić, Jelena, Minić, Simeon L., Trifunović, Sara, Prodić, Ivana, Ćirković-Veličković, Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" in Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 . .
35
24
34
33

Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074

Peruško, Marija; Al-Hanish, Ayah; Mihailović-Vesić, Jelena; Minić, Simeon L.; Trifunović, Sara; Prodić, Ivana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - DATA
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović-Vesić, Jelena
AU  - Minić, Simeon L.
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3027
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3027
ER  - 
@misc{
author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2017",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3027"
}
Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T.. (2017). Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074. in Food Chemistry
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3027
Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074. in Food Chemistry. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3027 .
Peruško, Marija, Al-Hanish, Ayah, Mihailović-Vesić, Jelena, Minić, Simeon L., Trifunović, Sara, Prodić, Ivana, Ćirković-Veličković, Tanja, "Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074" in Food Chemistry (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3027 .

Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis

Stein, Elisabeth; Mihailović-Vesić, Jelena; Inić-Kanada, Aleksandra; Smiljanić, Katarina; Peruško, Marija; Trifunović, Sara; Schuerer, Nadine; Stanić-Vučinić, Dragana; Ghasemian, Ehsan; Barisani-Asenbauer, Talin; Ćirković-Veličković, Tanja

(Assoc Research Vision Ophthalmology Inc, Rockville, 2017)

TY  - CONF
AU  - Stein, Elisabeth
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Peruško, Marija
AU  - Trifunović, Sara
AU  - Schuerer, Nadine
AU  - Stanić-Vučinić, Dragana
AU  - Ghasemian, Ehsan
AU  - Barisani-Asenbauer, Talin
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2139
PB  - Assoc Research Vision Ophthalmology Inc, Rockville
C3  - Investigative Ophthalmology and Visual Science
T1  - Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis
VL  - 58
IS  - 8
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2139
ER  - 
@conference{
author = "Stein, Elisabeth and Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Peruško, Marija and Trifunović, Sara and Schuerer, Nadine and Stanić-Vučinić, Dragana and Ghasemian, Ehsan and Barisani-Asenbauer, Talin and Ćirković-Veličković, Tanja",
year = "2017",
publisher = "Assoc Research Vision Ophthalmology Inc, Rockville",
journal = "Investigative Ophthalmology and Visual Science",
title = "Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis",
volume = "58",
number = "8",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2139"
}
Stein, E., Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Peruško, M., Trifunović, S., Schuerer, N., Stanić-Vučinić, D., Ghasemian, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2017). Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis. in Investigative Ophthalmology and Visual Science
Assoc Research Vision Ophthalmology Inc, Rockville., 58(8).
https://hdl.handle.net/21.15107/rcub_cherry_2139
Stein E, Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Peruško M, Trifunović S, Schuerer N, Stanić-Vučinić D, Ghasemian E, Barisani-Asenbauer T, Ćirković-Veličković T. Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis. in Investigative Ophthalmology and Visual Science. 2017;58(8).
https://hdl.handle.net/21.15107/rcub_cherry_2139 .
Stein, Elisabeth, Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Peruško, Marija, Trifunović, Sara, Schuerer, Nadine, Stanić-Vučinić, Dragana, Ghasemian, Ehsan, Barisani-Asenbauer, Talin, Ćirković-Veličković, Tanja, "Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis" in Investigative Ophthalmology and Visual Science, 58, no. 8 (2017),
https://hdl.handle.net/21.15107/rcub_cherry_2139 .

Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Elsevier Sci Ltd, Oxford, 2015)

TY  - JOUR
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5262
AB  - High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction
VL  - 177
SP  - 248
EP  - 257
DO  - 10.1016/j.foodchem.2015.01.042
ER  - 
@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2015",
abstract = "High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction",
volume = "177",
pages = "248-257",
doi = "10.1016/j.foodchem.2015.01.042"
}
Peruško, M., Al-Hanish, A., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2015). Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 177, 248-257.
https://doi.org/10.1016/j.foodchem.2015.01.042
Peruško M, Al-Hanish A, Ćirković-Veličković T, Stanić-Vučinić D. Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry. 2015;177:248-257.
doi:10.1016/j.foodchem.2015.01.042 .
Peruško, Marija, Al-Hanish, Ayah, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction" in Food Chemistry, 177 (2015):248-257,
https://doi.org/10.1016/j.foodchem.2015.01.042 . .
68
47
70
67

Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Elsevier Sci Ltd, Oxford, 2015)

TY  - JOUR
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1666
AB  - High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction
VL  - 177
SP  - 248
EP  - 257
DO  - 10.1016/j.foodchem.2015.01.042
ER  - 
@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2015",
abstract = "High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction",
volume = "177",
pages = "248-257",
doi = "10.1016/j.foodchem.2015.01.042"
}
Peruško, M., Al-Hanish, A., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2015). Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 177, 248-257.
https://doi.org/10.1016/j.foodchem.2015.01.042
Peruško M, Al-Hanish A, Ćirković-Veličković T, Stanić-Vučinić D. Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry. 2015;177:248-257.
doi:10.1016/j.foodchem.2015.01.042 .
Peruško, Marija, Al-Hanish, Ayah, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction" in Food Chemistry, 177 (2015):248-257,
https://doi.org/10.1016/j.foodchem.2015.01.042 . .
68
47
70