TY  - DATA
AU  - Mihajlović, L.
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3591
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3591
ER  - 

@misc{
author = "Mihajlović, L. and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3591"
}

Mihajlović, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a. in Food and Function
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3591

Mihajlović L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a. in Food and Function. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3591 .

Mihajlović, L., Radosavljević, Jelena, Nordlund, Emilia, Krstić-Ristivojević, Maja, Bohn, Torsten, Smit, Joost, Buchert, Johanna, Ćirković-Veličković, Tanja, "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a" in Food and Function (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3591 .

TY  - JOUR
AU  - Mihajlović, L.
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2254
AB  - Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase
VL  - 7
IS  - 5
SP  - 2357
EP  - 2366
DO  - 10.1039/c5fo01325a
ER  - 

@article{
author = "Mihajlović, L. and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase",
volume = "7",
number = "5",
pages = "2357-2366",
doi = "10.1039/c5fo01325a"
}

Mihajlović, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T.. (2016). Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase. in Food and Function
Royal Soc Chemistry, Cambridge., 7(5), 2357-2366.
https://doi.org/10.1039/c5fo01325a

Mihajlović L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase. in Food and Function. 2016;7(5):2357-2366.
doi:10.1039/c5fo01325a .

Mihajlović, L., Radosavljević, Jelena, Nordlund, Emilia, Krstić-Ristivojević, Maja, Bohn, Torsten, Smit, Joost, Buchert, Johanna, Ćirković-Veličković, Tanja, "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase" in Food and Function, 7, no. 5 (2016):2357-2366,
https://doi.org/10.1039/c5fo01325a . .

TY  - CHAP
AU  - Ćirković-Veličković, Tanja
AU  - Ognjenović, J.
AU  - Mihajlović, L.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/290
AB  - Separation of amino acids, peptides, and proteins (bioanalytes) via ion exchange (IE) has widespread usage because it is usually very simple to design and it has high capacity and easily achievable control of the separation process. Amino acids, as principal constituents of proteins and having a plethora of biological functions of their own, are always in focus when developing novel methods. Separation and quantification of amino acids is essential in food science, medicine, agricultural science, etc. Peptides exist in nature and have diverse functions. Digestion of proteins by enzymes also gives complex mixtures of peptides and IE finds its application in peptide separation. There are lots of reasons for the popularity of IE in protein isolation and purification. It is used in research, analysis, and large-scale purification of proteins. Ion exchange is ideal for the initial capture of proteins because of its high capacity, relatively low cost, and its ability to survive rigorous cleaning regimes. This chapter covers basic principles and modern applications of IE in separation of amino acids, peptides, and proteins. © 2012 Springer Science+Business Media B.V. All rights are reserved.
T2  - Ion Exchange Technology II: Applications
T1  - Separation of amino acids, peptides, and proteins by ion exchange chromatography
SP  - 1
EP  - 34
DO  - 10.1007/978-94-007-4026-6_1
ER  - 

@inbook{
author = "Ćirković-Veličković, Tanja and Ognjenović, J. and Mihajlović, L.",
year = "2012",
abstract = "Separation of amino acids, peptides, and proteins (bioanalytes) via ion exchange (IE) has widespread usage because it is usually very simple to design and it has high capacity and easily achievable control of the separation process. Amino acids, as principal constituents of proteins and having a plethora of biological functions of their own, are always in focus when developing novel methods. Separation and quantification of amino acids is essential in food science, medicine, agricultural science, etc. Peptides exist in nature and have diverse functions. Digestion of proteins by enzymes also gives complex mixtures of peptides and IE finds its application in peptide separation. There are lots of reasons for the popularity of IE in protein isolation and purification. It is used in research, analysis, and large-scale purification of proteins. Ion exchange is ideal for the initial capture of proteins because of its high capacity, relatively low cost, and its ability to survive rigorous cleaning regimes. This chapter covers basic principles and modern applications of IE in separation of amino acids, peptides, and proteins. © 2012 Springer Science+Business Media B.V. All rights are reserved.",
journal = "Ion Exchange Technology II: Applications",
booktitle = "Separation of amino acids, peptides, and proteins by ion exchange chromatography",
pages = "1-34",
doi = "10.1007/978-94-007-4026-6_1"
}

Ćirković-Veličković, T., Ognjenović, J.,& Mihajlović, L.. (2012). Separation of amino acids, peptides, and proteins by ion exchange chromatography. in Ion Exchange Technology II: Applications, 1-34.
https://doi.org/10.1007/978-94-007-4026-6_1

Ćirković-Veličković T, Ognjenović J, Mihajlović L. Separation of amino acids, peptides, and proteins by ion exchange chromatography. in Ion Exchange Technology II: Applications. 2012;:1-34.
doi:10.1007/978-94-007-4026-6_1 .

Ćirković-Veličković, Tanja, Ognjenović, J., Mihajlović, L., "Separation of amino acids, peptides, and proteins by ion exchange chromatography" in Ion Exchange Technology II: Applications (2012):1-34,
https://doi.org/10.1007/978-94-007-4026-6_1 . .

TY  - CONF
AU  - Ognjenović, J.
AU  - Mihajlovic, L.
AU  - Stanić-Vučinić, Dragana
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1544
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals
VL  - 67
SP  - 638
EP  - 639
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1544
ER  - 

@conference{
author = "Ognjenović, J. and Mihajlovic, L. and Stanić-Vučinić, Dragana and Atanasković-Marković, Marina and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2012",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals",
volume = "67",
pages = "638-639",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1544"
}

Ognjenović, J., Mihajlovic, L., Stanić-Vučinić, D., Atanasković-Marković, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2012). Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals. in Allergy
Wiley-Blackwell, Hoboken., 67, 638-639.
https://hdl.handle.net/21.15107/rcub_cherry_1544

Ognjenović J, Mihajlovic L, Stanić-Vučinić D, Atanasković-Marković M, Burazer LM, Ćirković-Veličković T. Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals. in Allergy. 2012;67:638-639.
https://hdl.handle.net/21.15107/rcub_cherry_1544 .

Ognjenović, J., Mihajlovic, L., Stanić-Vučinić, Dragana, Atanasković-Marković, Marina, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals" in Allergy, 67 (2012):638-639,
https://hdl.handle.net/21.15107/rcub_cherry_1544 .

TY  - CONF
AU  - Mihajlović, L.
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1592
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding
VL  - 66
SP  - 536
EP  - 536
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1592
ER  - 

@conference{
author = "Mihajlović, L. and Radosavljević, Jelena and Nordlund, Emilia and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding",
volume = "66",
pages = "536-536",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1592"
}

Mihajlović, L., Radosavljević, J., Nordlund, E., Smit, J., Buchert, J.,& Ćirković-Veličković, T.. (2011). Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding. in Allergy
Wiley-Blackwell, Hoboken., 66, 536-536.
https://hdl.handle.net/21.15107/rcub_cherry_1592

Mihajlović L, Radosavljević J, Nordlund E, Smit J, Buchert J, Ćirković-Veličković T. Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding. in Allergy. 2011;66:536-536.
https://hdl.handle.net/21.15107/rcub_cherry_1592 .

Mihajlović, L., Radosavljević, Jelena, Nordlund, Emilia, Smit, Joost, Buchert, Johanna, Ćirković-Veličković, Tanja, "Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding" in Allergy, 66 (2011):536-536,
https://hdl.handle.net/21.15107/rcub_cherry_1592 .

TY  - CONF
AU  - Mihajlović, L.
AU  - Ćirković-Veličković, Tanja
AU  - Jadranin, Milka
AU  - Burazer, Lidija M.
AU  - Milčić-Matić, Natalija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1469
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - The role of phenolic components of short ragweed pollen in igE binding and immune response to allergens
VL  - 65
SP  - 331
EP  - 331
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1469
ER  - 

@conference{
author = "Mihajlović, L. and Ćirković-Veličković, Tanja and Jadranin, Milka and Burazer, Lidija M. and Milčić-Matić, Natalija",
year = "2010",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "The role of phenolic components of short ragweed pollen in igE binding and immune response to allergens",
volume = "65",
pages = "331-331",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1469"
}

Mihajlović, L., Ćirković-Veličković, T., Jadranin, M., Burazer, L. M.,& Milčić-Matić, N.. (2010). The role of phenolic components of short ragweed pollen in igE binding and immune response to allergens. in Allergy
Wiley-Blackwell, Hoboken., 65, 331-331.
https://hdl.handle.net/21.15107/rcub_cherry_1469

Mihajlović L, Ćirković-Veličković T, Jadranin M, Burazer LM, Milčić-Matić N. The role of phenolic components of short ragweed pollen in igE binding and immune response to allergens. in Allergy. 2010;65:331-331.
https://hdl.handle.net/21.15107/rcub_cherry_1469 .

Mihajlović, L., Ćirković-Veličković, Tanja, Jadranin, Milka, Burazer, Lidija M., Milčić-Matić, Natalija, "The role of phenolic components of short ragweed pollen in igE binding and immune response to allergens" in Allergy, 65 (2010):331-331,
https://hdl.handle.net/21.15107/rcub_cherry_1469 .