TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4976
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
VL  - 42
SP  - 2626
EP  - 2636
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2021",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
volume = "42",
pages = "2626-2636",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2021). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley., 42, 2626-2636.
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2021;42:2626-2636.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis, 42 (2021):2626-2636,
https://doi.org/10.1002/elps.202000092 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4977
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
VL  - 42
IS  - 24
SP  - 2626
EP  - 2636
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2021",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
volume = "42",
number = "24",
pages = "2626-2636",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2021). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley., 42(24), 2626-2636.
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2021;42(24):2626-2636.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis, 42, no. 24 (2021):2626-2636,
https://doi.org/10.1002/elps.202000092 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica M.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2557
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700221
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica M.",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700221"
}

Anđelković, U., Tufegdžić, S.,& Popović, M. M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700221

Anđelković U, Tufegdžić S, Popović MM. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700221 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica M., "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700221 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica M.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2976
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700221
ER  - 

@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica M.",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700221"
}

Anđelković, U., Tufegdžić, S.,& Popović, M. M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700221

Anđelković U, Tufegdžić S, Popović MM. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700221 .

Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica M., "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700221 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
AU  - Martinovic, Tamara
AU  - Josic, Djuro
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2963
AB  - Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.
PB  - Elsevier Sci Ltd, Oxford
T2  - Trends in Analytical Chemistry / TRAC
T1  - Omics methods as a tool for investigation of food allergies
VL  - 96
SP  - 107
EP  - 115
DO  - 10.1016/j.trac.2017.07.011
ER  - 

@article{
author = "Anđelković, Uroš and Gavrović-Jankulović, Marija and Martinovic, Tamara and Josic, Djuro",
year = "2017",
abstract = "Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Trends in Analytical Chemistry / TRAC",
title = "Omics methods as a tool for investigation of food allergies",
volume = "96",
pages = "107-115",
doi = "10.1016/j.trac.2017.07.011"
}

Anđelković, U., Gavrović-Jankulović, M., Martinovic, T.,& Josic, D.. (2017). Omics methods as a tool for investigation of food allergies. in Trends in Analytical Chemistry / TRAC
Elsevier Sci Ltd, Oxford., 96, 107-115.
https://doi.org/10.1016/j.trac.2017.07.011

Anđelković U, Gavrović-Jankulović M, Martinovic T, Josic D. Omics methods as a tool for investigation of food allergies. in Trends in Analytical Chemistry / TRAC. 2017;96:107-115.
doi:10.1016/j.trac.2017.07.011 .

Anđelković, Uroš, Gavrović-Jankulović, Marija, Martinovic, Tamara, Josic, Djuro, "Omics methods as a tool for investigation of food allergies" in Trends in Analytical Chemistry / TRAC, 96 (2017):107-115,
https://doi.org/10.1016/j.trac.2017.07.011 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gavrović-Jankulović, Marija
AU  - Martinovic, Tamara
AU  - Josic, Djuro
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2553
AB  - Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.
PB  - Elsevier Sci Ltd, Oxford
T2  - Trends in Analytical Chemistry / TRAC
T1  - Omics methods as a tool for investigation of food allergies
VL  - 96
SP  - 107
EP  - 115
DO  - 10.1016/j.trac.2017.07.011
ER  - 

@article{
author = "Anđelković, Uroš and Gavrović-Jankulović, Marija and Martinovic, Tamara and Josic, Djuro",
year = "2017",
abstract = "Use of foodomics, mostly proteomic and genomic based methods, for study of allergens in food is presented. Immunological methods and nucleic acid-based methods are still most frequently used for diagnosis of allergies and for qualitative and quantitative determination of food allergens. They are sensitive, and can be used for the determination of allergens in trace concentrations. However, lack of specificity and cross-reaction of some antibodies can still be a relevant source of bias. The epitopes of protein allergens with posttranslational modifications and their changes originated during food processing cannot be traced by use of nucleic acid-based strategies. Recent developments of both antibody and nucleic acid-based biosensors, their miniaturization and increasing application of nanotechnology, significantly supported further use of both strategies. Regarding accuracy, reliability and sensitivity, mass spectrometry-based methods bring important advantage over both above presented strategies. Furthermore, the increasing use of mass spectrometry (MS) is discussed. Combined with proper sample preparation, liquid chromatography (LC) and/or different electrophoretic methods, targeted approach in mass spectrometry-based allergen analysis brings an additional strategic advance. However, MS is still rarely used for high-throughput analyses and detection and quantification of allergens for the reasons of price and relatively long time necessary for analysis. Recent developments of new high-resolution instruments are encouraging and enable development in the direction of a high-throughput strategy. Consequently, fast, very sensitive, reliable and accurate detection and quantification of allergens in highly complex samples such as food matrices, and the use of MS in routine determination of allergens can be reached in near future.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Trends in Analytical Chemistry / TRAC",
title = "Omics methods as a tool for investigation of food allergies",
volume = "96",
pages = "107-115",
doi = "10.1016/j.trac.2017.07.011"
}

Anđelković, U., Gavrović-Jankulović, M., Martinovic, T.,& Josic, D.. (2017). Omics methods as a tool for investigation of food allergies. in Trends in Analytical Chemistry / TRAC
Elsevier Sci Ltd, Oxford., 96, 107-115.
https://doi.org/10.1016/j.trac.2017.07.011

Anđelković U, Gavrović-Jankulović M, Martinovic T, Josic D. Omics methods as a tool for investigation of food allergies. in Trends in Analytical Chemistry / TRAC. 2017;96:107-115.
doi:10.1016/j.trac.2017.07.011 .

Anđelković, Uroš, Gavrović-Jankulović, Marija, Martinovic, Tamara, Josic, Djuro, "Omics methods as a tool for investigation of food allergies" in Trends in Analytical Chemistry / TRAC, 96 (2017):107-115,
https://doi.org/10.1016/j.trac.2017.07.011 . .

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Čavić, Milena
AU  - Nešić, Andrijana N.
AU  - Anđelković, Uroš
AU  - Akbari, Peyman
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2039
AB  - Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions
VL  - 1860
IS  - 3
SP  - 516
EP  - 526
DO  - 10.1016/j.bbagen.2015.12.005
ER  - 

@article{
author = "Grozdanović, Milica M. and Čavić, Milena and Nešić, Andrijana N. and Anđelković, Uroš and Akbari, Peyman and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2016",
abstract = "Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions",
volume = "1860",
number = "3",
pages = "516-526",
doi = "10.1016/j.bbagen.2015.12.005"
}

Grozdanović, M. M., Čavić, M., Nešić, A. N., Anđelković, U., Akbari, P., Smit, J.,& Gavrović-Jankulović, M.. (2016). Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1860(3), 516-526.
https://doi.org/10.1016/j.bbagen.2015.12.005

Grozdanović MM, Čavić M, Nešić AN, Anđelković U, Akbari P, Smit J, Gavrović-Jankulović M. Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions. in Biochimica et Biophysica Acta: General Subjects. 2016;1860(3):516-526.
doi:10.1016/j.bbagen.2015.12.005 .

Grozdanović, Milica M., Čavić, Milena, Nešić, Andrijana N., Anđelković, Uroš, Akbari, Peyman, Smit, Joost, Gavrović-Jankulović, Marija, "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions" in Biochimica et Biophysica Acta: General Subjects, 1860, no. 3 (2016):516-526,
https://doi.org/10.1016/j.bbagen.2015.12.005 . .

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Čavić, Milena
AU  - Nešić, Andrijana N.
AU  - Anđelković, Uroš
AU  - Akbari, Peyman
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3559
AB  - Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions
VL  - 1860
IS  - 3
SP  - 516
EP  - 526
DO  - 10.1016/j.bbagen.2015.12.005
ER  - 

@article{
author = "Grozdanović, Milica M. and Čavić, Milena and Nešić, Andrijana N. and Anđelković, Uroš and Akbari, Peyman and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2016",
abstract = "Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions",
volume = "1860",
number = "3",
pages = "516-526",
doi = "10.1016/j.bbagen.2015.12.005"
}

Grozdanović, M. M., Čavić, M., Nešić, A. N., Anđelković, U., Akbari, P., Smit, J.,& Gavrović-Jankulović, M.. (2016). Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1860(3), 516-526.
https://doi.org/10.1016/j.bbagen.2015.12.005

Grozdanović MM, Čavić M, Nešić AN, Anđelković U, Akbari P, Smit J, Gavrović-Jankulović M. Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions. in Biochimica et Biophysica Acta: General Subjects. 2016;1860(3):516-526.
doi:10.1016/j.bbagen.2015.12.005 .

Grozdanović, Milica M., Čavić, Milena, Nešić, Andrijana N., Anđelković, Uroš, Akbari, Peyman, Smit, Joost, Gavrović-Jankulović, Marija, "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions" in Biochimica et Biophysica Acta: General Subjects, 1860, no. 3 (2016):516-526,
https://doi.org/10.1016/j.bbagen.2015.12.005 . .

TY  - DATA
AU  - Anđelković, Uroš
AU  - Milutinović-Nikolić, Aleksandra D.
AU  - Jović-Jovičić, Nataša
AU  - Banković, Predrag
AU  - Bajt, Teja
AU  - Mojović, Zorica D.
AU  - Vujčić, Zoran
AU  - Jovanović, Dušan
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3365
AB  - The external invertase isoform 1 (EINV1) was immobilised on eight differently modified beidellite nanoclays, Modifications were composed of organo-modification with different amounts of surfactant - hexadecyl trimethylammonium cation (HDTMA), pillaring with Al/Fe containing polyhydroxy cations and acid modification of Na-enriched and pillared clays. The modified nanoclays were characterised by XRD, N-2-physisorption, SEM and FT-IR spectroscopy. The amount of bound enzyme activity was significantly influenced by the modification of beidellite ranging from 50 to remarkable 2200 U/g. Biochemical characterization was performed for five modified nanoclays showing the highest enzyme activity after invertase immobilisation. The investigation demonstrated that after immobilisation the structure and the catalytic properties of invertase were preserved, while Km values were slightly increased from 26 to 37 mM. immobilisation significantly improved thermal and storage stability of EINV1. Results indicate that beidellite nanoclays obtained by low cost modifications can be applied as a suitable support for the immobilisation of invertase. The immobilizate can be efficiently engaged in sucrose hydrolysis in batch reactor.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for article: Andjelković, U.; Milutinović-Nikolić, A.; Jović-Jovičić, N.; Banković, P.; Bajt, T.; Mojović, Z.; Vujčić, Z.; Jovanović, D. Efficient Stabilization of Saccharomyces Cerevisiae External Invertase by Immobilisation on Modified Beidellite Nanoclays. Food Chemistry 2015, 168, 262–269. https://doi.org/10.1016/j.foodchem.2014.07.055
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3365
ER  - 

@misc{
author = "Anđelković, Uroš and Milutinović-Nikolić, Aleksandra D. and Jović-Jovičić, Nataša and Banković, Predrag and Bajt, Teja and Mojović, Zorica D. and Vujčić, Zoran and Jovanović, Dušan",
year = "2015",
abstract = "The external invertase isoform 1 (EINV1) was immobilised on eight differently modified beidellite nanoclays, Modifications were composed of organo-modification with different amounts of surfactant - hexadecyl trimethylammonium cation (HDTMA), pillaring with Al/Fe containing polyhydroxy cations and acid modification of Na-enriched and pillared clays. The modified nanoclays were characterised by XRD, N-2-physisorption, SEM and FT-IR spectroscopy. The amount of bound enzyme activity was significantly influenced by the modification of beidellite ranging from 50 to remarkable 2200 U/g. Biochemical characterization was performed for five modified nanoclays showing the highest enzyme activity after invertase immobilisation. The investigation demonstrated that after immobilisation the structure and the catalytic properties of invertase were preserved, while Km values were slightly increased from 26 to 37 mM. immobilisation significantly improved thermal and storage stability of EINV1. Results indicate that beidellite nanoclays obtained by low cost modifications can be applied as a suitable support for the immobilisation of invertase. The immobilizate can be efficiently engaged in sucrose hydrolysis in batch reactor.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for article: Andjelković, U.; Milutinović-Nikolić, A.; Jović-Jovičić, N.; Banković, P.; Bajt, T.; Mojović, Z.; Vujčić, Z.; Jovanović, D. Efficient Stabilization of Saccharomyces Cerevisiae External Invertase by Immobilisation on Modified Beidellite Nanoclays. Food Chemistry 2015, 168, 262–269. https://doi.org/10.1016/j.foodchem.2014.07.055",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3365"
}

Anđelković, U., Milutinović-Nikolić, A. D., Jović-Jovičić, N., Banković, P., Bajt, T., Mojović, Z. D., Vujčić, Z.,& Jovanović, D.. (2015). Supplementary data for article: Andjelković, U.; Milutinović-Nikolić, A.; Jović-Jovičić, N.; Banković, P.; Bajt, T.; Mojović, Z.; Vujčić, Z.; Jovanović, D. Efficient Stabilization of Saccharomyces Cerevisiae External Invertase by Immobilisation on Modified Beidellite Nanoclays. Food Chemistry 2015, 168, 262–269. https://doi.org/10.1016/j.foodchem.2014.07.055. in Food Chemistry
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3365

Anđelković U, Milutinović-Nikolić AD, Jović-Jovičić N, Banković P, Bajt T, Mojović ZD, Vujčić Z, Jovanović D. Supplementary data for article: Andjelković, U.; Milutinović-Nikolić, A.; Jović-Jovičić, N.; Banković, P.; Bajt, T.; Mojović, Z.; Vujčić, Z.; Jovanović, D. Efficient Stabilization of Saccharomyces Cerevisiae External Invertase by Immobilisation on Modified Beidellite Nanoclays. Food Chemistry 2015, 168, 262–269. https://doi.org/10.1016/j.foodchem.2014.07.055. in Food Chemistry. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3365 .

Anđelković, Uroš, Milutinović-Nikolić, Aleksandra D., Jović-Jovičić, Nataša, Banković, Predrag, Bajt, Teja, Mojović, Zorica D., Vujčić, Zoran, Jovanović, Dušan, "Supplementary data for article: Andjelković, U.; Milutinović-Nikolić, A.; Jović-Jovičić, N.; Banković, P.; Bajt, T.; Mojović, Z.; Vujčić, Z.; Jovanović, D. Efficient Stabilization of Saccharomyces Cerevisiae External Invertase by Immobilisation on Modified Beidellite Nanoclays. Food Chemistry 2015, 168, 262–269. https://doi.org/10.1016/j.foodchem.2014.07.055" in Food Chemistry (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3365 .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Milutinović-Nikolić, Aleksandra D.
AU  - Jović-Jovičić, Nataša
AU  - Banković, Predrag
AU  - Bajt, Teja
AU  - Mojović, Zorica D.
AU  - Vujčić, Zoran
AU  - Jovanović, Dušan
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1865
AB  - The external invertase isoform 1 (EINV1) was immobilised on eight differently modified beidellite nanoclays, Modifications were composed of organo-modification with different amounts of surfactant - hexadecyl trimethylammonium cation (HDTMA), pillaring with Al/Fe containing polyhydroxy cations and acid modification of Na-enriched and pillared clays. The modified nanoclays were characterised by XRD, N-2-physisorption, SEM and FT-IR spectroscopy. The amount of bound enzyme activity was significantly influenced by the modification of beidellite ranging from 50 to remarkable 2200 U/g. Biochemical characterization was performed for five modified nanoclays showing the highest enzyme activity after invertase immobilisation. The investigation demonstrated that after immobilisation the structure and the catalytic properties of invertase were preserved, while Km values were slightly increased from 26 to 37 mM. immobilisation significantly improved thermal and storage stability of EINV1. Results indicate that beidellite nanoclays obtained by low cost modifications can be applied as a suitable support for the immobilisation of invertase. The immobilizate can be efficiently engaged in sucrose hydrolysis in batch reactor.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays
VL  - 168
SP  - 262
EP  - 269
DO  - 10.1016/j.foodchem.2014.07.055
ER  - 

@article{
author = "Anđelković, Uroš and Milutinović-Nikolić, Aleksandra D. and Jović-Jovičić, Nataša and Banković, Predrag and Bajt, Teja and Mojović, Zorica D. and Vujčić, Zoran and Jovanović, Dušan",
year = "2015",
abstract = "The external invertase isoform 1 (EINV1) was immobilised on eight differently modified beidellite nanoclays, Modifications were composed of organo-modification with different amounts of surfactant - hexadecyl trimethylammonium cation (HDTMA), pillaring with Al/Fe containing polyhydroxy cations and acid modification of Na-enriched and pillared clays. The modified nanoclays were characterised by XRD, N-2-physisorption, SEM and FT-IR spectroscopy. The amount of bound enzyme activity was significantly influenced by the modification of beidellite ranging from 50 to remarkable 2200 U/g. Biochemical characterization was performed for five modified nanoclays showing the highest enzyme activity after invertase immobilisation. The investigation demonstrated that after immobilisation the structure and the catalytic properties of invertase were preserved, while Km values were slightly increased from 26 to 37 mM. immobilisation significantly improved thermal and storage stability of EINV1. Results indicate that beidellite nanoclays obtained by low cost modifications can be applied as a suitable support for the immobilisation of invertase. The immobilizate can be efficiently engaged in sucrose hydrolysis in batch reactor.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays",
volume = "168",
pages = "262-269",
doi = "10.1016/j.foodchem.2014.07.055"
}

Anđelković, U., Milutinović-Nikolić, A. D., Jović-Jovičić, N., Banković, P., Bajt, T., Mojović, Z. D., Vujčić, Z.,& Jovanović, D.. (2015). Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays. in Food Chemistry
Elsevier Sci Ltd, Oxford., 168, 262-269.
https://doi.org/10.1016/j.foodchem.2014.07.055

Anđelković U, Milutinović-Nikolić AD, Jović-Jovičić N, Banković P, Bajt T, Mojović ZD, Vujčić Z, Jovanović D. Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays. in Food Chemistry. 2015;168:262-269.
doi:10.1016/j.foodchem.2014.07.055 .

Anđelković, Uroš, Milutinović-Nikolić, Aleksandra D., Jović-Jovičić, Nataša, Banković, Predrag, Bajt, Teja, Mojović, Zorica D., Vujčić, Zoran, Jovanović, Dušan, "Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays" in Food Chemistry, 168 (2015):262-269,
https://doi.org/10.1016/j.foodchem.2014.07.055 . .

TY  - JOUR
AU  - Prokopovic, Vladimir
AU  - Popović, Milica M.
AU  - Anđelković, Uroš
AU  - Marsavelski, Aleksandra
AU  - Rašković, Brankica
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1520
AB  - Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Archives of Oral Biology
T1  - Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein
VL  - 59
IS  - 3
SP  - 302
EP  - 309
DO  - 10.1016/j.archoralbio.2013.12.005
ER  - 

@article{
author = "Prokopovic, Vladimir and Popović, Milica M. and Anđelković, Uroš and Marsavelski, Aleksandra and Rašković, Brankica and Gavrović-Jankulović, Marija and Polović, Natalija",
year = "2014",
abstract = "Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Archives of Oral Biology",
title = "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein",
volume = "59",
number = "3",
pages = "302-309",
doi = "10.1016/j.archoralbio.2013.12.005"
}

Prokopovic, V., Popović, M. M., Anđelković, U., Marsavelski, A., Rašković, B., Gavrović-Jankulović, M.,& Polović, N.. (2014). Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology
Pergamon-Elsevier Science Ltd, Oxford., 59(3), 302-309.
https://doi.org/10.1016/j.archoralbio.2013.12.005

Prokopovic V, Popović MM, Anđelković U, Marsavelski A, Rašković B, Gavrović-Jankulović M, Polović N. Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology. 2014;59(3):302-309.
doi:10.1016/j.archoralbio.2013.12.005 .

Prokopovic, Vladimir, Popović, Milica M., Anđelković, Uroš, Marsavelski, Aleksandra, Rašković, Brankica, Gavrović-Jankulović, Marija, Polović, Natalija, "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein" in Archives of Oral Biology, 59, no. 3 (2014):302-309,
https://doi.org/10.1016/j.archoralbio.2013.12.005 . .

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Ostojić, Sanja B.
AU  - Aleksić, Ivana
AU  - Anđelković, Uroš
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1859
AB  - BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart
VL  - 94
IS  - 14
SP  - 3046
EP  - 3052
DO  - 10.1002/jsfa.6656
ER  - 

@article{
author = "Grozdanović, Milica M. and Ostojić, Sanja B. and Aleksić, Ivana and Anđelković, Uroš and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart",
volume = "94",
number = "14",
pages = "3046-3052",
doi = "10.1002/jsfa.6656"
}

Grozdanović, M. M., Ostojić, S. B., Aleksić, I., Anđelković, U., Petersen, A.,& Gavrović-Jankulović, M.. (2014). Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Hoboken., 94(14), 3046-3052.
https://doi.org/10.1002/jsfa.6656

Grozdanović MM, Ostojić SB, Aleksić I, Anđelković U, Petersen A, Gavrović-Jankulović M. Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture. 2014;94(14):3046-3052.
doi:10.1002/jsfa.6656 .

Grozdanović, Milica M., Ostojić, Sanja B., Aleksić, Ivana, Anđelković, Uroš, Petersen, Arnd, Gavrović-Jankulović, Marija, "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart" in Journal of the Science of Food and Agriculture, 94, no. 14 (2014):3046-3052,
https://doi.org/10.1002/jsfa.6656 . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Abughren, Mohamed
AU  - Nikolić, Jasna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1774
AB  - Allergy to banana fruit appears to have become an important cause of fruit allergy in Europe. Among five allergens that have been found, beta-1,3-glucanase denoted as Mus a 5 was identified as a candidate allergen for the component-resolved allergy diagnosis of banana allergy. Because of the variations in protein levels in banana fruit, in this study Mus a 5 was produced as a fusion protein with glutathione-S-transferase in Escherichia coli. The recombinant Mus a 5 was purified under native conditions by a combination of affinity, ion-exchange, and reversed phase chromatography. N-terminal sequence was confirmed by Edman degradation and 55 % of the primary structure was identified by mass fingerprint, while the secondary structure was assessed by circular dichroism spectroscopy. IgG reactivity of recombinant protein was shown in 2-D immunoblot with anti-Mus a 5 antibodies, while IgG and IgE binding to natural Mus a 5 was inhibited with the recombinant Mus a 5 in immunoblot inhibition test. IgE reactivity of recombinant Mus a 5 was shown in ELISA within a group of ten persons sensitized to banana fruit. Recombinant Mus a 5 is a novel reagent suitable for the component-resolved allergy diagnosis of banana allergy.
PB  - Humana Press Inc, Totowa
T2  - Molecular Biotechnology
T1  - Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit
VL  - 56
IS  - 6
SP  - 498
EP  - 506
DO  - 10.1007/s12033-013-9719-8
ER  - 

@article{
author = "Mrkić, Ivan and Abughren, Mohamed and Nikolić, Jasna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "Allergy to banana fruit appears to have become an important cause of fruit allergy in Europe. Among five allergens that have been found, beta-1,3-glucanase denoted as Mus a 5 was identified as a candidate allergen for the component-resolved allergy diagnosis of banana allergy. Because of the variations in protein levels in banana fruit, in this study Mus a 5 was produced as a fusion protein with glutathione-S-transferase in Escherichia coli. The recombinant Mus a 5 was purified under native conditions by a combination of affinity, ion-exchange, and reversed phase chromatography. N-terminal sequence was confirmed by Edman degradation and 55 % of the primary structure was identified by mass fingerprint, while the secondary structure was assessed by circular dichroism spectroscopy. IgG reactivity of recombinant protein was shown in 2-D immunoblot with anti-Mus a 5 antibodies, while IgG and IgE binding to natural Mus a 5 was inhibited with the recombinant Mus a 5 in immunoblot inhibition test. IgE reactivity of recombinant Mus a 5 was shown in ELISA within a group of ten persons sensitized to banana fruit. Recombinant Mus a 5 is a novel reagent suitable for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Humana Press Inc, Totowa",
journal = "Molecular Biotechnology",
title = "Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit",
volume = "56",
number = "6",
pages = "498-506",
doi = "10.1007/s12033-013-9719-8"
}

Mrkić, I., Abughren, M., Nikolić, J., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2014). Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit. in Molecular Biotechnology
Humana Press Inc, Totowa., 56(6), 498-506.
https://doi.org/10.1007/s12033-013-9719-8

Mrkić I, Abughren M, Nikolić J, Anđelković U, Vassilopoulou E, Sinaniotis A, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit. in Molecular Biotechnology. 2014;56(6):498-506.
doi:10.1007/s12033-013-9719-8 .

Mrkić, Ivan, Abughren, Mohamed, Nikolić, Jasna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit" in Molecular Biotechnology, 56, no. 6 (2014):498-506,
https://doi.org/10.1007/s12033-013-9719-8 . .

TY  - JOUR
AU  - Popović, Milica M.
AU  - Anđelković, Uroš
AU  - Burazer, Lidija M.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1403
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
VL  - 94
SP  - 53
EP  - 59
DO  - 10.1016/j.phytochem.2013.06.006
ER  - 

@article{
author = "Popović, Milica M. and Anđelković, Uroš and Burazer, Lidija M. and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
volume = "94",
pages = "53-59",
doi = "10.1016/j.phytochem.2013.06.006"
}

Popović, M. M., Anđelković, U., Burazer, L. M., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006

Popović MM, Anđelković U, Burazer LM, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006 .

Popović, Milica M., Anđelković, Uroš, Burazer, Lidija M., Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 . .

TY  - JOUR
AU  - Popović, Milica M.
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1612
AB  - The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.
PB  - Springer, New York
T2  - Indian Journal of Microbiology
T1  - In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)
VL  - 53
IS  - 1
SP  - 100
EP  - 105
DO  - 10.1007/s12088-012-0319-2
ER  - 

@article{
author = "Popović, Milica M. and Anđelković, Uroš and Grozdanović, Milica and Aleksić, Ivana and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.",
publisher = "Springer, New York",
journal = "Indian Journal of Microbiology",
title = "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)",
volume = "53",
number = "1",
pages = "100-105",
doi = "10.1007/s12088-012-0319-2"
}

Popović, M. M., Anđelković, U., Grozdanović, M., Aleksić, I.,& Gavrović-Jankulović, M.. (2013). In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology
Springer, New York., 53(1), 100-105.
https://doi.org/10.1007/s12088-012-0319-2

Popović MM, Anđelković U, Grozdanović M, Aleksić I, Gavrović-Jankulović M. In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology. 2013;53(1):100-105.
doi:10.1007/s12088-012-0319-2 .

Popović, Milica M., Anđelković, Uroš, Grozdanović, Milica, Aleksić, Ivana, Gavrović-Jankulović, Marija, "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)" in Indian Journal of Microbiology, 53, no. 1 (2013):100-105,
https://doi.org/10.1007/s12088-012-0319-2 . .

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1268
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley-Blackwell, Malden
T2  - Molecular Nutrition and Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
VL  - 56
IS  - 3
SP  - 446
EP  - 453
DO  - 10.1002/mnfr.201100541
ER  - 

@article{
author = "Aleksić, Ivana and Popović, Milica M. and Dimitrijevic, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley-Blackwell, Malden",
journal = "Molecular Nutrition and Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
volume = "56",
number = "3",
pages = "446-453",
doi = "10.1002/mnfr.201100541"
}

Aleksić, I., Popović, M. M., Dimitrijevic, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research
Wiley-Blackwell, Malden., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541

Aleksić I, Popović MM, Dimitrijevic R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541 .

Aleksić, Ivana, Popović, Milica M., Dimitrijevic, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition and Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Theisgen, Stephan
AU  - Scheidt, Holger A.
AU  - Petković, Marijana
AU  - Huster, Daniel
AU  - Vujčić, Zoran
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1245
AB  - Understanding the effect of surface charge on the stability of proteins is one prerequisite for "tailoring" proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins. (C) 2011 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - Biochimie
T1  - The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density
VL  - 94
IS  - 2
SP  - 510
EP  - 515
DO  - 10.1016/j.biochi.2011.08.020
ER  - 

@article{
author = "Anđelković, Uroš and Theisgen, Stephan and Scheidt, Holger A. and Petković, Marijana and Huster, Daniel and Vujčić, Zoran",
year = "2012",
abstract = "Understanding the effect of surface charge on the stability of proteins is one prerequisite for "tailoring" proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins. (C) 2011 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "Biochimie",
title = "The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density",
volume = "94",
number = "2",
pages = "510-515",
doi = "10.1016/j.biochi.2011.08.020"
}

Anđelković, U., Theisgen, S., Scheidt, H. A., Petković, M., Huster, D.,& Vujčić, Z.. (2012). The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. in Biochimie
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 94(2), 510-515.
https://doi.org/10.1016/j.biochi.2011.08.020

Anđelković U, Theisgen S, Scheidt HA, Petković M, Huster D, Vujčić Z. The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. in Biochimie. 2012;94(2):510-515.
doi:10.1016/j.biochi.2011.08.020 .

Anđelković, Uroš, Theisgen, Stephan, Scheidt, Holger A., Petković, Marijana, Huster, Daniel, Vujčić, Zoran, "The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density" in Biochimie, 94, no. 2 (2012):510-515,
https://doi.org/10.1016/j.biochi.2011.08.020 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Anđelković, Uroš
AU  - Lončar, Nikola L.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1133
AB  - Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.
PB  - Amer Chemical Soc, Washington
T2  - Journal of Agricultural and Food Chemistry
T1  - Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar
VL  - 58
IS  - 22
SP  - 11896
EP  - 11900
DO  - 10.1021/jf101836r
ER  - 

@article{
author = "Vujčić, Zoran and Milovanovic, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava and Anđelković, Uroš and Lončar, Nikola L.",
year = "2010",
abstract = "Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.",
publisher = "Amer Chemical Soc, Washington",
journal = "Journal of Agricultural and Food Chemistry",
title = "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar",
volume = "58",
number = "22",
pages = "11896-11900",
doi = "10.1021/jf101836r"
}

Vujčić, Z., Milovanovic, A., Božić, N., Dojnov, B., Vujčić, M., Anđelković, U.,& Lončar, N. L.. (2010). Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry
Amer Chemical Soc, Washington., 58(22), 11896-11900.
https://doi.org/10.1021/jf101836r

Vujčić Z, Milovanovic A, Božić N, Dojnov B, Vujčić M, Anđelković U, Lončar NL. Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry. 2010;58(22):11896-11900.
doi:10.1021/jf101836r .

Vujčić, Zoran, Milovanovic, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, Anđelković, Uroš, Lončar, Nikola L., "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar" in Journal of Agricultural and Food Chemistry, 58, no. 22 (2010):11896-11900,
https://doi.org/10.1021/jf101836r . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Picuric, Srdjan
AU  - Vujčić, Zoran
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1052
AB  - Four external invertase isoforms (EINV1, EINV2, EINV3 and EINV4) from Saccharomyces cerevisiae were highly purified by isoelectric precipitation, ethanol precipitation, ion-exchange on QAE-Sephadex and gel filtration using Sephacryl S-200. Unlike previously published procedures for external invertase purification, a specially designed step elution was applied on QAE-Sephadex which enabled the separation of four isoforms. The isoforms have the same molecular mass and catalytic properties: K-m for sucrose (25.6 mM), pH optimum (3.5-5.0) and temperature optimum (60 degrees C), but they exhibit significant difference in pl values, thermal stability and chemical reactivity. Deglycosylation Studies showed that the observed differences between isoforms arise from posttranslational modifications. Results showed that external invertase is a mixture of at least four isoforms, but in order to improve the efficiency of food industry processes, only the most stable isoform (EINV1) should be purified and utilised. Substantially different chemical reactivity of the isoforms could be used to improve the yield of covalent immobilization procedures. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms
VL  - 120
IS  - 3
SP  - 799
EP  - 804
DO  - 10.1016/j.foodchem.2009.11.013
ER  - 

@article{
author = "Anđelković, Uroš and Picuric, Srdjan and Vujčić, Zoran",
year = "2010",
abstract = "Four external invertase isoforms (EINV1, EINV2, EINV3 and EINV4) from Saccharomyces cerevisiae were highly purified by isoelectric precipitation, ethanol precipitation, ion-exchange on QAE-Sephadex and gel filtration using Sephacryl S-200. Unlike previously published procedures for external invertase purification, a specially designed step elution was applied on QAE-Sephadex which enabled the separation of four isoforms. The isoforms have the same molecular mass and catalytic properties: K-m for sucrose (25.6 mM), pH optimum (3.5-5.0) and temperature optimum (60 degrees C), but they exhibit significant difference in pl values, thermal stability and chemical reactivity. Deglycosylation Studies showed that the observed differences between isoforms arise from posttranslational modifications. Results showed that external invertase is a mixture of at least four isoforms, but in order to improve the efficiency of food industry processes, only the most stable isoform (EINV1) should be purified and utilised. Substantially different chemical reactivity of the isoforms could be used to improve the yield of covalent immobilization procedures. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms",
volume = "120",
number = "3",
pages = "799-804",
doi = "10.1016/j.foodchem.2009.11.013"
}

Anđelković, U., Picuric, S.,& Vujčić, Z.. (2010). Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(3), 799-804.
https://doi.org/10.1016/j.foodchem.2009.11.013

Anđelković U, Picuric S, Vujčić Z. Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms. in Food Chemistry. 2010;120(3):799-804.
doi:10.1016/j.foodchem.2009.11.013 .

Anđelković, Uroš, Picuric, Srdjan, Vujčić, Zoran, "Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms" in Food Chemistry, 120, no. 3 (2010):799-804,
https://doi.org/10.1016/j.foodchem.2009.11.013 . .