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Supplementary data for the article: Pećinar, Ilinka, Djurdja Krstić, Gianluca Caruso, and Jelena B. Popović-Djordjević. n.d. ‘Rapid Characterization of Hypanthium and Seed in Wild and Cultivated Rosehip: Application of Raman Microscopy Combined with Multivariate Analysis’. Royal Society Open Science 8 (3): 202064. https://doi.org/10.1098/rsos.202064.

Pećinar, Ilinka; Krstić, Đurđa D.; Caruso, Gianluca; Popović-Đorđević, Jelena

TY  - BOOK
AU  - Pećinar, Ilinka
AU  - Krstić, Đurđa D.
AU  - Caruso, Gianluca
AU  - Popović-Đorđević, Jelena
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4461
PB  - The Royal Society
T2  - Royal Society Open Science
T1  - Supplementary data for the article: Pećinar, Ilinka, Djurdja Krstić, Gianluca Caruso, and Jelena B. Popović-Djordjević. n.d. ‘Rapid Characterization of Hypanthium and Seed in Wild and Cultivated Rosehip: Application of Raman Microscopy Combined with Multivariate Analysis’. Royal Society Open Science 8 (3): 202064. https://doi.org/10.1098/rsos.202064.
ER  - 
@book{
author = "Pećinar, Ilinka and Krstić, Đurđa D. and Caruso, Gianluca and Popović-Đorđević, Jelena",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4461",
publisher = "The Royal Society",
journal = "Royal Society Open Science",
title = "Supplementary data for the article: Pećinar, Ilinka, Djurdja Krstić, Gianluca Caruso, and Jelena B. Popović-Djordjević. n.d. ‘Rapid Characterization of Hypanthium and Seed in Wild and Cultivated Rosehip: Application of Raman Microscopy Combined with Multivariate Analysis’. Royal Society Open Science 8 (3): 202064. https://doi.org/10.1098/rsos.202064."
}
Pećinar, I., Krstić, Đ. D., Caruso, G.,& Popović-Đorđević, J.Supplementary data for the article: Pećinar, Ilinka, Djurdja Krstić, Gianluca Caruso, and Jelena B. Popović-Djordjević. n.d. ‘Rapid Characterization of Hypanthium and Seed in Wild and Cultivated Rosehip: Application of Raman Microscopy Combined with Multivariate Analysis’. Royal Society Open Science 8 (3): 202064. https://doi.org/10.1098/rsos.202064..
Royal Society Open Science
The Royal Society..
Pećinar I, Krstić ĐD, Caruso G, Popović-Đorđević J. Supplementary data for the article: Pećinar, Ilinka, Djurdja Krstić, Gianluca Caruso, and Jelena B. Popović-Djordjević. n.d. ‘Rapid Characterization of Hypanthium and Seed in Wild and Cultivated Rosehip: Application of Raman Microscopy Combined with Multivariate Analysis’. Royal Society Open Science 8 (3): 202064. https://doi.org/10.1098/rsos.202064.. Royal Society Open Science.
Pećinar Ilinka, Krstić Đurđa D., Caruso Gianluca, Popović-Đorđević Jelena, "Supplementary data for the article: Pećinar, Ilinka, Djurdja Krstić, Gianluca Caruso, and Jelena B. Popović-Djordjević. n.d. ‘Rapid Characterization of Hypanthium and Seed in Wild and Cultivated Rosehip: Application of Raman Microscopy Combined with Multivariate Analysis’. Royal Society Open Science 8 (3): 202064. https://doi.org/10.1098/rsos.202064." Royal Society Open Science

Rapid characterization of hypanthium and seed in wild and cultivated rosehip: application of Raman microscopy combined with multivariate analysis

Pećinar, Ilinka; Krstić, Đurđa D.; Caruso, Gianluca; Popović-Đorđević, Jelena

TY  - JOUR
AU  - Pećinar, Ilinka
AU  - Krstić, Đurđa D.
AU  - Caruso, Gianluca
AU  - Popović-Đorđević, Jelena
UR  - https://royalsocietypublishing.org/doi/10.1098/rsos.202064
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4460
AB  - Rosehip (pseudo-fruit) of dog rose (Rosa canina L.) is highly valued, and owing to nutritional and sensory properties it has a significant place in the food industry. This work represents an innovative report focusing on the evaluation of the phytochemical composition of rosehips (hypanthium and seed) grown in different locations in Serbia, using Raman microspectroscopy combined with multivariate data analysis. Some significant differences arose between the analysed rosehip samples with regard to the chemical profile of both hypanthium parenchyma cells and seed, although no evident discrimination was recorded between the samples of wild and cultivated rosehip. The differences between the hypanthium samples compared were mainly determined by the content of carotenoids, phenolic compounds and polysaccharides, whereas phenolics, polysaccharides (pectin, cellulose and hemicellulose) and lipids (to a lower extent) contributed to the seed sample discrimination. The differences observed between the rosehip samples may be attributed to abiotic factors (growing, ripening and storage conditions), which had a significant impact on the carotenoid and polyphenols biosynthesis.
PB  - The Royal Society
T2  - Royal Society Open Science
T1  - Rapid characterization of hypanthium and seed in wild and cultivated rosehip: application of Raman microscopy combined with multivariate analysis
VL  - 8
IS  - 3
SP  - 202064
DO  - 10.1098/rsos.202064
ER  - 
@article{
author = "Pećinar, Ilinka and Krstić, Đurđa D. and Caruso, Gianluca and Popović-Đorđević, Jelena",
url = "https://royalsocietypublishing.org/doi/10.1098/rsos.202064, http://cherry.chem.bg.ac.rs/handle/123456789/4460",
abstract = "Rosehip (pseudo-fruit) of dog rose (Rosa canina L.) is highly valued, and owing to nutritional and sensory properties it has a significant place in the food industry. This work represents an innovative report focusing on the evaluation of the phytochemical composition of rosehips (hypanthium and seed) grown in different locations in Serbia, using Raman microspectroscopy combined with multivariate data analysis. Some significant differences arose between the analysed rosehip samples with regard to the chemical profile of both hypanthium parenchyma cells and seed, although no evident discrimination was recorded between the samples of wild and cultivated rosehip. The differences between the hypanthium samples compared were mainly determined by the content of carotenoids, phenolic compounds and polysaccharides, whereas phenolics, polysaccharides (pectin, cellulose and hemicellulose) and lipids (to a lower extent) contributed to the seed sample discrimination. The differences observed between the rosehip samples may be attributed to abiotic factors (growing, ripening and storage conditions), which had a significant impact on the carotenoid and polyphenols biosynthesis.",
publisher = "The Royal Society",
journal = "Royal Society Open Science",
title = "Rapid characterization of hypanthium and seed in wild and cultivated rosehip: application of Raman microscopy combined with multivariate analysis",
volume = "8",
number = "3",
pages = "202064",
doi = "10.1098/rsos.202064"
}
Pećinar, I., Krstić, Đ. D., Caruso, G.,& Popović-Đorđević, J.Rapid characterization of hypanthium and seed in wild and cultivated rosehip: application of Raman microscopy combined with multivariate analysis.
Royal Society Open Science
The Royal Society., 8(3), 202064.
https://doi.org/10.1098/rsos.202064
Pećinar I, Krstić ĐD, Caruso G, Popović-Đorđević J. Rapid characterization of hypanthium and seed in wild and cultivated rosehip: application of Raman microscopy combined with multivariate analysis. Royal Society Open Science.8(3):202064
Pećinar Ilinka, Krstić Đurđa D., Caruso Gianluca, Popović-Đorđević Jelena, "Rapid characterization of hypanthium and seed in wild and cultivated rosehip: application of Raman microscopy combined with multivariate analysis" Royal Society Open Science, 8, no. 3:202064,
https://doi.org/10.1098/rsos.202064 .
1
1

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

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

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

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

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

TY  - JOUR
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4446
AB  - Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.
PB  - Blackwell Publishing Ltd
T2  - Allergy
T2  - Allergy
T1  - Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome
DO  - 10.1111/all.14889
ER  - 
@article{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
url = "https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889, http://cherry.chem.bg.ac.rs/handle/123456789/4446",
abstract = "Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.",
publisher = "Blackwell Publishing Ltd",
journal = "Allergy, Allergy",
title = "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome",
doi = "10.1111/all.14889"
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome.
Allergy
Blackwell Publishing Ltd..
https://doi.org/10.1111/all.14889
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. Allergy.
Peruško Marija, Apostolović Danijela, Kiewiet Mensiena Berentje Geertje, Grundström Jeanette, Hamsten Carl, Starkhammar Maria, Ćirković-Veličković Tanja, Hage Marianne van, "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome" Allergy,
https://doi.org/10.1111/all.14889 .
4

Polyphenol profile of buckwheat honey, nectar and pollen

Nešović, Milica; Gašić, Uroš M.; Tosti, Tomislav; Horvacki, Nikola; Šikoparija, Branko; Nedić, Nebojša; Blagojević, Stevan; Ignjatović, Ljubiša; Tešić, Živoslav Lj.

TY  - JOUR
AU  - Nešović, Milica
AU  - Gašić, Uroš M.
AU  - Tosti, Tomislav
AU  - Horvacki, Nikola
AU  - Šikoparija, Branko
AU  - Nedić, Nebojša
AU  - Blagojević, Stevan
AU  - Ignjatović, Ljubiša
AU  - Tešić, Živoslav Lj.
UR  - https://royalsocietypublishing.org/doi/10.1098/rsos.201576
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4451
AB  - A focus of research in recent years is the comparison of honey as the final product of bees with pollen and nectar of the plant from which the honey originates, as the main food source for bees. Buckwheat honey is recognized as a nutritionally valuable product, which provides a scientifically proven health benefit and is confirmed as a functional food. The quality of this type of honey is attributed to high levels of phytochemicals in buckwheat. The purpose of this study was the examination of similarity between buckwheat honey and buckwheat nectar and pollen, as well as simultaneous investigation of their chemical profiles and the origin of the honey. The phenolic profile of buckwheat pollen showed a lower number of flavonoids and phenolic acids than those of nectar and honey samples, but confirmed the presence of the most characteristic polyphenols derived from the buckwheat plant. The notable difference was found to be the presence of (epi)catechin units, its galloylated derivatives and procyanidin dimers, which were not present in honey. Honey polyphenols displayed a pronounced correlation with those of nectar, but not with those of pollen. Finally, by comparing the polyphenolic profiles of honey, nectar and pollen sharing the same geographical origin, new data could be provided for a potential assessment of the botanical origin of buckwheat honey.
PB  - The Royal Society
T2  - Royal Society Open Science
T1  - Polyphenol profile of buckwheat honey, nectar and pollen
VL  - 7
IS  - 12
SP  - 201576
DO  - 10.1098/rsos.201576
ER  - 
@article{
author = "Nešović, Milica and Gašić, Uroš M. and Tosti, Tomislav and Horvacki, Nikola and Šikoparija, Branko and Nedić, Nebojša and Blagojević, Stevan and Ignjatović, Ljubiša and Tešić, Živoslav Lj.",
url = "https://royalsocietypublishing.org/doi/10.1098/rsos.201576, http://cherry.chem.bg.ac.rs/handle/123456789/4451",
abstract = "A focus of research in recent years is the comparison of honey as the final product of bees with pollen and nectar of the plant from which the honey originates, as the main food source for bees. Buckwheat honey is recognized as a nutritionally valuable product, which provides a scientifically proven health benefit and is confirmed as a functional food. The quality of this type of honey is attributed to high levels of phytochemicals in buckwheat. The purpose of this study was the examination of similarity between buckwheat honey and buckwheat nectar and pollen, as well as simultaneous investigation of their chemical profiles and the origin of the honey. The phenolic profile of buckwheat pollen showed a lower number of flavonoids and phenolic acids than those of nectar and honey samples, but confirmed the presence of the most characteristic polyphenols derived from the buckwheat plant. The notable difference was found to be the presence of (epi)catechin units, its galloylated derivatives and procyanidin dimers, which were not present in honey. Honey polyphenols displayed a pronounced correlation with those of nectar, but not with those of pollen. Finally, by comparing the polyphenolic profiles of honey, nectar and pollen sharing the same geographical origin, new data could be provided for a potential assessment of the botanical origin of buckwheat honey.",
publisher = "The Royal Society",
journal = "Royal Society Open Science",
title = "Polyphenol profile of buckwheat honey, nectar and pollen",
volume = "7",
number = "12",
pages = "201576",
doi = "10.1098/rsos.201576"
}
Nešović, M., Gašić, U. M., Tosti, T., Horvacki, N., Šikoparija, B., Nedić, N., Blagojević, S., Ignjatović, L.,& Tešić, Ž. Lj.Polyphenol profile of buckwheat honey, nectar and pollen.
Royal Society Open Science
The Royal Society., 7(12), 201576.
https://doi.org/10.1098/rsos.201576
Nešović M, Gašić UM, Tosti T, Horvacki N, Šikoparija B, Nedić N, Blagojević S, Ignjatović L, Tešić ŽL. Polyphenol profile of buckwheat honey, nectar and pollen. Royal Society Open Science.7(12):201576
Nešović Milica, Gašić Uroš M., Tosti Tomislav, Horvacki Nikola, Šikoparija Branko, Nedić Nebojša, Blagojević Stevan, Ignjatović Ljubiša, Tešić Živoslav Lj., "Polyphenol profile of buckwheat honey, nectar and pollen" Royal Society Open Science, 7, no. 12:201576,
https://doi.org/10.1098/rsos.201576 .
1

Supplementary data for article: Banjanac, T.; Dragićević, M.; Šiler, B.; Gašić, U.; Bohanec, B.; Nestorović Živković, J.; Trifunović, S.; Mišić, D. Chemodiversity of Two Closely Related Tetraploid Centaurium Species and Their Hexaploid Hybrid: Metabolomic Search for High-Resolution Taxonomic Classifiers. Phytochemistry 2017, 140, 27–44. https://doi.org/10.1016/j.phytochem.2017.04.005

Banjanac, Tijana; Dragičević, Milan; Šiler, Branislav; Gašić, Uroš M.; Bohanec, Borut; Nestorović Živković, Jasmina; Trifunović, Snežana S.; Mišić, Danijela

TY  - BOOK
AU  - Banjanac, Tijana
AU  - Dragičević, Milan
AU  - Šiler, Branislav
AU  - Gašić, Uroš M.
AU  - Bohanec, Borut
AU  - Nestorović Živković, Jasmina
AU  - Trifunović, Snežana S.
AU  - Mišić, Danijela
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3098
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Supplementary data for article: Banjanac, T.; Dragićević, M.; Šiler, B.; Gašić, U.; Bohanec, B.; Nestorović Živković, J.; Trifunović, S.; Mišić, D. Chemodiversity of Two Closely Related Tetraploid Centaurium Species and Their Hexaploid Hybrid: Metabolomic Search for High-Resolution Taxonomic Classifiers. Phytochemistry 2017, 140, 27–44. https://doi.org/10.1016/j.phytochem.2017.04.005
ER  - 
@book{
author = "Banjanac, Tijana and Dragičević, Milan and Šiler, Branislav and Gašić, Uroš M. and Bohanec, Borut and Nestorović Živković, Jasmina and Trifunović, Snežana S. and Mišić, Danijela",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3098",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Supplementary data for article: Banjanac, T.; Dragićević, M.; Šiler, B.; Gašić, U.; Bohanec, B.; Nestorović Živković, J.; Trifunović, S.; Mišić, D. Chemodiversity of Two Closely Related Tetraploid Centaurium Species and Their Hexaploid Hybrid: Metabolomic Search for High-Resolution Taxonomic Classifiers. Phytochemistry 2017, 140, 27–44. https://doi.org/10.1016/j.phytochem.2017.04.005"
}
Banjanac, T., Dragičević, M., Šiler, B., Gašić, U. M., Bohanec, B., Nestorović Živković, J., Trifunović, S. S.,& Mišić, D.Supplementary data for article: Banjanac, T.; Dragićević, M.; Šiler, B.; Gašić, U.; Bohanec, B.; Nestorović Živković, J.; Trifunović, S.; Mišić, D. Chemodiversity of Two Closely Related Tetraploid Centaurium Species and Their Hexaploid Hybrid: Metabolomic Search for High-Resolution Taxonomic Classifiers. Phytochemistry 2017, 140, 27–44. https://doi.org/10.1016/j.phytochem.2017.04.005.
Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford..
Banjanac T, Dragičević M, Šiler B, Gašić UM, Bohanec B, Nestorović Živković J, Trifunović SS, Mišić D. Supplementary data for article: Banjanac, T.; Dragićević, M.; Šiler, B.; Gašić, U.; Bohanec, B.; Nestorović Živković, J.; Trifunović, S.; Mišić, D. Chemodiversity of Two Closely Related Tetraploid Centaurium Species and Their Hexaploid Hybrid: Metabolomic Search for High-Resolution Taxonomic Classifiers. Phytochemistry 2017, 140, 27–44. https://doi.org/10.1016/j.phytochem.2017.04.005. Phytochemistry.
Banjanac Tijana, Dragičević Milan, Šiler Branislav, Gašić Uroš M., Bohanec Borut, Nestorović Živković Jasmina, Trifunović Snežana S., Mišić Danijela, "Supplementary data for article: Banjanac, T.; Dragićević, M.; Šiler, B.; Gašić, U.; Bohanec, B.; Nestorović Živković, J.; Trifunović, S.; Mišić, D. Chemodiversity of Two Closely Related Tetraploid Centaurium Species and Their Hexaploid Hybrid: Metabolomic Search for High-Resolution Taxonomic Classifiers. Phytochemistry 2017, 140, 27–44. https://doi.org/10.1016/j.phytochem.2017.04.005" Phytochemistry

Supplementary data for the article: Veljković, I. S.; Kretić, D. S.; Veljković, D. Ž. Geometrical and Energetic Characteristics of Se⋯Se Interactions in Crystal Structures of Organoselenium Molecules. CrystEngComm 2021, 23 (18), 3383–3390. https://doi.org/10.1039/D1CE00129A.

Veljković, Ivana S.; Kretić, Danijela S.; Veljković, Dušan Ž.

TY  - BOOK
AU  - Veljković, Ivana S.
AU  - Kretić, Danijela S.
AU  - Veljković, Dušan Ž.
UR  - https://pubs.rsc.org/en/content/articlelanding/2021/ce/d1ce00129a
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4431
PB  - The Royal Society of Chemistry
T2  - CrystEngComm
T2  - CrystEngCommCrystEngComm
T1  - Supplementary data for the article: Veljković, I. S.; Kretić, D. S.; Veljković, D. Ž. Geometrical and Energetic Characteristics of Se⋯Se Interactions in Crystal Structures of Organoselenium Molecules. CrystEngComm 2021, 23 (18), 3383–3390. https://doi.org/10.1039/D1CE00129A.
ER  - 
@book{
author = "Veljković, Ivana S. and Kretić, Danijela S. and Veljković, Dušan Ž.",
url = "https://pubs.rsc.org/en/content/articlelanding/2021/ce/d1ce00129a, http://cherry.chem.bg.ac.rs/handle/123456789/4431",
publisher = "The Royal Society of Chemistry",
journal = "CrystEngComm, CrystEngCommCrystEngComm",
title = "Supplementary data for the article: Veljković, I. S.; Kretić, D. S.; Veljković, D. Ž. Geometrical and Energetic Characteristics of Se⋯Se Interactions in Crystal Structures of Organoselenium Molecules. CrystEngComm 2021, 23 (18), 3383–3390. https://doi.org/10.1039/D1CE00129A."
}
Veljković, I. S., Kretić, D. S.,& Veljković, D. Ž.Supplementary data for the article: Veljković, I. S.; Kretić, D. S.; Veljković, D. Ž. Geometrical and Energetic Characteristics of Se⋯Se Interactions in Crystal Structures of Organoselenium Molecules. CrystEngComm 2021, 23 (18), 3383–3390. https://doi.org/10.1039/D1CE00129A..
CrystEngCommCrystEngComm
The Royal Society of Chemistry..
Veljković IS, Kretić DS, Veljković DŽ. Supplementary data for the article: Veljković, I. S.; Kretić, D. S.; Veljković, D. Ž. Geometrical and Energetic Characteristics of Se⋯Se Interactions in Crystal Structures of Organoselenium Molecules. CrystEngComm 2021, 23 (18), 3383–3390. https://doi.org/10.1039/D1CE00129A.. CrystEngCommCrystEngComm.
Veljković Ivana S., Kretić Danijela S., Veljković Dušan Ž., "Supplementary data for the article: Veljković, I. S.; Kretić, D. S.; Veljković, D. Ž. Geometrical and Energetic Characteristics of Se⋯Se Interactions in Crystal Structures of Organoselenium Molecules. CrystEngComm 2021, 23 (18), 3383–3390. https://doi.org/10.1039/D1CE00129A." CrystEngCommCrystEngComm

Supplementary data for article: Keškić, T.; Čobeljić, B.; Gruden, M.; Anđelković, K.; Pevec, A.; Turel, I.; Radanović, D.; Zlatar, M. What Is the Nature of Interactions of BF4–, NO3–, and ClO4– to Cu(II) Complexes with Girard’s T Hydrazine? When Can Binuclear Complexes Be Formed? Crystal Growth & Design 2019, 19 (8), 4810–4821. https://doi.org/10.1021/acs.cgd.9b00760

Keškić, Tanja; Čobeljić, Božidar; Gruden-Pavlović, Maja; Anđelković, Katarina K.; Pevec, Andrej; Turel, Iztok; Radanović, Dušanka D.; Zlatar, Matija

TY  - BOOK
AU  - Keškić, Tanja
AU  - Čobeljić, Božidar
AU  - Gruden-Pavlović, Maja
AU  - Anđelković, Katarina K.
AU  - Pevec, Andrej
AU  - Turel, Iztok
AU  - Radanović, Dušanka D.
AU  - Zlatar, Matija
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3680
PB  - ACS Publications
T2  - Crystal Growth & Design
T1  - Supplementary data for article: Keškić, T.; Čobeljić, B.; Gruden, M.; Anđelković, K.; Pevec, A.; Turel, I.; Radanović, D.; Zlatar, M. What Is the Nature of Interactions of BF4–, NO3–, and ClO4– to Cu(II) Complexes with Girard’s T Hydrazine? When Can Binuclear Complexes Be Formed? Crystal Growth & Design 2019, 19 (8), 4810–4821. https://doi.org/10.1021/acs.cgd.9b00760
ER  - 
@book{
author = "Keškić, Tanja and Čobeljić, Božidar and Gruden-Pavlović, Maja and Anđelković, Katarina K. and Pevec, Andrej and Turel, Iztok and Radanović, Dušanka D. and Zlatar, Matija",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3680",
publisher = "ACS Publications",
journal = "Crystal Growth & Design",
title = "Supplementary data for article: Keškić, T.; Čobeljić, B.; Gruden, M.; Anđelković, K.; Pevec, A.; Turel, I.; Radanović, D.; Zlatar, M. What Is the Nature of Interactions of BF4–, NO3–, and ClO4– to Cu(II) Complexes with Girard’s T Hydrazine? When Can Binuclear Complexes Be Formed? Crystal Growth & Design 2019, 19 (8), 4810–4821. https://doi.org/10.1021/acs.cgd.9b00760"
}
Keškić, T., Čobeljić, B., Gruden-Pavlović, M., Anđelković, K. K., Pevec, A., Turel, I., Radanović, D. D.,& Zlatar, M.Supplementary data for article: Keškić, T.; Čobeljić, B.; Gruden, M.; Anđelković, K.; Pevec, A.; Turel, I.; Radanović, D.; Zlatar, M. What Is the Nature of Interactions of BF4–, NO3–, and ClO4– to Cu(II) Complexes with Girard’s T Hydrazine? When Can Binuclear Complexes Be Formed? Crystal Growth & Design 2019, 19 (8), 4810–4821. https://doi.org/10.1021/acs.cgd.9b00760.
Crystal Growth & Design
ACS Publications..
Keškić T, Čobeljić B, Gruden-Pavlović M, Anđelković KK, Pevec A, Turel I, Radanović DD, Zlatar M. Supplementary data for article: Keškić, T.; Čobeljić, B.; Gruden, M.; Anđelković, K.; Pevec, A.; Turel, I.; Radanović, D.; Zlatar, M. What Is the Nature of Interactions of BF4–, NO3–, and ClO4– to Cu(II) Complexes with Girard’s T Hydrazine? When Can Binuclear Complexes Be Formed? Crystal Growth & Design 2019, 19 (8), 4810–4821. https://doi.org/10.1021/acs.cgd.9b00760. Crystal Growth & Design.
Keškić Tanja, Čobeljić Božidar, Gruden-Pavlović Maja, Anđelković Katarina K., Pevec Andrej, Turel Iztok, Radanović Dušanka D., Zlatar Matija, "Supplementary data for article: Keškić, T.; Čobeljić, B.; Gruden, M.; Anđelković, K.; Pevec, A.; Turel, I.; Radanović, D.; Zlatar, M. What Is the Nature of Interactions of BF4–, NO3–, and ClO4– to Cu(II) Complexes with Girard’s T Hydrazine? When Can Binuclear Complexes Be Formed? Crystal Growth & Design 2019, 19 (8), 4810–4821. https://doi.org/10.1021/acs.cgd.9b00760" Crystal Growth & Design
3

Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization

Popović, Nikolina; Stanišić, Marija; Ilić Đurđić, Karla; Prodanović, Olivera; Polović, Natalija; Prodanović, Radivoje

(Elsevier, 2021)

TY  - BOOK
AU  - Popović, Nikolina
AU  - Stanišić, Marija
AU  - Ilić Đurđić, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S235218642100047X
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4493
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4494
PB  - Elsevier
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization
ER  - 
@book{
author = "Popović, Nikolina and Stanišić, Marija and Ilić Đurđić, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S235218642100047X, http://cherry.chem.bg.ac.rs/handle/123456789/4493, http://cherry.chem.bg.ac.rs/handle/123456789/4494",
publisher = "Elsevier",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization"
}
Popović, N., Stanišić, M., Ilić Đurđić, K., Prodanović, O., Polović, N.,& Prodanović, R. (2021). Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization.
Environmental Technology & InnovationEnvironmental Technology & Innovation
Elsevier..
Popović N, Stanišić M, Ilić Đurđić K, Prodanović O, Polović N, Prodanović R. Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. Environmental Technology & InnovationEnvironmental Technology & Innovation. 2021;
Popović Nikolina, Stanišić Marija, Ilić Đurđić Karla, Prodanović Olivera, Polović Natalija, Prodanović Radivoje, "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization" Environmental Technology & InnovationEnvironmental Technology & Innovation (2021)

Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization

Popović, Nikolina; Stanišić, Marija; Ilić Đurđić, Karla; Prodanović, Olivera; Polović, Natalija; Prodanović, Radivoje

(Elsevier, 2021)

TY  - JOUR
AU  - Popović, Nikolina
AU  - Stanišić, Marija
AU  - Ilić Đurđić, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S235218642100047X
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4493
AB  - Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV–Vis,FTIR, and 1H NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.
PB  - Elsevier
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization
VL  - 22
SP  - 101399
DO  - 10.1016/j.eti.2021.101399
ER  - 
@article{
author = "Popović, Nikolina and Stanišić, Marija and Ilić Đurđić, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S235218642100047X, http://cherry.chem.bg.ac.rs/handle/123456789/4493",
abstract = "Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV–Vis,FTIR, and 1H NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.",
publisher = "Elsevier",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization",
volume = "22",
pages = "101399",
doi = "10.1016/j.eti.2021.101399"
}
Popović, N., Stanišić, M., Ilić Đurđić, K., Prodanović, O., Polović, N.,& Prodanović, R. (2021). Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization.
Environmental Technology & InnovationEnvironmental Technology & Innovation
Elsevier., 22, 101399.
https://doi.org/10.1016/j.eti.2021.101399
Popović N, Stanišić M, Ilić Đurđić K, Prodanović O, Polović N, Prodanović R. Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. Environmental Technology & InnovationEnvironmental Technology & Innovation. 2021;22:101399
Popović Nikolina, Stanišić Marija, Ilić Đurđić Karla, Prodanović Olivera, Polović Natalija, Prodanović Radivoje, "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization" Environmental Technology & InnovationEnvironmental Technology & Innovation, 22 (2021):101399,
https://doi.org/10.1016/j.eti.2021.101399 .
1

Supplementary data for the article: Bayram, N. E.; Gercek, Y. C.; Çelik, S.; Mayda, N.; Kostić, A. Ž.; Dramićanin, A. M.; Özkök, A. Phenolic and Free Amino Acid Profiles of Bee Bread and Bee Pollen with the Same Botanical Origin – Similarities and Differences. Arabian Journal of Chemistry 2021, 14 (3), 103004. https://doi.org/10.1016/j.arabjc.2021.103004.

Bayram, Nesrin Ecem; Gercek, Yusuf Can; Çelik, Saffet; Mayda, Nazlı; Kostić, Aleksandar Ž.; Dramićanin, Aleksandra M.; Özkök, Aslı

(Elsevier, 2021)

TY  - BOOK
AU  - Bayram, Nesrin Ecem
AU  - Gercek, Yusuf Can
AU  - Çelik, Saffet
AU  - Mayda, Nazlı
AU  - Kostić, Aleksandar Ž.
AU  - Dramićanin, Aleksandra M.
AU  - Özkök, Aslı
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4491
PB  - Elsevier
T2  - Arabian Journal of Chemistry
T1  - Supplementary data for the article: Bayram, N. E.; Gercek, Y. C.; Çelik, S.; Mayda, N.; Kostić, A. Ž.; Dramićanin, A. M.; Özkök, A. Phenolic and Free Amino Acid Profiles of Bee Bread and Bee Pollen with the Same Botanical Origin – Similarities and Differences. Arabian Journal of Chemistry 2021, 14 (3), 103004. https://doi.org/10.1016/j.arabjc.2021.103004.
ER  - 
@book{
author = "Bayram, Nesrin Ecem and Gercek, Yusuf Can and Çelik, Saffet and Mayda, Nazlı and Kostić, Aleksandar Ž. and Dramićanin, Aleksandra M. and Özkök, Aslı",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4491",
publisher = "Elsevier",
journal = "Arabian Journal of Chemistry",
title = "Supplementary data for the article: Bayram, N. E.; Gercek, Y. C.; Çelik, S.; Mayda, N.; Kostić, A. Ž.; Dramićanin, A. M.; Özkök, A. Phenolic and Free Amino Acid Profiles of Bee Bread and Bee Pollen with the Same Botanical Origin – Similarities and Differences. Arabian Journal of Chemistry 2021, 14 (3), 103004. https://doi.org/10.1016/j.arabjc.2021.103004."
}
Bayram, N. E., Gercek, Y. C., Çelik, S., Mayda, N., Kostić, A. Ž., Dramićanin, A. M.,& Özkök, A. (2021). Supplementary data for the article: Bayram, N. E.; Gercek, Y. C.; Çelik, S.; Mayda, N.; Kostić, A. Ž.; Dramićanin, A. M.; Özkök, A. Phenolic and Free Amino Acid Profiles of Bee Bread and Bee Pollen with the Same Botanical Origin – Similarities and Differences. Arabian Journal of Chemistry 2021, 14 (3), 103004. https://doi.org/10.1016/j.arabjc.2021.103004..
Arabian Journal of Chemistry
Elsevier..
Bayram NE, Gercek YC, Çelik S, Mayda N, Kostić AŽ, Dramićanin AM, Özkök A. Supplementary data for the article: Bayram, N. E.; Gercek, Y. C.; Çelik, S.; Mayda, N.; Kostić, A. Ž.; Dramićanin, A. M.; Özkök, A. Phenolic and Free Amino Acid Profiles of Bee Bread and Bee Pollen with the Same Botanical Origin – Similarities and Differences. Arabian Journal of Chemistry 2021, 14 (3), 103004. https://doi.org/10.1016/j.arabjc.2021.103004.. Arabian Journal of Chemistry. 2021;
Bayram Nesrin Ecem, Gercek Yusuf Can, Çelik Saffet, Mayda Nazlı, Kostić Aleksandar Ž., Dramićanin Aleksandra M., Özkök Aslı, "Supplementary data for the article: Bayram, N. E.; Gercek, Y. C.; Çelik, S.; Mayda, N.; Kostić, A. Ž.; Dramićanin, A. M.; Özkök, A. Phenolic and Free Amino Acid Profiles of Bee Bread and Bee Pollen with the Same Botanical Origin – Similarities and Differences. Arabian Journal of Chemistry 2021, 14 (3), 103004. https://doi.org/10.1016/j.arabjc.2021.103004." Arabian Journal of Chemistry (2021)

Phenolic and free amino acid profiles of bee bread and bee pollen with the same botanical origin – similarities and differences

Bayram, Nesrin Ecem; Gercek, Yusuf Can; Çelik, Saffet; Mayda, Nazlı; Kostić, Aleksandar Ž.; Dramićanin, Aleksandra M.; Özkök, Aslı

(2021)

TY  - JOUR
AU  - Bayram, Nesrin Ecem
AU  - Gercek, Yusuf Can
AU  - Çelik, Saffet
AU  - Mayda, Nazlı
AU  - Kostić, Aleksandar Ž.
AU  - Dramićanin, Aleksandra M.
AU  - Özkök, Aslı
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1878535221000198
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4491
AB  - In this study, the chemical profile of bee pollen (BP) and bee bread (BB) samples collected from the same beehive were analyzed by LC–MS/MS (liquid chromatography technique coupled with tandem mass spectrometry), providing the identification of 23 phenolic compounds and 42 free amino acids (FAAs). Rutin was the phenolic compound with the highest rate of occurrence in both BP and BB samples. However, concentrations of protocatechuic acid, 2,5-dihydroxybenzoic acid and kaempferol compounds were significantly higher in BB samples than in BP samples from the same hive probably as result of microbial activity and glycosides degradation. The obtained data revealed that the phenolic profiles of the samples differ not only by the type of a product but also by region. Among FAAs proline was the predominant compound in all the analyzed BP and BB samples followed by l-asparagine (BP samples) and l-aspartic acid (BP and BB samples). A high content of proline can be used as a parameter of sample freshness. Also, Principal Component Analysis (PCA) and Cluster analysis proved the possibility of using phlorizin as a chemotaxonomic marker for Rosaceae (Malus or Prunus genus) pollen presence in BP1 sample. In addition, amino acid profile had higher impact on BP and BB sample differentiation due to lower FAAs content in BB samples probably caused by microbial activity. To the best of our knowledge, this study is the first to compare the individual phenolic compounds and free amino acids of bee pollen and bee bread samples with the same botanical origin (predominantly originated from plants belonging to the following families: Asteraceae, Fabaceae, Plantaginaceae and Rosaceae).
T2  - Arabian Journal of Chemistry
T2  - Arabian Journal of Chemistry
T1  - Phenolic and free amino acid profiles of bee bread and bee pollen with the same botanical origin – similarities and differences
VL  - 14
IS  - 3
SP  - 103004
DO  - 10.1016/j.arabjc.2021.103004
ER  - 
@article{
author = "Bayram, Nesrin Ecem and Gercek, Yusuf Can and Çelik, Saffet and Mayda, Nazlı and Kostić, Aleksandar Ž. and Dramićanin, Aleksandra M. and Özkök, Aslı",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S1878535221000198, http://cherry.chem.bg.ac.rs/handle/123456789/4491",
abstract = "In this study, the chemical profile of bee pollen (BP) and bee bread (BB) samples collected from the same beehive were analyzed by LC–MS/MS (liquid chromatography technique coupled with tandem mass spectrometry), providing the identification of 23 phenolic compounds and 42 free amino acids (FAAs). Rutin was the phenolic compound with the highest rate of occurrence in both BP and BB samples. However, concentrations of protocatechuic acid, 2,5-dihydroxybenzoic acid and kaempferol compounds were significantly higher in BB samples than in BP samples from the same hive probably as result of microbial activity and glycosides degradation. The obtained data revealed that the phenolic profiles of the samples differ not only by the type of a product but also by region. Among FAAs proline was the predominant compound in all the analyzed BP and BB samples followed by l-asparagine (BP samples) and l-aspartic acid (BP and BB samples). A high content of proline can be used as a parameter of sample freshness. Also, Principal Component Analysis (PCA) and Cluster analysis proved the possibility of using phlorizin as a chemotaxonomic marker for Rosaceae (Malus or Prunus genus) pollen presence in BP1 sample. In addition, amino acid profile had higher impact on BP and BB sample differentiation due to lower FAAs content in BB samples probably caused by microbial activity. To the best of our knowledge, this study is the first to compare the individual phenolic compounds and free amino acids of bee pollen and bee bread samples with the same botanical origin (predominantly originated from plants belonging to the following families: Asteraceae, Fabaceae, Plantaginaceae and Rosaceae).",
journal = "Arabian Journal of Chemistry, Arabian Journal of Chemistry",
title = "Phenolic and free amino acid profiles of bee bread and bee pollen with the same botanical origin – similarities and differences",
volume = "14",
number = "3",
pages = "103004",
doi = "10.1016/j.arabjc.2021.103004"
}
Bayram, N. E., Gercek, Y. C., Çelik, S., Mayda, N., Kostić, A. Ž., Dramićanin, A. M.,& Özkök, A. (2021). Phenolic and free amino acid profiles of bee bread and bee pollen with the same botanical origin – similarities and differences.
Arabian Journal of Chemistry, 14(3), 103004.
https://doi.org/10.1016/j.arabjc.2021.103004
Bayram NE, Gercek YC, Çelik S, Mayda N, Kostić AŽ, Dramićanin AM, Özkök A. Phenolic and free amino acid profiles of bee bread and bee pollen with the same botanical origin – similarities and differences. Arabian Journal of Chemistry. 2021;14(3):103004
Bayram Nesrin Ecem, Gercek Yusuf Can, Çelik Saffet, Mayda Nazlı, Kostić Aleksandar Ž., Dramićanin Aleksandra M., Özkök Aslı, "Phenolic and free amino acid profiles of bee bread and bee pollen with the same botanical origin – similarities and differences" Arabian Journal of Chemistry, 14, no. 3 (2021):103004,
https://doi.org/10.1016/j.arabjc.2021.103004 .
4

MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation

Milovanović, Vladimir; Minić, Rajna; Vakić, Jelena; Ivanović, Saša; Čupić, Vitomir; Borozan, Sunćica; Nešić, Andrijana; Živković, Irena

(Elsevier, 2021)

TY  - JOUR
AU  - Milovanović, Vladimir
AU  - Minić, Rajna
AU  - Vakić, Jelena
AU  - Ivanović, Saša
AU  - Čupić, Vitomir
AU  - Borozan, Sunćica
AU  - Nešić, Andrijana
AU  - Živković, Irena
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0041010121000362
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4490
AB  - The MTT assay is routinely used to detect the activity of living cells. While working with Vipera ammodytes venom we detected the reduction of MTT without the presence of cells, in a concentration-dependent manner. By combining non-reducing PAGE, L-amino acid oxidase (LAAO) assays, and standard MTT assays, we established and confirmed that venom MTT reduction is catalyzed by only one enzyme, the LAAO. Even though it was previously known that the dimeric and tetrameric forms of LAAO are active, we conclude that the enzyme is also active in the monomeric form. Our results have led to the definition of a new MTT assay in a microtiter plate for in vitro testing of svLAAO activity i.e. from the venom of the V. ammodytes snake. Potentially, this method can be used for testing hemorrhagic venoms of other snakes as well as the LAAO neutralization capability of appropriate antivenoms.
PB  - Elsevier
T2  - Toxicon
T2  - ToxiconToxicon
T1  - MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation
VL  - 192
SP  - 57
EP  - 65
DO  - 10.1016/j.toxicon.2021.01.012
ER  - 
@article{
author = "Milovanović, Vladimir and Minić, Rajna and Vakić, Jelena and Ivanović, Saša and Čupić, Vitomir and Borozan, Sunćica and Nešić, Andrijana and Živković, Irena",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S0041010121000362, http://cherry.chem.bg.ac.rs/handle/123456789/4490",
abstract = "The MTT assay is routinely used to detect the activity of living cells. While working with Vipera ammodytes venom we detected the reduction of MTT without the presence of cells, in a concentration-dependent manner. By combining non-reducing PAGE, L-amino acid oxidase (LAAO) assays, and standard MTT assays, we established and confirmed that venom MTT reduction is catalyzed by only one enzyme, the LAAO. Even though it was previously known that the dimeric and tetrameric forms of LAAO are active, we conclude that the enzyme is also active in the monomeric form. Our results have led to the definition of a new MTT assay in a microtiter plate for in vitro testing of svLAAO activity i.e. from the venom of the V. ammodytes snake. Potentially, this method can be used for testing hemorrhagic venoms of other snakes as well as the LAAO neutralization capability of appropriate antivenoms.",
publisher = "Elsevier",
journal = "Toxicon, ToxiconToxicon",
title = "MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation",
volume = "192",
pages = "57-65",
doi = "10.1016/j.toxicon.2021.01.012"
}
Milovanović, V., Minić, R., Vakić, J., Ivanović, S., Čupić, V., Borozan, S., Nešić, A.,& Živković, I. (2021). MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation.
ToxiconToxicon
Elsevier., 192, 57-65.
https://doi.org/10.1016/j.toxicon.2021.01.012
Milovanović V, Minić R, Vakić J, Ivanović S, Čupić V, Borozan S, Nešić A, Živković I. MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation. ToxiconToxicon. 2021;192:57-65
Milovanović Vladimir, Minić Rajna, Vakić Jelena, Ivanović Saša, Čupić Vitomir, Borozan Sunćica, Nešić Andrijana, Živković Irena, "MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation" ToxiconToxicon, 192 (2021):57-65,
https://doi.org/10.1016/j.toxicon.2021.01.012 .
1

BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms

Lopandić, Zorana; Dragačević, Luka; Popović, Dragan; Anđelković, Uroš; Minić, Rajna; Gavrović-Jankulović, Marija

(MDPI, 2021)

TY  - JOUR
AU  - Lopandić, Zorana
AU  - Dragačević, Luka
AU  - Popović, Dragan
AU  - Anđelković, Uroš
AU  - Minić, Rajna
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - https://www.mdpi.com/2218-273X/11/2/180
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4489
AB  - Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.
PB  - MDPI
T2  - Biomolecules
T2  - Biomolecules
T1  - BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms
VL  - 11
IS  - 2
SP  - 180
DO  - 10.3390/biom11020180
ER  - 
@article{
author = "Lopandić, Zorana and Dragačević, Luka and Popović, Dragan and Anđelković, Uroš and Minić, Rajna and Gavrović-Jankulović, Marija",
year = "2021",
url = "https://www.mdpi.com/2218-273X/11/2/180, http://cherry.chem.bg.ac.rs/handle/123456789/4489",
abstract = "Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms.",
publisher = "MDPI",
journal = "Biomolecules, Biomolecules",
title = "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms",
volume = "11",
number = "2",
pages = "180",
doi = "10.3390/biom11020180"
}
Lopandić, Z., Dragačević, L., Popović, D., Anđelković, U., Minić, R.,& Gavrović-Jankulović, M. (2021). BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms.
Biomolecules
MDPI., 11(2), 180.
https://doi.org/10.3390/biom11020180
Lopandić Z, Dragačević L, Popović D, Anđelković U, Minić R, Gavrović-Jankulović M. BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. Biomolecules. 2021;11(2):180
Lopandić Zorana, Dragačević Luka, Popović Dragan, Anđelković Uroš, Minić Rajna, Gavrović-Jankulović Marija, "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms" Biomolecules, 11, no. 2 (2021):180,
https://doi.org/10.3390/biom11020180 .

Supplementary data for the article: Natić, M.; Dabić Zagorac, D.; Gašić, U.; Dojčinović, B.; Ćirić, I.; Relić, D.; Todić, S.; Sredojević, M. Autochthonous and International Grape Varieties Grown in Serbia - Phenolic and Elemental Composition. Food Bioscience 2021, 40, 100889. https://doi.org/10.1016/j.fbio.2021.100889.

Natić, Maja; Dabić Zagorac, Dragana; Gašić, Uroš; Dojčinović, Biljana; Ćirić, Ivanka; Relić, Dubravka; Todić, Slavica; Sredojević, Milica

(Elsevier, 2021)

TY  - BOOK
AU  - Natić, Maja
AU  - Dabić Zagorac, Dragana
AU  - Gašić, Uroš
AU  - Dojčinović, Biljana
AU  - Ćirić, Ivanka
AU  - Relić, Dubravka
AU  - Todić, Slavica
AU  - Sredojević, Milica
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4487
UR  - https://www.sciencedirect.com/science/article/pii/S2212429221000146
PB  - Elsevier
T2  - Food Bioscience
T2  - Food BioscienceFood Bioscience
T1  - Supplementary data for the article: Natić, M.; Dabić Zagorac, D.; Gašić, U.; Dojčinović, B.; Ćirić, I.; Relić, D.; Todić, S.; Sredojević, M. Autochthonous and International Grape Varieties Grown in Serbia - Phenolic and Elemental Composition. Food Bioscience 2021, 40, 100889. https://doi.org/10.1016/j.fbio.2021.100889.
ER  - 
@book{
author = "Natić, Maja and Dabić Zagorac, Dragana and Gašić, Uroš and Dojčinović, Biljana and Ćirić, Ivanka and Relić, Dubravka and Todić, Slavica and Sredojević, Milica",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4487, https://www.sciencedirect.com/science/article/pii/S2212429221000146",
publisher = "Elsevier",
journal = "Food Bioscience, Food BioscienceFood Bioscience",
title = "Supplementary data for the article: Natić, M.; Dabić Zagorac, D.; Gašić, U.; Dojčinović, B.; Ćirić, I.; Relić, D.; Todić, S.; Sredojević, M. Autochthonous and International Grape Varieties Grown in Serbia - Phenolic and Elemental Composition. Food Bioscience 2021, 40, 100889. https://doi.org/10.1016/j.fbio.2021.100889."
}
Natić, M., Dabić Zagorac, D., Gašić, U., Dojčinović, B., Ćirić, I., Relić, D., Todić, S.,& Sredojević, M. (2021). Supplementary data for the article: Natić, M.; Dabić Zagorac, D.; Gašić, U.; Dojčinović, B.; Ćirić, I.; Relić, D.; Todić, S.; Sredojević, M. Autochthonous and International Grape Varieties Grown in Serbia - Phenolic and Elemental Composition. Food Bioscience 2021, 40, 100889. https://doi.org/10.1016/j.fbio.2021.100889..
Food BioscienceFood Bioscience
Elsevier..
Natić M, Dabić Zagorac D, Gašić U, Dojčinović B, Ćirić I, Relić D, Todić S, Sredojević M. Supplementary data for the article: Natić, M.; Dabić Zagorac, D.; Gašić, U.; Dojčinović, B.; Ćirić, I.; Relić, D.; Todić, S.; Sredojević, M. Autochthonous and International Grape Varieties Grown in Serbia - Phenolic and Elemental Composition. Food Bioscience 2021, 40, 100889. https://doi.org/10.1016/j.fbio.2021.100889.. Food BioscienceFood Bioscience. 2021;
Natić Maja, Dabić Zagorac Dragana, Gašić Uroš, Dojčinović Biljana, Ćirić Ivanka, Relić Dubravka, Todić Slavica, Sredojević Milica, "Supplementary data for the article: Natić, M.; Dabić Zagorac, D.; Gašić, U.; Dojčinović, B.; Ćirić, I.; Relić, D.; Todić, S.; Sredojević, M. Autochthonous and International Grape Varieties Grown in Serbia - Phenolic and Elemental Composition. Food Bioscience 2021, 40, 100889. https://doi.org/10.1016/j.fbio.2021.100889." Food BioscienceFood Bioscience (2021)

Autochthonous and international grape varieties grown in Serbia - Phenolic and elemental composition

Natić, Maja; Dabić Zagorac, Dragana; Gašić, Uroš; Dojčinović, Biljana; Ćirić, Ivanka; Relić, Dubravka; Todić, Slavica; Sredojević, Milica

(Elsevier, 2021)

TY  - JOUR
AU  - Natić, Maja
AU  - Dabić Zagorac, Dragana
AU  - Gašić, Uroš
AU  - Dojčinović, Biljana
AU  - Ćirić, Ivanka
AU  - Relić, Dubravka
AU  - Todić, Slavica
AU  - Sredojević, Milica
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S2212429221000146
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4487
AB  - The phenolic and elemental profiles of Serbian autochthonous grape varieties ‘Smederevka’ and ‘Plovdina’ were studied and compared with some international varieties. Total phenolic content and radical scavenging activity were highest in seeds of ‘Plovdina’, and in ‘Smederevka’ skins, which also had the highest contents of ferulic, chlorogenic and caffeic acids (16.0, 1.44 and 0.98 mg/kg, respectively). Protocatechuic acid was quantified only in the seeds of these varieties. Untypically for Vitis vinifera L. species, the presence of malvidin 3,5-O-dihexoside was found in the skins of ‘Vranac’ and ‘Muscat Hamburg’. In ‘Plovdina’ skins among the anthocyanins, hexosides of peonidin and delphinidin were prevalent. ‘Plovdina’ grapes had lower quantities of Al, Ni and Na in comparison to the other varieties intended for white wine production. Significant correlations among the most abundant elements, such as K, P, Ca, Mg, S, Fe, Cu, and Zn, pointed to potential positive interactions. For elements that have toxicological reference values, the health risk assessment was calculated for adults and children, and suggested that all samples were safe for human consumption.
PB  - Elsevier
T2  - Food Bioscience
T2  - Food BioscienceFood Bioscience
T1  - Autochthonous and international grape varieties grown in Serbia - Phenolic and elemental composition
VL  - 40
SP  - 100889
DO  - 10.1016/j.fbio.2021.100889
ER  - 
@article{
author = "Natić, Maja and Dabić Zagorac, Dragana and Gašić, Uroš and Dojčinović, Biljana and Ćirić, Ivanka and Relić, Dubravka and Todić, Slavica and Sredojević, Milica",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S2212429221000146, http://cherry.chem.bg.ac.rs/handle/123456789/4487",
abstract = "The phenolic and elemental profiles of Serbian autochthonous grape varieties ‘Smederevka’ and ‘Plovdina’ were studied and compared with some international varieties. Total phenolic content and radical scavenging activity were highest in seeds of ‘Plovdina’, and in ‘Smederevka’ skins, which also had the highest contents of ferulic, chlorogenic and caffeic acids (16.0, 1.44 and 0.98 mg/kg, respectively). Protocatechuic acid was quantified only in the seeds of these varieties. Untypically for Vitis vinifera L. species, the presence of malvidin 3,5-O-dihexoside was found in the skins of ‘Vranac’ and ‘Muscat Hamburg’. In ‘Plovdina’ skins among the anthocyanins, hexosides of peonidin and delphinidin were prevalent. ‘Plovdina’ grapes had lower quantities of Al, Ni and Na in comparison to the other varieties intended for white wine production. Significant correlations among the most abundant elements, such as K, P, Ca, Mg, S, Fe, Cu, and Zn, pointed to potential positive interactions. For elements that have toxicological reference values, the health risk assessment was calculated for adults and children, and suggested that all samples were safe for human consumption.",
publisher = "Elsevier",
journal = "Food Bioscience, Food BioscienceFood Bioscience",
title = "Autochthonous and international grape varieties grown in Serbia - Phenolic and elemental composition",
volume = "40",
pages = "100889",
doi = "10.1016/j.fbio.2021.100889"
}
Natić, M., Dabić Zagorac, D., Gašić, U., Dojčinović, B., Ćirić, I., Relić, D., Todić, S.,& Sredojević, M. (2021). Autochthonous and international grape varieties grown in Serbia - Phenolic and elemental composition.
Food BioscienceFood Bioscience
Elsevier., 40, 100889.
https://doi.org/10.1016/j.fbio.2021.100889
Natić M, Dabić Zagorac D, Gašić U, Dojčinović B, Ćirić I, Relić D, Todić S, Sredojević M. Autochthonous and international grape varieties grown in Serbia - Phenolic and elemental composition. Food BioscienceFood Bioscience. 2021;40:100889
Natić Maja, Dabić Zagorac Dragana, Gašić Uroš, Dojčinović Biljana, Ćirić Ivanka, Relić Dubravka, Todić Slavica, Sredojević Milica, "Autochthonous and international grape varieties grown in Serbia - Phenolic and elemental composition" Food BioscienceFood Bioscience, 40 (2021):100889,
https://doi.org/10.1016/j.fbio.2021.100889 .

Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity

Gligorijević, Nikola; Minić, Simeon; Radibratović, Milica; Papadimitriou, Vassiliki; Nedić, Olgica; Sotiroudis, Theodore G.; Nikolić, Milan R.

(Elsevier, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Radibratović, Milica
AU  - Papadimitriou, Vassiliki
AU  - Nedić, Olgica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan R.
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1386142521000597
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4486
AB  - Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.
PB  - Elsevier
T2  - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
T2  - Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
T1  - Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity
VL  - 251
SP  - 119483
DO  - 10.1016/j.saa.2021.119483
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon and Radibratović, Milica and Papadimitriou, Vassiliki and Nedić, Olgica and Sotiroudis, Theodore G. and Nikolić, Milan R.",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S1386142521000597, http://cherry.chem.bg.ac.rs/handle/123456789/4486",
abstract = "Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.",
publisher = "Elsevier",
journal = "Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy",
title = "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity",
volume = "251",
pages = "119483",
doi = "10.1016/j.saa.2021.119483"
}
Gligorijević, N., Minić, S., Radibratović, M., Papadimitriou, V., Nedić, O., Sotiroudis, T. G.,& Nikolić, M. R. (2021). Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity.
Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Elsevier., 251, 119483.
https://doi.org/10.1016/j.saa.2021.119483
Gligorijević N, Minić S, Radibratović M, Papadimitriou V, Nedić O, Sotiroudis TG, Nikolić MR. Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2021;251:119483
Gligorijević Nikola, Minić Simeon, Radibratović Milica, Papadimitriou Vassiliki, Nedić Olgica, Sotiroudis Theodore G., Nikolić Milan R., "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity" Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 251 (2021):119483,
https://doi.org/10.1016/j.saa.2021.119483 .
1

Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls

Ilić Đurđić, Karla; Ostafe, Raluca; Prodanović, Olivera; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Fischer, Rainer; Schillberg, Stefan; Prodanović, Radivoje

(Springer, 2021)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4101
AB  - The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) from Phanerochaete chrysosporium is a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 104 independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.
PB  - Springer
T2  - Frontiers of Environmental Science & Engineering
T2  - Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
T1  - Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls
VL  - 15
IS  - 2
SP  - 19
DO  - 10.1007/s11783-020-1311-4
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Prodanović, Olivera and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4101",
abstract = "The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) from Phanerochaete chrysosporium is a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 104 independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.",
publisher = "Springer",
journal = "Frontiers of Environmental Science & Engineering, Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.",
title = "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls",
volume = "15",
number = "2",
pages = "19",
doi = "10.1007/s11783-020-1311-4"
}
Ilić Đurđić, K., Ostafe, R., Prodanović, O., Đurđević Đelmaš, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R. (2021). Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls.
Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
Springer., 15(2), 19.
https://doi.org/10.1007/s11783-020-1311-4
Ilić Đurđić K, Ostafe R, Prodanović O, Đurđević Đelmaš A, Popović N, Fischer R, Schillberg S, Prodanović R. Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.. 2021;15(2):19
Ilić Đurđić Karla, Ostafe Raluca, Prodanović Olivera, Đurđević Đelmaš Aleksandra, Popović Nikolina, Fischer Rainer, Schillberg Stefan, Prodanović Radivoje, "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls" Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng., 15, no. 2 (2021):19,
https://doi.org/10.1007/s11783-020-1311-4 .
4
3

Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4

Ilić Đurđić, Karla; Ostafe, Raluca; Prodanović, Olivera; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Fischer, Rainer; Schillberg, Stefan; Prodanović, Radivoje

(Springer, 2021)

TY  - BOOK
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4103
PB  - Springer
T2  - Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
T1  - Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4
ER  - 
@book{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Prodanović, Olivera and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4103",
publisher = "Springer",
journal = "Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.",
title = "Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4"
}
Ilić Đurđić, K., Ostafe, R., Prodanović, O., Đurđević Đelmaš, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R. (2021). Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4.
Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
Springer..
Ilić Đurđić K, Ostafe R, Prodanović O, Đurđević Đelmaš A, Popović N, Fischer R, Schillberg S, Prodanović R. Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4. Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.. 2021;
Ilić Đurđić Karla, Ostafe Raluca, Prodanović Olivera, Đurđević Đelmaš Aleksandra, Popović Nikolina, Fischer Rainer, Schillberg Stefan, Prodanović Radivoje, "Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4" Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng. (2021)

Imobilizacija ćelijskih zidova lakazom u kalcijum L do pa alginatnim kuglicama, uz dodatno fotoumrežavanje, u cilju povećanja temperaturne stabilnosti imobilizata

Janjić, Dajana

(2021)

TY  - BOOK
AU  - Janjić, Dajana
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4341
AB  - Cilj ovog rada je bio ekspresija lakaze na površini ćelija Saccharomyces cerevisiae liziranje
dobijenih ćelija organskim rastvaračem sa ciljem povećanja specifične en zimske aktivnosti i njihova
imobilizacija . Imobilizacija je vršena u kuglicama L dopa alginata, sintetisanog u reakcijama
perjodatne okcidacije, a zatim i reduktivne aminacije sa L hidroksifenilalaninom (L dopom). Dobijeni
derivat alginata je okarakterisan UV Vis spektroskopijom i korišćen za imobilizaciju enzima. Dobijene
kuglice sa lakazom na ćelijskim zidovima su pored jonskog umrežavanja kalcijumom dodatno
fotoumrežavane kovalentno sa eozinom Y, u prisustvu led zelenog svetla. Upoređena je specifična
ak tivnost enzima u kuglicama bez dodatnog fotoumreženja i sa fotoumreženjem, kao i temperaturna
stabilnost ovih imobilizata.
T1  - Imobilizacija ćelijskih zidova lakazom u kalcijum L do pa alginatnim kuglicama, uz dodatno fotoumrežavanje, u cilju povećanja temperaturne stabilnosti imobilizata
SP  - 1
EP  - 66
ER  - 
@mastersthesis{
author = "Janjić, Dajana",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4341",
abstract = "Cilj ovog rada je bio ekspresija lakaze na površini ćelija Saccharomyces cerevisiae liziranje
dobijenih ćelija organskim rastvaračem sa ciljem povećanja specifične en zimske aktivnosti i njihova
imobilizacija . Imobilizacija je vršena u kuglicama L dopa alginata, sintetisanog u reakcijama
perjodatne okcidacije, a zatim i reduktivne aminacije sa L hidroksifenilalaninom (L dopom). Dobijeni
derivat alginata je okarakterisan UV Vis spektroskopijom i korišćen za imobilizaciju enzima. Dobijene
kuglice sa lakazom na ćelijskim zidovima su pored jonskog umrežavanja kalcijumom dodatno
fotoumrežavane kovalentno sa eozinom Y, u prisustvu led zelenog svetla. Upoređena je specifična
ak tivnost enzima u kuglicama bez dodatnog fotoumreženja i sa fotoumreženjem, kao i temperaturna
stabilnost ovih imobilizata.",
title = "Imobilizacija ćelijskih zidova lakazom u kalcijum L do pa alginatnim kuglicama, uz dodatno fotoumrežavanje, u cilju povećanja temperaturne stabilnosti imobilizata",
pages = "1-66"
}
Janjić, D. (2021). Imobilizacija ćelijskih zidova lakazom u kalcijum L do pa alginatnim kuglicama, uz dodatno fotoumrežavanje, u cilju povećanja temperaturne stabilnosti imobilizata.
, 1-66.
Janjić D. Imobilizacija ćelijskih zidova lakazom u kalcijum L do pa alginatnim kuglicama, uz dodatno fotoumrežavanje, u cilju povećanja temperaturne stabilnosti imobilizata. 2021;:1-66
Janjić Dajana, "Imobilizacija ćelijskih zidova lakazom u kalcijum L do pa alginatnim kuglicama, uz dodatno fotoumrežavanje, u cilju povećanja temperaturne stabilnosti imobilizata" (2021):1-66

On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy

Milošević, Jelica; Prodanović, Radivoje; Polović, Natalija

(MDPI, 2021)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4388
UR  - https://www.mdpi.com/1420-3049/26/4/970
AB  - Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis— Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.
PB  - MDPI
T2  - Molecules
T1  - On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy
VL  - 26
IS  - 4
SP  - 970
DO  - 10.3390/molecules26040970
ER  - 
@article{
author = "Milošević, Jelica and Prodanović, Radivoje and Polović, Natalija",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4388, https://www.mdpi.com/1420-3049/26/4/970",
abstract = "Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis— Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.",
publisher = "MDPI",
journal = "Molecules",
title = "On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy",
volume = "26",
number = "4",
pages = "970",
doi = "10.3390/molecules26040970"
}
Milošević, J., Prodanović, R.,& Polović, N. (2021). On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy.
Molecules
MDPI., 26(4), 970.
https://doi.org/10.3390/molecules26040970
Milošević J, Prodanović R, Polović N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules. 2021;26(4):970
Milošević Jelica, Prodanović Radivoje, Polović Natalija, "On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy" Molecules, 26, no. 4 (2021):970,
https://doi.org/10.3390/molecules26040970 .
2
2

Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970

Milošević, Jelica; Prodanović, Radivoje; Polović, Natalija

(MDPI, 2021)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4391
PB  - MDPI
T2  - Molecules
T1  - Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970
VL  - 26
IS  - 4
SP  - 970
ER  - 
@article{
author = "Milošević, Jelica and Prodanović, Radivoje and Polović, Natalija",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4391",
publisher = "MDPI",
journal = "Molecules",
title = "Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970",
volume = "26",
number = "4",
pages = "970"
}
Milošević, J., Prodanović, R.,& Polović, N. (2021). Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970.
Molecules
MDPI., 26(4), 970.
Milošević J, Prodanović R, Polović N. Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970. Molecules. 2021;26(4):970
Milošević Jelica, Prodanović Radivoje, Polović Natalija, "Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970" Molecules, 26, no. 4 (2021):970

A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A

Menghiu, Gheorghita; Ostafe, Vasile; Prodanović, Radivoje; Fischer, Rainer; Ostafe, Raluca

(MDPI, 2021)

TY  - JOUR
AU  - Menghiu, Gheorghita
AU  - Ostafe, Vasile
AU  - Prodanović, Radivoje
AU  - Fischer, Rainer
AU  - Ostafe, Raluca
PY  - 2021
UR  - https://www.mdpi.com/1422-0067/22/6/3041
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4393
AB  - Chitinases catalyze the degradation of chitin, a polymer of N-acetylglucosamine found in crustacean shells, insect cuticles, and fungal cell walls. There is great interest in the development of improved chitinases to address the environmental burden of chitin waste from the food processing industry as well as the potential medical, agricultural, and industrial uses of partially deacetylated chitin (chitosan) and its products (chito-oligosaccharides). The depolymerization of chitin can be achieved using chemical and physical treatments, but an enzymatic process would be more environmentally friendly and more sustainable. However, chitinases are slow-acting enzymes, limiting their biotechnological exploitation, although this can be overcome by molecular evolution approaches to enhance the features required for specific applications. The two main goals of this study were the development of a high-throughput screening system for chitinase activity (which could be extrapolated to other hydrolytic enzymes), and the deployment of this new method to select improved chitinase variants. We therefore cloned and expressed the Bacillus licheniformis DSM8785 chitinase A (chiA) gene in Escherichia coli BL21 (DE3) cells and generated a mutant library by error-prone PCR. We then developed a screening method based on fluorescence-activated cell sorting (FACS) using the model substrate 4-methylumbelliferyl β-d-N,N′,N″-triacetyl chitotrioside to identify improved enzymes. We prevented cross-talk between emulsion compartments caused by the hydrophobicity of 4-methylumbelliferone, the fluorescent product of the enzymatic reaction, by incorporating cyclodextrins into the aqueous phases. We also addressed the toxicity of long-term chiA expression in E. coli by limiting the reaction time. We identified 12 mutants containing 2–8 mutations per gene resulting in up to twofold higher activity than wild-type ChiA.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A
VL  - 22
IS  - 6
SP  - 3041
DO  - 10.3390/ijms22063041
ER  - 
@article{
author = "Menghiu, Gheorghita and Ostafe, Vasile and Prodanović, Radivoje and Fischer, Rainer and Ostafe, Raluca",
year = "2021",
url = "https://www.mdpi.com/1422-0067/22/6/3041, http://cherry.chem.bg.ac.rs/handle/123456789/4393",
abstract = "Chitinases catalyze the degradation of chitin, a polymer of N-acetylglucosamine found in crustacean shells, insect cuticles, and fungal cell walls. There is great interest in the development of improved chitinases to address the environmental burden of chitin waste from the food processing industry as well as the potential medical, agricultural, and industrial uses of partially deacetylated chitin (chitosan) and its products (chito-oligosaccharides). The depolymerization of chitin can be achieved using chemical and physical treatments, but an enzymatic process would be more environmentally friendly and more sustainable. However, chitinases are slow-acting enzymes, limiting their biotechnological exploitation, although this can be overcome by molecular evolution approaches to enhance the features required for specific applications. The two main goals of this study were the development of a high-throughput screening system for chitinase activity (which could be extrapolated to other hydrolytic enzymes), and the deployment of this new method to select improved chitinase variants. We therefore cloned and expressed the Bacillus licheniformis DSM8785 chitinase A (chiA) gene in Escherichia coli BL21 (DE3) cells and generated a mutant library by error-prone PCR. We then developed a screening method based on fluorescence-activated cell sorting (FACS) using the model substrate 4-methylumbelliferyl β-d-N,N′,N″-triacetyl chitotrioside to identify improved enzymes. We prevented cross-talk between emulsion compartments caused by the hydrophobicity of 4-methylumbelliferone, the fluorescent product of the enzymatic reaction, by incorporating cyclodextrins into the aqueous phases. We also addressed the toxicity of long-term chiA expression in E. coli by limiting the reaction time. We identified 12 mutants containing 2–8 mutations per gene resulting in up to twofold higher activity than wild-type ChiA.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A",
volume = "22",
number = "6",
pages = "3041",
doi = "10.3390/ijms22063041"
}
Menghiu, G., Ostafe, V., Prodanović, R., Fischer, R.,& Ostafe, R. (2021). A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A.
International Journal of Molecular Sciences
MDPI., 22(6), 3041.
https://doi.org/10.3390/ijms22063041
Menghiu G, Ostafe V, Prodanović R, Fischer R, Ostafe R. A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A. International Journal of Molecular Sciences. 2021;22(6):3041
Menghiu Gheorghita, Ostafe Vasile, Prodanović Radivoje, Fischer Rainer, Ostafe Raluca, "A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A" International Journal of Molecular Sciences, 22, no. 6 (2021):3041,
https://doi.org/10.3390/ijms22063041 .

Supplementary data for the article: Menghiu, G.; Ostafe, V.; Prodanović, R.; Fischer, R.; Ostafe, R. A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A. International Journal of Molecular Sciences 2021, 22 (6), 3041. https://doi.org/10.3390/ijms22063041.

Menghiu, Gheorghita; Ostafe, Vasile; Prodanović, Radivoje; Fischer, Rainer; Ostafe, Raluca

(MDPI, 2021)


                                            

                                            
Menghiu, G., Ostafe, V., Prodanović, R., Fischer, R.,& Ostafe, R. (2021). Supplementary data for the article: Menghiu, G.; Ostafe, V.; Prodanović, R.; Fischer, R.; Ostafe, R. A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A. International Journal of Molecular Sciences 2021, 22 (6), 3041. https://doi.org/10.3390/ijms22063041..
International Journal of Molecular Sciences
MDPI..
Menghiu G, Ostafe V, Prodanović R, Fischer R, Ostafe R. Supplementary data for the article: Menghiu, G.; Ostafe, V.; Prodanović, R.; Fischer, R.; Ostafe, R. A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A. International Journal of Molecular Sciences 2021, 22 (6), 3041. https://doi.org/10.3390/ijms22063041.. International Journal of Molecular Sciences. 2021;
Menghiu Gheorghita, Ostafe Vasile, Prodanović Radivoje, Fischer Rainer, Ostafe Raluca, "Supplementary data for the article: Menghiu, G.; Ostafe, V.; Prodanović, R.; Fischer, R.; Ostafe, R. A High-Throughput Screening System Based on Fluorescence-Activated Cell Sorting for the Directed Evolution of Chitinase A. International Journal of Molecular Sciences 2021, 22 (6), 3041. https://doi.org/10.3390/ijms22063041." International Journal of Molecular Sciences (2021)

Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization

Popović, Nikolina; Pržulj, Dunja; Mladenović, Maja; Prodanović, Olivera; Ece, Selin; Ilić Đurđić, Karla; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(2021)

TY  - JOUR
AU  - Popović, Nikolina
AU  - Pržulj, Dunja
AU  - Mladenović, Maja
AU  - Prodanović, Olivera
AU  - Ece, Selin
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0141813021008813
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4404
AB  - High amounts of toxic textile dyes are released into the environment due to coloring and wastewaters treatment processes' inefficiency. To remove dyes from the environment and wastewaters, researchers focused on applying immobilized enzymes due to mild reaction conditions and enzyme nontoxicity. Laccases are oxidases with wide substrate specificity, capable of degradation of many different dye types. Laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The specific activity of surface-displayed laccase was increased by toluene-induced lysis to 3.1 U/g of cell walls. For cell wall laccase immobilization within hydrogel beads, alginate was modified by dopamine using periodate oxidation and reductive amination and characterized by UV–Vis, FTIR, and NMR spectroscopy. Cell wall laccase was immobilized within alginate and dopamine-alginate beads additionally cross-linked by oxygen and laccase. The immobilized enzyme's specific activity was two times higher using dopamine-alginate compared to native alginate beads, and immobilization yield increased 16 times. Cell wall laccase immobilized within dopamine-alginate beads decolorized Amido Black 10B, Reactive Black 5, Evans Blue, and Remazol Brilliant Blue with 100% efficiency and after ten rounds of multiple-use retained decolorization efficiency of 90% with Evans Blue and 61% with Amido Black.
T2  - International Journal of Biological Macromolecules
T1  - Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization
VL  - 181
SP  - 1072
EP  - 1080
DO  - 10.1016/j.ijbiomac.2021.04.115
ER  - 
@article{
author = "Popović, Nikolina and Pržulj, Dunja and Mladenović, Maja and Prodanović, Olivera and Ece, Selin and Ilić Đurđić, Karla and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2021",
url = "https://www.sciencedirect.com/science/article/pii/S0141813021008813, http://cherry.chem.bg.ac.rs/handle/123456789/4404",
abstract = "High amounts of toxic textile dyes are released into the environment due to coloring and wastewaters treatment processes' inefficiency. To remove dyes from the environment and wastewaters, researchers focused on applying immobilized enzymes due to mild reaction conditions and enzyme nontoxicity. Laccases are oxidases with wide substrate specificity, capable of degradation of many different dye types. Laccase from Streptomyces cyaneus was expressed on the surface of Saccharomyces cerevisiae EBY100 cells. The specific activity of surface-displayed laccase was increased by toluene-induced lysis to 3.1 U/g of cell walls. For cell wall laccase immobilization within hydrogel beads, alginate was modified by dopamine using periodate oxidation and reductive amination and characterized by UV–Vis, FTIR, and NMR spectroscopy. Cell wall laccase was immobilized within alginate and dopamine-alginate beads additionally cross-linked by oxygen and laccase. The immobilized enzyme's specific activity was two times higher using dopamine-alginate compared to native alginate beads, and immobilization yield increased 16 times. Cell wall laccase immobilized within dopamine-alginate beads decolorized Amido Black 10B, Reactive Black 5, Evans Blue, and Remazol Brilliant Blue with 100% efficiency and after ten rounds of multiple-use retained decolorization efficiency of 90% with Evans Blue and 61% with Amido Black.",
journal = "International Journal of Biological Macromolecules",
title = "Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization",
volume = "181",
pages = "1072-1080",
doi = "10.1016/j.ijbiomac.2021.04.115"
}
Popović, N., Pržulj, D., Mladenović, M., Prodanović, O., Ece, S., Ilić Đurđić, K., Ostafe, R., Fischer, R.,& Prodanović, R. (2021). Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization.
International Journal of Biological Macromolecules, 181, 1072-1080.
https://doi.org/10.1016/j.ijbiomac.2021.04.115
Popović N, Pržulj D, Mladenović M, Prodanović O, Ece S, Ilić Đurđić K, Ostafe R, Fischer R, Prodanović R. Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization. International Journal of Biological Macromolecules. 2021;181:1072-1080
Popović Nikolina, Pržulj Dunja, Mladenović Maja, Prodanović Olivera, Ece Selin, Ilić Đurđić Karla, Ostafe Raluca, Fischer Rainer, Prodanović Radivoje, "Immobilization of yeast cell walls with surface displayed laccase from Streptomyces cyaneus within dopamine-alginate beads for dye decolorization" International Journal of Biological Macromolecules, 181 (2021):1072-1080,
https://doi.org/10.1016/j.ijbiomac.2021.04.115 .
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