TY  - JOUR
AU  - Novakovi, Miroslav M.
AU  - Ilić-Tomić, Tatjana
AU  - Tešević, Vele
AU  - Simić, Katarina
AU  - Ivanović, Stefan
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1310
AB  - TheTrametes versicolorlaccase catalyzed oxidation of chalcone butein afforded four dimers of aurone sulfuretin (i.e.two regioisomeric pairs of diasteromers,1-4) as the major products. The formation of the dimers was explained by a two step process involving the initial cyclization of butein into aurone sulfuretin, followed by the combination of two molecules of sulfuretin. The coupling process occurred between the 2,10-double bond of one molecule of sulfuretin and the (3 ',4 ') catechol group of the other to yield a dimeric structure. This was confirmed by the experiment involving the laccase catalyzed oxidation of sulfuretin yielding the same dimeric bisaurones. Compounds1,3and4, were isolated using semipreparative HPLC and characterized by the detailed analysis of the NMR, MS, IR, and UV-vis data. The structure of compound2, isolated as a mixture containingca.25% of compound1,was proposed by the comparison of(1)H NMR data to compound1and by using LC-ESIMS analysis. The starting chalcone butein and the products of the biocatalytic transformation, aurone sulfuretin and sulfuretin dimers1,3and4,were evaluated for their cytotoxic and antioxidative propertiesin vitrousing a healthy human fibroblast (MRC5) cell line. The biotransformation products showed lower cytotoxicity but higher antioxidative properties. TheC. coggygriabark methanol extract rich in butein and sulfuretin was also biotransformed by laccase. The transformed extract exhibited significantly improved antioxidative activities.
PB  - Royal Soc Chemistry, Cambridge
T2  - New Journal of Chemistry
T1  - Bisaurones - enzymatic production and biological evaluation
EP  - 9655
IS  - 23
SP  - 9647
VL  - 44
DO  - 10.1039/d0nj00758g
ER  - 

@article{
author = "Novakovi, Miroslav M. and Ilić-Tomić, Tatjana and Tešević, Vele and Simić, Katarina and Ivanović, Stefan and Simić, Stefan and Opsenica, Igor and Nikodinović-Runić, Jasmina",
year = "2020",
abstract = "TheTrametes versicolorlaccase catalyzed oxidation of chalcone butein afforded four dimers of aurone sulfuretin (i.e.two regioisomeric pairs of diasteromers,1-4) as the major products. The formation of the dimers was explained by a two step process involving the initial cyclization of butein into aurone sulfuretin, followed by the combination of two molecules of sulfuretin. The coupling process occurred between the 2,10-double bond of one molecule of sulfuretin and the (3 ',4 ') catechol group of the other to yield a dimeric structure. This was confirmed by the experiment involving the laccase catalyzed oxidation of sulfuretin yielding the same dimeric bisaurones. Compounds1,3and4, were isolated using semipreparative HPLC and characterized by the detailed analysis of the NMR, MS, IR, and UV-vis data. The structure of compound2, isolated as a mixture containingca.25% of compound1,was proposed by the comparison of(1)H NMR data to compound1and by using LC-ESIMS analysis. The starting chalcone butein and the products of the biocatalytic transformation, aurone sulfuretin and sulfuretin dimers1,3and4,were evaluated for their cytotoxic and antioxidative propertiesin vitrousing a healthy human fibroblast (MRC5) cell line. The biotransformation products showed lower cytotoxicity but higher antioxidative properties. TheC. coggygriabark methanol extract rich in butein and sulfuretin was also biotransformed by laccase. The transformed extract exhibited significantly improved antioxidative activities.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "New Journal of Chemistry",
title = "Bisaurones - enzymatic production and biological evaluation",
pages = "9655-9647",
number = "23",
volume = "44",
doi = "10.1039/d0nj00758g"
}

Novakovi, M. M., Ilić-Tomić, T., Tešević, V., Simić, K., Ivanović, S., Simić, S., Opsenica, I.,& Nikodinović-Runić, J.. (2020). Bisaurones - enzymatic production and biological evaluation. in New Journal of Chemistry
Royal Soc Chemistry, Cambridge., 44(23), 9647-9655.
https://doi.org/10.1039/d0nj00758g

Novakovi MM, Ilić-Tomić T, Tešević V, Simić K, Ivanović S, Simić S, Opsenica I, Nikodinović-Runić J. Bisaurones - enzymatic production and biological evaluation. in New Journal of Chemistry. 2020;44(23):9647-9655.
doi:10.1039/d0nj00758g .

Novakovi, Miroslav M., Ilić-Tomić, Tatjana, Tešević, Vele, Simić, Katarina, Ivanović, Stefan, Simić, Stefan, Opsenica, Igor, Nikodinović-Runić, Jasmina, "Bisaurones - enzymatic production and biological evaluation" in New Journal of Chemistry, 44, no. 23 (2020):9647-9655,
https://doi.org/10.1039/d0nj00758g . .

TY  - JOUR
AU  - Novaković, Miroslav
AU  - Simić, Stefan
AU  - Koracak, Ljiljana
AU  - Zlatović, Mario
AU  - Ilić-Tomić, Tatjana
AU  - Asakawa, Yoshinori
AU  - Nikodinović-Runić, Jasmina
AU  - Opsenica, Igor
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1367
AB  - Chemical and biocatalytic synthesis of seven previously undescribed marchantin A ester derivatives has been presented. Chemical synthesis afforded three peresterified bisbibenzyl products (TE1-TE3), while enzymatic method, using lipase, produced regioselective monoester derivatives (ME1-ME4). The antiproliferative activities of all prepared derivatives of marchantin A were tested on MRC-5 healthy human lung fibroblast, A549 human lung cancer, and MDA-MB-231 human breast cancer cell lines. All tested esters were less cytotoxic in comparison to marchantin A, but they also exhibited lower cytotoxicity against healthy cells. Monoesters displayed higher cytotoxic activities than the corresponding peresterified products, presumably due to the presence of free catechol group. Monohexanoyl ester ME3 displayed the same IC50 like marchantin A against MDA-MB-231 cells, but the selectivity was higher. In this way, regioselective enzymatic monoesterification enhanced selectivity of marchantin A. ME3 was also the most active among all derivatives against lung cancer cells A549 with the slightly lower activity and selectivity in comparison to marchantin A.
PB  - Elsevier, Amsterdam
T2  - Fitoterapia
T1  - Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives
VL  - 142
DO  - 10.1016/j.fitote.2020.104520
ER  - 

@article{
author = "Novaković, Miroslav and Simić, Stefan and Koracak, Ljiljana and Zlatović, Mario and Ilić-Tomić, Tatjana and Asakawa, Yoshinori and Nikodinović-Runić, Jasmina and Opsenica, Igor",
year = "2020",
abstract = "Chemical and biocatalytic synthesis of seven previously undescribed marchantin A ester derivatives has been presented. Chemical synthesis afforded three peresterified bisbibenzyl products (TE1-TE3), while enzymatic method, using lipase, produced regioselective monoester derivatives (ME1-ME4). The antiproliferative activities of all prepared derivatives of marchantin A were tested on MRC-5 healthy human lung fibroblast, A549 human lung cancer, and MDA-MB-231 human breast cancer cell lines. All tested esters were less cytotoxic in comparison to marchantin A, but they also exhibited lower cytotoxicity against healthy cells. Monoesters displayed higher cytotoxic activities than the corresponding peresterified products, presumably due to the presence of free catechol group. Monohexanoyl ester ME3 displayed the same IC50 like marchantin A against MDA-MB-231 cells, but the selectivity was higher. In this way, regioselective enzymatic monoesterification enhanced selectivity of marchantin A. ME3 was also the most active among all derivatives against lung cancer cells A549 with the slightly lower activity and selectivity in comparison to marchantin A.",
publisher = "Elsevier, Amsterdam",
journal = "Fitoterapia",
title = "Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives",
volume = "142",
doi = "10.1016/j.fitote.2020.104520"
}

Novaković, M., Simić, S., Koracak, L., Zlatović, M., Ilić-Tomić, T., Asakawa, Y., Nikodinović-Runić, J.,& Opsenica, I.. (2020). Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives. in Fitoterapia
Elsevier, Amsterdam., 142.
https://doi.org/10.1016/j.fitote.2020.104520

Novaković M, Simić S, Koracak L, Zlatović M, Ilić-Tomić T, Asakawa Y, Nikodinović-Runić J, Opsenica I. Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives. in Fitoterapia. 2020;142.
doi:10.1016/j.fitote.2020.104520 .

Novaković, Miroslav, Simić, Stefan, Koracak, Ljiljana, Zlatović, Mario, Ilić-Tomić, Tatjana, Asakawa, Yoshinori, Nikodinović-Runić, Jasmina, Opsenica, Igor, "Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives" in Fitoterapia, 142 (2020),
https://doi.org/10.1016/j.fitote.2020.104520 . .

TY  - JOUR
AU  - Novaković, Miroslav
AU  - Simić, Stefan
AU  - Koracak, Ljiljana
AU  - Zlatović, Mario
AU  - Ilić-Tomić, Tatjana
AU  - Asakawa, Yoshinori
AU  - Nikodinović-Runić, Jasmina
AU  - Opsenica, Igor
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1755
AB  - Chemical and biocatalytic synthesis of seven previously undescribed marchantin A ester derivatives has been presented. Chemical synthesis afforded three peresterified bisbibenzyl products (TE1-TE3), while enzymatic method, using lipase, produced regioselective monoester derivatives (ME1-ME4). The antiproliferative activities of all prepared derivatives of marchantin A were tested on MRC-5 healthy human lung fibroblast, A549 human lung cancer, and MDA-MB-231 human breast cancer cell lines. All tested esters were less cytotoxic in comparison to marchantin A, but they also exhibited lower cytotoxicity against healthy cells. Monoesters displayed higher cytotoxic activities than the corresponding peresterified products, presumably due to the presence of free catechol group. Monohexanoyl ester ME3 displayed the same IC50 like marchantin A against MDA-MB-231 cells, but the selectivity was higher. In this way, regioselective enzymatic monoesterification enhanced selectivity of marchantin A. ME3 was also the most active among all derivatives against lung cancer cells A549 with the slightly lower activity and selectivity in comparison to marchantin A.
PB  - Elsevier, Amsterdam
T2  - Fitoterapia
T1  - Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives
VL  - 142
DO  - 10.1016/j.fitote.2020.104520
ER  - 

@article{
author = "Novaković, Miroslav and Simić, Stefan and Koracak, Ljiljana and Zlatović, Mario and Ilić-Tomić, Tatjana and Asakawa, Yoshinori and Nikodinović-Runić, Jasmina and Opsenica, Igor",
year = "2020",
abstract = "Chemical and biocatalytic synthesis of seven previously undescribed marchantin A ester derivatives has been presented. Chemical synthesis afforded three peresterified bisbibenzyl products (TE1-TE3), while enzymatic method, using lipase, produced regioselective monoester derivatives (ME1-ME4). The antiproliferative activities of all prepared derivatives of marchantin A were tested on MRC-5 healthy human lung fibroblast, A549 human lung cancer, and MDA-MB-231 human breast cancer cell lines. All tested esters were less cytotoxic in comparison to marchantin A, but they also exhibited lower cytotoxicity against healthy cells. Monoesters displayed higher cytotoxic activities than the corresponding peresterified products, presumably due to the presence of free catechol group. Monohexanoyl ester ME3 displayed the same IC50 like marchantin A against MDA-MB-231 cells, but the selectivity was higher. In this way, regioselective enzymatic monoesterification enhanced selectivity of marchantin A. ME3 was also the most active among all derivatives against lung cancer cells A549 with the slightly lower activity and selectivity in comparison to marchantin A.",
publisher = "Elsevier, Amsterdam",
journal = "Fitoterapia",
title = "Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives",
volume = "142",
doi = "10.1016/j.fitote.2020.104520"
}

Novaković, M., Simić, S., Koracak, L., Zlatović, M., Ilić-Tomić, T., Asakawa, Y., Nikodinović-Runić, J.,& Opsenica, I.. (2020). Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives. in Fitoterapia
Elsevier, Amsterdam., 142.
https://doi.org/10.1016/j.fitote.2020.104520

Novaković M, Simić S, Koracak L, Zlatović M, Ilić-Tomić T, Asakawa Y, Nikodinović-Runić J, Opsenica I. Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives. in Fitoterapia. 2020;142.
doi:10.1016/j.fitote.2020.104520 .

Novaković, Miroslav, Simić, Stefan, Koracak, Ljiljana, Zlatović, Mario, Ilić-Tomić, Tatjana, Asakawa, Yoshinori, Nikodinović-Runić, Jasmina, Opsenica, Igor, "Chemo- and biocatalytic esterification of marchantin A and cytotoxic activity of ester derivatives" in Fitoterapia, 142 (2020),
https://doi.org/10.1016/j.fitote.2020.104520 . .

TY  - JOUR
AU  - Ilić-Tomić, Tatjana
AU  - Tešević, Vele
AU  - Simić, Katarina
AU  - Ivanović, Stefan
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1761
AB  - TheTrametes versicolorlaccase catalyzed oxidation of chalcone butein afforded four dimers of aurone sulfuretin (i.e.two regioisomeric pairs of diasteromers,1-4) as the major products. The formation of the dimers was explained by a two step process involving the initial cyclization of butein into aurone sulfuretin, followed by the combination of two molecules of sulfuretin. The coupling process occurred between the 2,10-double bond of one molecule of sulfuretin and the (3 ',4 ') catechol group of the other to yield a dimeric structure. This was confirmed by the experiment involving the laccase catalyzed oxidation of sulfuretin yielding the same dimeric bisaurones. Compounds1,3and4, were isolated using semipreparative HPLC and characterized by the detailed analysis of the NMR, MS, IR, and UV-vis data. The structure of compound2, isolated as a mixture containingca.25% of compound1,was proposed by the comparison of(1)H NMR data to compound1and by using LC-ESIMS analysis. The starting chalcone butein and the products of the biocatalytic transformation, aurone sulfuretin and sulfuretin dimers1,3and4,were evaluated for their cytotoxic and antioxidative propertiesin vitrousing a healthy human fibroblast (MRC5) cell line. The biotransformation products showed lower cytotoxicity but higher antioxidative properties. TheC. coggygriabark methanol extract rich in butein and sulfuretin was also biotransformed by laccase. The transformed extract exhibited significantly improved antioxidative activities.
PB  - Royal Soc Chemistry, Cambridge
T2  - New Journal of Chemistry
T1  - Bisaurones - enzymatic production and biological evaluation
EP  - 9655
IS  - 23
SP  - 9647
VL  - 44
DO  - 10.1039/d0nj00758g
ER  - 

@article{
author = "Ilić-Tomić, Tatjana and Tešević, Vele and Simić, Katarina and Ivanović, Stefan and Simić, Stefan and Opsenica, Igor and Nikodinović-Runić, Jasmina",
year = "2020",
abstract = "TheTrametes versicolorlaccase catalyzed oxidation of chalcone butein afforded four dimers of aurone sulfuretin (i.e.two regioisomeric pairs of diasteromers,1-4) as the major products. The formation of the dimers was explained by a two step process involving the initial cyclization of butein into aurone sulfuretin, followed by the combination of two molecules of sulfuretin. The coupling process occurred between the 2,10-double bond of one molecule of sulfuretin and the (3 ',4 ') catechol group of the other to yield a dimeric structure. This was confirmed by the experiment involving the laccase catalyzed oxidation of sulfuretin yielding the same dimeric bisaurones. Compounds1,3and4, were isolated using semipreparative HPLC and characterized by the detailed analysis of the NMR, MS, IR, and UV-vis data. The structure of compound2, isolated as a mixture containingca.25% of compound1,was proposed by the comparison of(1)H NMR data to compound1and by using LC-ESIMS analysis. The starting chalcone butein and the products of the biocatalytic transformation, aurone sulfuretin and sulfuretin dimers1,3and4,were evaluated for their cytotoxic and antioxidative propertiesin vitrousing a healthy human fibroblast (MRC5) cell line. The biotransformation products showed lower cytotoxicity but higher antioxidative properties. TheC. coggygriabark methanol extract rich in butein and sulfuretin was also biotransformed by laccase. The transformed extract exhibited significantly improved antioxidative activities.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "New Journal of Chemistry",
title = "Bisaurones - enzymatic production and biological evaluation",
pages = "9655-9647",
number = "23",
volume = "44",
doi = "10.1039/d0nj00758g"
}

Ilić-Tomić, T., Tešević, V., Simić, K., Ivanović, S., Simić, S., Opsenica, I.,& Nikodinović-Runić, J.. (2020). Bisaurones - enzymatic production and biological evaluation. in New Journal of Chemistry
Royal Soc Chemistry, Cambridge., 44(23), 9647-9655.
https://doi.org/10.1039/d0nj00758g

Ilić-Tomić T, Tešević V, Simić K, Ivanović S, Simić S, Opsenica I, Nikodinović-Runić J. Bisaurones - enzymatic production and biological evaluation. in New Journal of Chemistry. 2020;44(23):9647-9655.
doi:10.1039/d0nj00758g .

Ilić-Tomić, Tatjana, Tešević, Vele, Simić, Katarina, Ivanović, Stefan, Simić, Stefan, Opsenica, Igor, Nikodinović-Runić, Jasmina, "Bisaurones - enzymatic production and biological evaluation" in New Journal of Chemistry, 44, no. 23 (2020):9647-9655,
https://doi.org/10.1039/d0nj00758g . .

TY  - JOUR
AU  - Simić, Stefan
AU  - Jeremić, Sanja
AU  - Đokić, Lidija
AU  - Bozić, Nataša
AU  - Vujcić, Zoran
AU  - Loncar, Nikola
AU  - Senthamaraikannan, Ramsankar
AU  - Babu, Ramesh
AU  - Opsenica, Igor M.
AU  - Nikodinović-Runić, Jasmina
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1406
AB  - Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7-24 h with good yields (70-99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 degrees C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.
PB  - New York : Elsevier Science Inc
T2  - Enzyme and Microbial Technology
T1  - Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines
VL  - 132
DO  - 10.1016/j.enzmictec.2019.109411
ER  - 

@article{
author = "Simić, Stefan and Jeremić, Sanja and Đokić, Lidija and Bozić, Nataša and Vujcić, Zoran and Loncar, Nikola and Senthamaraikannan, Ramsankar and Babu, Ramesh and Opsenica, Igor M. and Nikodinović-Runić, Jasmina",
year = "2020",
abstract = "Biocatalytic oxidations mediated by laccases are gaining importance due to their versatility and beneficial environmental effects. In this study, the oxidation of 1,4-dihydropyridines has been performed using three different types of bacterial laccase-based catalysts: purified laccase from Bacillus licheniformis ATCC 9945a (BliLacc), Escherichia coli whole cells expressing this laccase, and bacterial nanocellulose (BNC) supported BliLacc catalysts. The catalysts based on bacterial laccase were compared to the commercially available Trametes versicolor laccase (TvLacc). The oxidation product of 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylate was obtained within 7-24 h with good yields (70-99%) with all three biocatalysts. The substrate scope was examined with five additional 1,4-dihydropyridines, one of which was oxidized in high yield. Whole-cell biocatalyst was stable when stored for up to 1-month at 4 degrees C. In addition, evidence has been provided that multicopper oxidase CueO from the E. coli expression host contributed to the oxidation efficiency of the whole-cell biocatalyst. The immobilized whole-cell biocatalyst showed satisfactory activity and retained 37% of its original activity after three biotransformation cycles.",
publisher = "New York : Elsevier Science Inc",
journal = "Enzyme and Microbial Technology",
title = "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines",
volume = "132",
doi = "10.1016/j.enzmictec.2019.109411"
}

Simić, S., Jeremić, S., Đokić, L., Bozić, N., Vujcić, Z., Loncar, N., Senthamaraikannan, R., Babu, R., Opsenica, I. M.,& Nikodinović-Runić, J.. (2020). Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology
New York : Elsevier Science Inc., 132.
https://doi.org/10.1016/j.enzmictec.2019.109411

Simić S, Jeremić S, Đokić L, Bozić N, Vujcić Z, Loncar N, Senthamaraikannan R, Babu R, Opsenica IM, Nikodinović-Runić J. Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines. in Enzyme and Microbial Technology. 2020;132.
doi:10.1016/j.enzmictec.2019.109411 .

Simić, Stefan, Jeremić, Sanja, Đokić, Lidija, Bozić, Nataša, Vujcić, Zoran, Loncar, Nikola, Senthamaraikannan, Ramsankar, Babu, Ramesh, Opsenica, Igor M., Nikodinović-Runić, Jasmina, "Development of an efficient biocatalytic system based on bacterial laccase for the oxidation of selected 1,4-dihydropyridines" in Enzyme and Microbial Technology, 132 (2020),
https://doi.org/10.1016/j.enzmictec.2019.109411 . .

TY  - JOUR
AU  - Zerva, Anastasia
AU  - Simić, Stefan
AU  - Topakas, Evangelos
AU  - Nikodinović-Runić, Jasmina
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1227
AB  - There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society's increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.
PB  - MDPI, Basel
T2  - Catalysts
T1  - Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)
IS  - 12
VL  - 9
DO  - 10.3390/catal9121023
ER  - 

@article{
author = "Zerva, Anastasia and Simić, Stefan and Topakas, Evangelos and Nikodinović-Runić, Jasmina",
year = "2019",
abstract = "There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society's increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.",
publisher = "MDPI, Basel",
journal = "Catalysts",
title = "Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)",
number = "12",
volume = "9",
doi = "10.3390/catal9121023"
}

Zerva, A., Simić, S., Topakas, E.,& Nikodinović-Runić, J.. (2019). Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019). in Catalysts
MDPI, Basel., 9(12).
https://doi.org/10.3390/catal9121023

Zerva A, Simić S, Topakas E, Nikodinović-Runić J. Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019). in Catalysts. 2019;9(12).
doi:10.3390/catal9121023 .

Zerva, Anastasia, Simić, Stefan, Topakas, Evangelos, Nikodinović-Runić, Jasmina, "Applications of Microbial Laccases: Patent Review of the Past Decade (2009-2019)" in Catalysts, 9, no. 12 (2019),
https://doi.org/10.3390/catal9121023 . .

TY  - JOUR
AU  - Ajdačić, Vladimir
AU  - Nikolić, Andrea
AU  - Simić, Stefan
AU  - Manojlović, Dragan
AU  - Stojanović, Zoran
AU  - Nikodinović-Runić, Jasmina
AU  - Opsenica, Igor M.
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1171
AB  - A facile decarbonylation reaction of a variety of aromatic and heteroaromatic aldehydes using maghemite-supported palladium catalyst has been developed. The magnetic properties of catalyst facilitated an easy and efficient recovery of the catalyst from the reaction mixture using an external magnet. It was found that the catalyst could be reused up to four consecutive catalytic runs without a significant change in activity. In addition, the catalyst was also very effective in the dehalogenation of aryl halides. This is the first report on efficient utilization of directly immobilized Pd on maghemite in decarbonylation and dehalogenation reactions.
PB  - Georg Thieme Verlag Kg, Stuttgart
T2  - Synthesis-Stuttgart
T1  - Decarbonylation of Aromatic Aldehydes and Dehalogenation of Aryl Halides Using Maghemite-Supported Palladium Catalyst
EP  - 126
IS  - 1
SP  - 119
VL  - 50
DO  - 10.1055/s-0036-1590892
ER  - 

@article{
author = "Ajdačić, Vladimir and Nikolić, Andrea and Simić, Stefan and Manojlović, Dragan and Stojanović, Zoran and Nikodinović-Runić, Jasmina and Opsenica, Igor M.",
year = "2018",
abstract = "A facile decarbonylation reaction of a variety of aromatic and heteroaromatic aldehydes using maghemite-supported palladium catalyst has been developed. The magnetic properties of catalyst facilitated an easy and efficient recovery of the catalyst from the reaction mixture using an external magnet. It was found that the catalyst could be reused up to four consecutive catalytic runs without a significant change in activity. In addition, the catalyst was also very effective in the dehalogenation of aryl halides. This is the first report on efficient utilization of directly immobilized Pd on maghemite in decarbonylation and dehalogenation reactions.",
publisher = "Georg Thieme Verlag Kg, Stuttgart",
journal = "Synthesis-Stuttgart",
title = "Decarbonylation of Aromatic Aldehydes and Dehalogenation of Aryl Halides Using Maghemite-Supported Palladium Catalyst",
pages = "126-119",
number = "1",
volume = "50",
doi = "10.1055/s-0036-1590892"
}

Ajdačić, V., Nikolić, A., Simić, S., Manojlović, D., Stojanović, Z., Nikodinović-Runić, J.,& Opsenica, I. M.. (2018). Decarbonylation of Aromatic Aldehydes and Dehalogenation of Aryl Halides Using Maghemite-Supported Palladium Catalyst. in Synthesis-Stuttgart
Georg Thieme Verlag Kg, Stuttgart., 50(1), 119-126.
https://doi.org/10.1055/s-0036-1590892

Ajdačić V, Nikolić A, Simić S, Manojlović D, Stojanović Z, Nikodinović-Runić J, Opsenica IM. Decarbonylation of Aromatic Aldehydes and Dehalogenation of Aryl Halides Using Maghemite-Supported Palladium Catalyst. in Synthesis-Stuttgart. 2018;50(1):119-126.
doi:10.1055/s-0036-1590892 .

Ajdačić, Vladimir, Nikolić, Andrea, Simić, Stefan, Manojlović, Dragan, Stojanović, Zoran, Nikodinović-Runić, Jasmina, Opsenica, Igor M., "Decarbonylation of Aromatic Aldehydes and Dehalogenation of Aryl Halides Using Maghemite-Supported Palladium Catalyst" in Synthesis-Stuttgart, 50, no. 1 (2018):119-126,
https://doi.org/10.1055/s-0036-1590892 . .