TY  - JOUR
AU  - Slavić, Marinela Šokarda
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Stanisavljević, Nemanja S.
AU  - Gardijan, Lazar
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6351
AB  - α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respectively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications
VL  - 249
SP  - 126055
DO  - 10.1016/j.ijbiomac.2023.126055
ER  - 

@article{
author = "Slavić, Marinela Šokarda and Kojić, Milan and Margetić, Aleksandra and Stanisavljević, Nemanja S. and Gardijan, Lazar and Božić, Nataša and Vujčić, Zoran",
year = "2023",
abstract = "α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respectively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications",
volume = "249",
pages = "126055",
doi = "10.1016/j.ijbiomac.2023.126055"
}

Slavić, M. Š., Kojić, M., Margetić, A., Stanisavljević, N. S., Gardijan, L., Božić, N.,& Vujčić, Z.. (2023). Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. in International Journal of Biological Macromolecules
Elsevier., 249, 126055.
https://doi.org/10.1016/j.ijbiomac.2023.126055

Slavić MŠ, Kojić M, Margetić A, Stanisavljević NS, Gardijan L, Božić N, Vujčić Z. Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. in International Journal of Biological Macromolecules. 2023;249:126055.
doi:10.1016/j.ijbiomac.2023.126055 .

Slavić, Marinela Šokarda, Kojić, Milan, Margetić, Aleksandra, Stanisavljević, Nemanja S., Gardijan, Lazar, Božić, Nataša, Vujčić, Zoran, "Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications" in International Journal of Biological Macromolecules, 249 (2023):126055,
https://doi.org/10.1016/j.ijbiomac.2023.126055 . .

TY  - JOUR
AU  - Pavlović, Marija
AU  - Šokarda Slavić, Marinela
AU  - Ristović, Marina
AU  - Stojanović, Sanja
AU  - Margetić, Aleksandra
AU  - Momčilović, Miloš
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6321
AB  - The main goal of this study was to examine the efficiency of a newly isolated fungus from quince, Aspergillus tubingensis FAT43, to produce the pectinolytic complex using agricultural and industrial waste as the substrate for solid state fermentation. Sugar beet pulp was the most effective substrate inducer of pectinolytic complex synthesis out of all the waste residues examined. For endo-pectinolytic and total pectinolytic activity, respectively, statistical optimization using Placked-Burman Design and Optimal (Custom) Design increased production by 2.22 and 2.15-fold, respectively. Liquification, clarification, and an increase in the amount of reducing sugar in fruit juices (apple, banana, apricot, orange, and quince) processed with pectinolytic complex were identified. Enzymatic pre-treatment considerably increases yield (14%–22%) and clarification (90%). After enzymatic treatment, the best liquefaction was observed in orange juice, whereas the best clarification was obtained in apricot juice. Additionally, the pectinolytic treatment of apricot juice resulted in the highest increase in reducing sugar concentration (11%) compared to all other enzymatically treated juices. Optimizing the production of a highly active pectinolytic complex and its efficient utilization in the processing of fruit juices, including the generation of an increasing amount of waste, are the significant outcomes of this research.
PB  - Oxford University Press
T2  - Letters in Applied Microbiology
T1  - Optimization of solid-state fermentation for enhanced production of pectinolytic complex by Aspergillus tubingensis FAT43 and its application in fruit juice processing
VL  - 76
IS  - 8
SP  - ovad083
DO  - 10.1093/lambio/ovad083
ER  - 

@article{
author = "Pavlović, Marija and Šokarda Slavić, Marinela and Ristović, Marina and Stojanović, Sanja and Margetić, Aleksandra and Momčilović, Miloš and Vujčić, Zoran",
year = "2023",
abstract = "The main goal of this study was to examine the efficiency of a newly isolated fungus from quince, Aspergillus tubingensis FAT43, to produce the pectinolytic complex using agricultural and industrial waste as the substrate for solid state fermentation. Sugar beet pulp was the most effective substrate inducer of pectinolytic complex synthesis out of all the waste residues examined. For endo-pectinolytic and total pectinolytic activity, respectively, statistical optimization using Placked-Burman Design and Optimal (Custom) Design increased production by 2.22 and 2.15-fold, respectively. Liquification, clarification, and an increase in the amount of reducing sugar in fruit juices (apple, banana, apricot, orange, and quince) processed with pectinolytic complex were identified. Enzymatic pre-treatment considerably increases yield (14%–22%) and clarification (90%). After enzymatic treatment, the best liquefaction was observed in orange juice, whereas the best clarification was obtained in apricot juice. Additionally, the pectinolytic treatment of apricot juice resulted in the highest increase in reducing sugar concentration (11%) compared to all other enzymatically treated juices. Optimizing the production of a highly active pectinolytic complex and its efficient utilization in the processing of fruit juices, including the generation of an increasing amount of waste, are the significant outcomes of this research.",
publisher = "Oxford University Press",
journal = "Letters in Applied Microbiology",
title = "Optimization of solid-state fermentation for enhanced production of pectinolytic complex by Aspergillus tubingensis FAT43 and its application in fruit juice processing",
volume = "76",
number = "8",
pages = "ovad083",
doi = "10.1093/lambio/ovad083"
}

Pavlović, M., Šokarda Slavić, M., Ristović, M., Stojanović, S., Margetić, A., Momčilović, M.,& Vujčić, Z.. (2023). Optimization of solid-state fermentation for enhanced production of pectinolytic complex by Aspergillus tubingensis FAT43 and its application in fruit juice processing. in Letters in Applied Microbiology
Oxford University Press., 76(8), ovad083.
https://doi.org/10.1093/lambio/ovad083

Pavlović M, Šokarda Slavić M, Ristović M, Stojanović S, Margetić A, Momčilović M, Vujčić Z. Optimization of solid-state fermentation for enhanced production of pectinolytic complex by Aspergillus tubingensis FAT43 and its application in fruit juice processing. in Letters in Applied Microbiology. 2023;76(8):ovad083.
doi:10.1093/lambio/ovad083 .

Pavlović, Marija, Šokarda Slavić, Marinela, Ristović, Marina, Stojanović, Sanja, Margetić, Aleksandra, Momčilović, Miloš, Vujčić, Zoran, "Optimization of solid-state fermentation for enhanced production of pectinolytic complex by Aspergillus tubingensis FAT43 and its application in fruit juice processing" in Letters in Applied Microbiology, 76, no. 8 (2023):ovad083,
https://doi.org/10.1093/lambio/ovad083 . .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Ralić, Vanja
AU  - Nastasijević, Branislav
AU  - Matijević, Milica
AU  - Vujčić, Zoran
AU  - Margetić, Aleksandra
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6388
AB  - Poly(γ-glutamic acid) (PGA), naturally produced by Bacillus species, is a biodegradable, non-toxic, biocompatible, and non-immunogenic negatively charged polymer. Due to its properties, it has found various applications in the food, cosmetic and pharmaceutical industries. In this work, Bacillus subtilis 17B was selected as the best PGA producer among fifty wild-types Bacillus strains tested and characterized as a glutamate-independent producer. The production of PGA by the newly identified strain was optimized and increased tenfold using the Box-Behnken experimental design. The purity of PGA after recovery and purification from the fermentation broth was confirmed by SDS-PAGE followed by Methylene Blue staining. PGA was characterized by ESI MS and used for the preparation of a new nanocomposite with TiO2. The synthesis of PGA/TiO2 nanocomposite, its structural analysis, and cytotoxic effect on the cervical cancer cell line (HeLa cell) was investigated to determine the potential anti-cancer usage of this newly prepared material. Encouraging, PGA/TiO2 nanocomposite showed an increased cytotoxic effect compared to TiO2 alone.
AB  - Поли(γ-глутаминска киселина) (ПГK), коју производе бактерије рода Bacillus, је биоразградив, нетоксичан, биокомпатибилан и неимуноген негативно наелектрисани полимер. Због својих својстава нашао је разноврсну примену у прехрамбеној, козметичкој и фармацеутској индустрији. У овом раду, Bacillus ѕubtilis 17Б је изабран као најбољи ПГК продуцер међу педесетак тестираних природних изолата бактерија из овог рода и окарактерисан као глутамат независтан продуцер. Производња ПГК овим новоидентификованим сојем је оптимизована и десетоструко увећана коришћењем Box-Behnken експерименталног дизајна. Чистоћа ПГК након изоловања и пречишћавања из ферметационе течности је потврђена електрофорезом (SDS-PAGE) након бојења метиленским плавим. ПГК је окарактерисана масеном спекроскопијом (ESI MS) и коришћена за добијање новог нанокомпозита са ТiО2. Синтеза ПГК/ТiО2 нанокомпозита, његова структурна анализа и цитотоксични ефекат на ћелијску линију рака грлића материце (HeLa ћелије) је испитан да би се утврдила потенцијална употреба овог новодобијеног материјала у борби против ћелија рака. Нанокомпозит ПГК/ТiО2показао је повећан цитотоксични ефекат на поменуте ћелије рака у поређењу са самим ТiО2.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - A novel PGA/TiO2 nanocomposite prepared with poly(γ-glutamic acid) from the newly isolated Bacillus subtilis 17B strain
T1  - Нови ПГК/TiO2 нанокомпозит добијен од поли(γ -глутаминске киселине) из новоизолованог соја bacillus subtilis 17B
DO  - 10.2298/JSC221116011S
ER  - 

@article{
author = "Šokarda Slavić, Marinela and Ralić, Vanja and Nastasijević, Branislav and Matijević, Milica and Vujčić, Zoran and Margetić, Aleksandra",
year = "2023",
abstract = "Poly(γ-glutamic acid) (PGA), naturally produced by Bacillus species, is a biodegradable, non-toxic, biocompatible, and non-immunogenic negatively charged polymer. Due to its properties, it has found various applications in the food, cosmetic and pharmaceutical industries. In this work, Bacillus subtilis 17B was selected as the best PGA producer among fifty wild-types Bacillus strains tested and characterized as a glutamate-independent producer. The production of PGA by the newly identified strain was optimized and increased tenfold using the Box-Behnken experimental design. The purity of PGA after recovery and purification from the fermentation broth was confirmed by SDS-PAGE followed by Methylene Blue staining. PGA was characterized by ESI MS and used for the preparation of a new nanocomposite with TiO2. The synthesis of PGA/TiO2 nanocomposite, its structural analysis, and cytotoxic effect on the cervical cancer cell line (HeLa cell) was investigated to determine the potential anti-cancer usage of this newly prepared material. Encouraging, PGA/TiO2 nanocomposite showed an increased cytotoxic effect compared to TiO2 alone., Поли(γ-глутаминска киселина) (ПГK), коју производе бактерије рода Bacillus, је биоразградив, нетоксичан, биокомпатибилан и неимуноген негативно наелектрисани полимер. Због својих својстава нашао је разноврсну примену у прехрамбеној, козметичкој и фармацеутској индустрији. У овом раду, Bacillus ѕubtilis 17Б је изабран као најбољи ПГК продуцер међу педесетак тестираних природних изолата бактерија из овог рода и окарактерисан као глутамат независтан продуцер. Производња ПГК овим новоидентификованим сојем је оптимизована и десетоструко увећана коришћењем Box-Behnken експерименталног дизајна. Чистоћа ПГК након изоловања и пречишћавања из ферметационе течности је потврђена електрофорезом (SDS-PAGE) након бојења метиленским плавим. ПГК је окарактерисана масеном спекроскопијом (ESI MS) и коришћена за добијање новог нанокомпозита са ТiО2. Синтеза ПГК/ТiО2 нанокомпозита, његова структурна анализа и цитотоксични ефекат на ћелијску линију рака грлића материце (HeLa ћелије) је испитан да би се утврдила потенцијална употреба овог новодобијеног материјала у борби против ћелија рака. Нанокомпозит ПГК/ТiО2показао је повећан цитотоксични ефекат на поменуте ћелије рака у поређењу са самим ТiО2.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "A novel PGA/TiO2 nanocomposite prepared with poly(γ-glutamic acid) from the newly isolated Bacillus subtilis 17B strain, Нови ПГК/TiO2 нанокомпозит добијен од поли(γ -глутаминске киселине) из новоизолованог соја bacillus subtilis 17B",
doi = "10.2298/JSC221116011S"
}

Šokarda Slavić, M., Ralić, V., Nastasijević, B., Matijević, M., Vujčić, Z.,& Margetić, A.. (2023). A novel PGA/TiO2 nanocomposite prepared with poly(γ-glutamic acid) from the newly isolated Bacillus subtilis 17B strain. in Journal of the Serbian Chemical Society
Serbian Chemical Society..
https://doi.org/10.2298/JSC221116011S

Šokarda Slavić M, Ralić V, Nastasijević B, Matijević M, Vujčić Z, Margetić A. A novel PGA/TiO2 nanocomposite prepared with poly(γ-glutamic acid) from the newly isolated Bacillus subtilis 17B strain. in Journal of the Serbian Chemical Society. 2023;.
doi:10.2298/JSC221116011S .

Šokarda Slavić, Marinela, Ralić, Vanja, Nastasijević, Branislav, Matijević, Milica, Vujčić, Zoran, Margetić, Aleksandra, "A novel PGA/TiO2 nanocomposite prepared with poly(γ-glutamic acid) from the newly isolated Bacillus subtilis 17B strain" in Journal of the Serbian Chemical Society (2023),
https://doi.org/10.2298/JSC221116011S . .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Margetić, Aleksandra
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Mišić, Milan
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5796
AB  - Bioethanol is one of the main bio-based molecules produced mainly from sugar cane, molasses and corn. Its environmental advantages allow it to be considered as safe and the cleanest fuel alternative. Starch is a widespread renewable carbohydrate conventionally used for bioethanol production via energy demanding liquefaction and saccharification processes. Raw starch hydrolysis using enzymes capable of degrading it below the gelatinization temperature significantly simplifies the process and reduces the cost of starch processing. In this study, an innovative modified simultaneous saccharification and fermentation process is proposed for the production of bioethanol from highly concentrated raw corn starch (30 % w/v). A two-step synergistic hydrolysis and fermentation was carried out in a single bioreactor vessel. To ensure high process efficiency, factors influencing the hydrolysis of concentrated raw corn starch by raw starch degrading α-amylase from Bacillus paralicheniformis ATCC 9945a (BliAmy) and commercial glucoamylase were investigated. Box–Behnken experimental design was used to predict the effects of different ratios of added enzymes, glucoamylase addition time, incubation time, and pH on hydrolysis yield. Optimal conditions for the highest yield of hydrolysis of raw corn starch (90 %) were obtained after 8 h using 5.0 IU BliAmy per mg of starch and 0.5 % (v/v) glucoamylase at pH 4.5 and 60 °C. Obtained glucose was further fermented with Saccharomyces cerevisiae at 30 °C in the same vessel for bioethanol production. Bioethanol concentration at 129.2 g/L, with productivity of 2.94 g/L/h and ethanol yield (YP/S) at 0.50 g EtOH/g total sugar, equivalent to 87.8 % theoretical yield, was obtained by modified simultaneous saccharification and fermentation. This work enriches the information of bioethanol production and offers a novel strategy for raw starch hydrolysis under industrial conditions.
T2  - Fuel
T1  - Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch
VL  - 338
SP  - 127363
DO  - 10.1016/j.fuel.2022.127363
ER  - 

@article{
author = "Šokarda Slavić, Marinela and Margetić, Aleksandra and Dojnov, Biljana and Vujčić, Miroslava and Mišić, Milan and Božić, Nataša and Vujčić, Zoran",
year = "2023",
abstract = "Bioethanol is one of the main bio-based molecules produced mainly from sugar cane, molasses and corn. Its environmental advantages allow it to be considered as safe and the cleanest fuel alternative. Starch is a widespread renewable carbohydrate conventionally used for bioethanol production via energy demanding liquefaction and saccharification processes. Raw starch hydrolysis using enzymes capable of degrading it below the gelatinization temperature significantly simplifies the process and reduces the cost of starch processing. In this study, an innovative modified simultaneous saccharification and fermentation process is proposed for the production of bioethanol from highly concentrated raw corn starch (30 % w/v). A two-step synergistic hydrolysis and fermentation was carried out in a single bioreactor vessel. To ensure high process efficiency, factors influencing the hydrolysis of concentrated raw corn starch by raw starch degrading α-amylase from Bacillus paralicheniformis ATCC 9945a (BliAmy) and commercial glucoamylase were investigated. Box–Behnken experimental design was used to predict the effects of different ratios of added enzymes, glucoamylase addition time, incubation time, and pH on hydrolysis yield. Optimal conditions for the highest yield of hydrolysis of raw corn starch (90 %) were obtained after 8 h using 5.0 IU BliAmy per mg of starch and 0.5 % (v/v) glucoamylase at pH 4.5 and 60 °C. Obtained glucose was further fermented with Saccharomyces cerevisiae at 30 °C in the same vessel for bioethanol production. Bioethanol concentration at 129.2 g/L, with productivity of 2.94 g/L/h and ethanol yield (YP/S) at 0.50 g EtOH/g total sugar, equivalent to 87.8 % theoretical yield, was obtained by modified simultaneous saccharification and fermentation. This work enriches the information of bioethanol production and offers a novel strategy for raw starch hydrolysis under industrial conditions.",
journal = "Fuel",
title = "Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch",
volume = "338",
pages = "127363",
doi = "10.1016/j.fuel.2022.127363"
}

Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel, 338, 127363.
https://doi.org/10.1016/j.fuel.2022.127363

Šokarda Slavić M, Margetić A, Dojnov B, Vujčić M, Mišić M, Božić N, Vujčić Z. Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel. 2023;338:127363.
doi:10.1016/j.fuel.2022.127363 .

Šokarda Slavić, Marinela, Margetić, Aleksandra, Dojnov, Biljana, Vujčić, Miroslava, Mišić, Milan, Božić, Nataša, Vujčić, Zoran, "Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch" in Fuel, 338 (2023):127363,
https://doi.org/10.1016/j.fuel.2022.127363 . .

TY  - DATA
AU  - Šokarda Slavić, Marinela
AU  - Margetić, Aleksandra
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Mišić, Milan
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5836
AB  - Bioethanol is one of the main bio-based molecules produced mainly from sugar cane, molasses and corn. Its environmental advantages allow it to be considered as safe and the cleanest fuel alternative. Starch is a widespread renewable carbohydrate conventionally used for bioethanol production via energy demanding liquefaction and saccharification processes. Raw starch hydrolysis using enzymes capable of degrading it below the gelatinization temperature significantly simplifies the process and reduces the cost of starch processing. In this study, an innovative modified simultaneous saccharification and fermentation process is proposed for the production of bioethanol from highly concentrated raw corn starch (30 % w/v). A two-step synergistic hydrolysis and fermentation was carried out in a single bioreactor vessel. To ensure high process efficiency, factors influencing the hydrolysis of concentrated raw corn starch by raw starch degrading α-amylase from Bacillus paralicheniformis ATCC 9945a (BliAmy) and commercial glucoamylase were investigated. Box–Behnken experimental design was used to predict the effects of different ratios of added enzymes, glucoamylase addition time, incubation time, and pH on hydrolysis yield. Optimal conditions for the highest yield of hydrolysis of raw corn starch (90 %) were obtained after 8 h using 5.0 IU BliAmy per mg of starch and 0.5 % (v/v) glucoamylase at pH 4.5 and 60 °C. Obtained glucose was further fermented with Saccharomyces cerevisiae at 30 °C in the same vessel for bioethanol production. Bioethanol concentration at 129.2 g/L, with productivity of 2.94 g/L/h and ethanol yield (YP/S) at 0.50 g EtOH/g total sugar, equivalent to 87.8 % theoretical yield, was obtained by modified simultaneous saccharification and fermentation. This work enriches the information of bioethanol production and offers a novel strategy for raw starch hydrolysis under industrial conditions.
T2  - Fuel
T1  - Supplementary material for: Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel, 338, 127363. https://doi.org/10.1016/j.fuel.2022.127363
VL  - 338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5836
ER  - 

@misc{
author = "Šokarda Slavić, Marinela and Margetić, Aleksandra and Dojnov, Biljana and Vujčić, Miroslava and Mišić, Milan and Božić, Nataša and Vujčić, Zoran",
year = "2023",
abstract = "Bioethanol is one of the main bio-based molecules produced mainly from sugar cane, molasses and corn. Its environmental advantages allow it to be considered as safe and the cleanest fuel alternative. Starch is a widespread renewable carbohydrate conventionally used for bioethanol production via energy demanding liquefaction and saccharification processes. Raw starch hydrolysis using enzymes capable of degrading it below the gelatinization temperature significantly simplifies the process and reduces the cost of starch processing. In this study, an innovative modified simultaneous saccharification and fermentation process is proposed for the production of bioethanol from highly concentrated raw corn starch (30 % w/v). A two-step synergistic hydrolysis and fermentation was carried out in a single bioreactor vessel. To ensure high process efficiency, factors influencing the hydrolysis of concentrated raw corn starch by raw starch degrading α-amylase from Bacillus paralicheniformis ATCC 9945a (BliAmy) and commercial glucoamylase were investigated. Box–Behnken experimental design was used to predict the effects of different ratios of added enzymes, glucoamylase addition time, incubation time, and pH on hydrolysis yield. Optimal conditions for the highest yield of hydrolysis of raw corn starch (90 %) were obtained after 8 h using 5.0 IU BliAmy per mg of starch and 0.5 % (v/v) glucoamylase at pH 4.5 and 60 °C. Obtained glucose was further fermented with Saccharomyces cerevisiae at 30 °C in the same vessel for bioethanol production. Bioethanol concentration at 129.2 g/L, with productivity of 2.94 g/L/h and ethanol yield (YP/S) at 0.50 g EtOH/g total sugar, equivalent to 87.8 % theoretical yield, was obtained by modified simultaneous saccharification and fermentation. This work enriches the information of bioethanol production and offers a novel strategy for raw starch hydrolysis under industrial conditions.",
journal = "Fuel",
title = "Supplementary material for: Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel, 338, 127363. https://doi.org/10.1016/j.fuel.2022.127363",
volume = "338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5836"
}

Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Supplementary material for: Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel, 338, 127363. https://doi.org/10.1016/j.fuel.2022.127363. in Fuel, 338.
https://hdl.handle.net/21.15107/rcub_cherry_5836

Šokarda Slavić M, Margetić A, Dojnov B, Vujčić M, Mišić M, Božić N, Vujčić Z. Supplementary material for: Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel, 338, 127363. https://doi.org/10.1016/j.fuel.2022.127363. in Fuel. 2023;338.
https://hdl.handle.net/21.15107/rcub_cherry_5836 .

Šokarda Slavić, Marinela, Margetić, Aleksandra, Dojnov, Biljana, Vujčić, Miroslava, Mišić, Milan, Božić, Nataša, Vujčić, Zoran, "Supplementary material for: Šokarda Slavić, M., Margetić, A., Dojnov, B., Vujčić, M., Mišić, M., Božić, N.,& Vujčić, Z.. (2023). Modified simultaneous saccharification and fermentation for the production of bioethanol from highly concentrated raw corn starch. in Fuel, 338, 127363. https://doi.org/10.1016/j.fuel.2022.127363" in Fuel, 338 (2023),
https://hdl.handle.net/21.15107/rcub_cherry_5836 .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Pavlović, Marija
AU  - Nikolić, Stefan
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5992
AB  - The combination ofb-oligosaccharides from enzymatically hydrolysed barleyb-glucan has attracted inter-est recently due to its positive effects on human health. This study aimed to assess the impact of theendo-b-1,3-1,4-glucanase enzyme fromBacillus  subtilis168 on improving the nutritional and bioactiveproperties of barleyb-glucan. A new procedure for the isolation ofb-glucan was developed, at a lowertemperature (45°C), enabling purity from starch contamination, without affecting the yield (6 gb-glucanfrom 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned intoE. colipQE_Ek enables the highproduction and purification (82% yield, 1.8 mg mL 1and 440 U mg 1) of an enzyme identical to thenatural one (25.5 kDa). The enzymatic reaction showed high efficiency ofb-glucan degradation by recom-binant enzyme, giving a mixture of products (of which 3-O-b-cellobiosyl-D-glucose and 3-O-b-cellotriosyl-D-glucose are the most abundant), the reduction of viscosity (17%) and increase in antioxidant capacitiesby 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicatethe possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barleyb-glucan used as functional foods.
PB  - Wiley
T2  - International Journal of Food Science and Technology
T1  - Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase
VL  - 58
IS  - 12
SP  - 6825
EP  - 6835
DO  - 10.1111/ijfs.16647
ER  - 

@article{
author = "Šokarda Slavić, Marinela and Kojić, Milan and Margetić, Aleksandra and Ristović, Marina and Pavlović, Marija and Nikolić, Stefan and Vujčić, Zoran",
year = "2023",
abstract = "The combination ofb-oligosaccharides from enzymatically hydrolysed barleyb-glucan has attracted inter-est recently due to its positive effects on human health. This study aimed to assess the impact of theendo-b-1,3-1,4-glucanase enzyme fromBacillus  subtilis168 on improving the nutritional and bioactiveproperties of barleyb-glucan. A new procedure for the isolation ofb-glucan was developed, at a lowertemperature (45°C), enabling purity from starch contamination, without affecting the yield (6 gb-glucanfrom 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned intoE. colipQE_Ek enables the highproduction and purification (82% yield, 1.8 mg mL 1and 440 U mg 1) of an enzyme identical to thenatural one (25.5 kDa). The enzymatic reaction showed high efficiency ofb-glucan degradation by recom-binant enzyme, giving a mixture of products (of which 3-O-b-cellobiosyl-D-glucose and 3-O-b-cellotriosyl-D-glucose are the most abundant), the reduction of viscosity (17%) and increase in antioxidant capacitiesby 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicatethe possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barleyb-glucan used as functional foods.",
publisher = "Wiley",
journal = "International Journal of Food Science and Technology",
title = "Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase",
volume = "58",
number = "12",
pages = "6825-6835",
doi = "10.1111/ijfs.16647"
}

Šokarda Slavić, M., Kojić, M., Margetić, A., Ristović, M., Pavlović, M., Nikolić, S.,& Vujčić, Z.. (2023). Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase. in International Journal of Food Science and Technology
Wiley., 58(12), 6825-6835.
https://doi.org/10.1111/ijfs.16647

Šokarda Slavić M, Kojić M, Margetić A, Ristović M, Pavlović M, Nikolić S, Vujčić Z. Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase. in International Journal of Food Science and Technology. 2023;58(12):6825-6835.
doi:10.1111/ijfs.16647 .

Šokarda Slavić, Marinela, Kojić, Milan, Margetić, Aleksandra, Ristović, Marina, Pavlović, Marija, Nikolić, Stefan, Vujčić, Zoran, "Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase" in International Journal of Food Science and Technology, 58, no. 12 (2023):6825-6835,
https://doi.org/10.1111/ijfs.16647 . .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Pavlović, Marija
AU  - Nikolić, Stefan
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6008
AB  - The combination ofb-oligosaccharides from enzymatically hydrolysed barleyb-glucan has attracted inter-est recently due to its positive effects on human health. This study aimed to assess the impact of theendo-b-1,3-1,4-glucanase enzyme fromBacillus  subtilis168 on improving the nutritional and bioactiveproperties of barleyb-glucan. A new procedure for the isolation ofb-glucan was developed, at a lowertemperature (45°C), enabling purity from starch contamination, without affecting the yield (6 gb-glucanfrom 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned intoE. colipQE_Ek enables the highproduction and purification (82% yield, 1.8 mg mL 1and 440 U mg 1) of an enzyme identical to thenatural one (25.5 kDa). The enzymatic reaction showed high efficiency ofb-glucan degradation by recom-binant enzyme, giving a mixture of products (of which 3-O-b-cellobiosyl-D-glucose and 3-O-b-cellotriosyl-D-glucose are the most abundant), the reduction of viscosity (17%) and increase in antioxidant capacitiesby 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicatethe possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barleyb-glucan used as functional foods.
PB  - Wiley
T2  - International Journal of Food Science and Technology
T1  - Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase
VL  - 58
IS  - 12
SP  - 6825
EP  - 6835
DO  - 10.1111/ijfs.16647
ER  - 

@article{
author = "Šokarda Slavić, Marinela and Kojić, Milan and Margetić, Aleksandra and Ristović, Marina and Pavlović, Marija and Nikolić, Stefan and Vujčić, Zoran",
year = "2023",
abstract = "The combination ofb-oligosaccharides from enzymatically hydrolysed barleyb-glucan has attracted inter-est recently due to its positive effects on human health. This study aimed to assess the impact of theendo-b-1,3-1,4-glucanase enzyme fromBacillus  subtilis168 on improving the nutritional and bioactiveproperties of barleyb-glucan. A new procedure for the isolation ofb-glucan was developed, at a lowertemperature (45°C), enabling purity from starch contamination, without affecting the yield (6 gb-glucanfrom 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned intoE. colipQE_Ek enables the highproduction and purification (82% yield, 1.8 mg mL 1and 440 U mg 1) of an enzyme identical to thenatural one (25.5 kDa). The enzymatic reaction showed high efficiency ofb-glucan degradation by recom-binant enzyme, giving a mixture of products (of which 3-O-b-cellobiosyl-D-glucose and 3-O-b-cellotriosyl-D-glucose are the most abundant), the reduction of viscosity (17%) and increase in antioxidant capacitiesby 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicatethe possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barleyb-glucan used as functional foods.",
publisher = "Wiley",
journal = "International Journal of Food Science and Technology",
title = "Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase",
volume = "58",
number = "12",
pages = "6825-6835",
doi = "10.1111/ijfs.16647"
}

Šokarda Slavić, M., Kojić, M., Margetić, A., Ristović, M., Pavlović, M., Nikolić, S.,& Vujčić, Z.. (2023). Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase. in International Journal of Food Science and Technology
Wiley., 58(12), 6825-6835.
https://doi.org/10.1111/ijfs.16647

Šokarda Slavić M, Kojić M, Margetić A, Ristović M, Pavlović M, Nikolić S, Vujčić Z. Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase. in International Journal of Food Science and Technology. 2023;58(12):6825-6835.
doi:10.1111/ijfs.16647 .

Šokarda Slavić, Marinela, Kojić, Milan, Margetić, Aleksandra, Ristović, Marina, Pavlović, Marija, Nikolić, Stefan, Vujčić, Zoran, "Improvement of nutritional and bioactive properties of barleyb-glucan-based food products usingBacillus subtilis168endo-b-1,3-1,4-glucanase" in International Journal of Food Science and Technology, 58, no. 12 (2023):6825-6835,
https://doi.org/10.1111/ijfs.16647 . .

TY  - JOUR
AU  - Stojanović, Sanja
AU  - Ristović, Marina
AU  - Stepanović, Jelena
AU  - Margetić, Aleksandra
AU  - Duduk, Bojan
AU  - Vujčić, Zoran
AU  - Dojnov, Biljana
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5517
AB  - Production of fructooligosaccharides (FOS) is a trending topic due to their prebiotic effect becoming increasingly important for the modern human diet. The most suitable process for FOS production is the one using fungal inulinases. Introduction of new fungal inulinase producers and their implementation in production of inulinase enzymes is therefore gaining interest. This study provides a new approach to FOS synthesis by fungal enzyme complex without prior separation of any specific enzyme. Inulinase enzyme complexes could be used for the synthesis of FOS in two possible ways – hydrolysis of inulin (FOSh) and transfructosylation process of sucrose (FOSs), as demonstrated here. Depending on the fungal growth inducing substrate, a variety of inulinase enzyme complexes was obtained – one of which was most successful in production of FOSh and another one of FOSs. Substrates derived from crops: triticale, wheat bran, Jerusalem artichoke and Aspergillus welwitschiae isolate, previously proven as safe for use in food, were utilized for production of inulinase enzyme cocktails. The highest FOSs production was obtained by enzyme complex rich in β-fructofuranosidase, while the highest FOSh production was obtained by enzyme complex rich in endoinulinase. Both FOSh and FOSs showed antioxidant potential according to ABTS and ORAC, which classifies them as a suitable additive in functional food. Simultaneous zymographic detection of inulinase enzymes, which could contribute to expansion of the knowledge on fungal enzymes, was developed and applied here. It demonstrated the presence of different inulinase isoforms depending on fungal growth substrate. These findings, which rely on the innate ability of fungi to co-produce all inulinases from a cocktail, could be useful as a new, easy approach to FOS production by fungal enzymes without their separation and purification, contributing to cheaper and faster production processes.
PB  - Elsevier
T2  - Food Research International
T2  - Food Research International
T1  - Aspergillus welwitschiae inulinase enzyme cocktails obtained on agro-material inducers for the purpose of fructooligosaccharides production
VL  - 160
DO  - 10.1016/j.foodres.2022.111755
ER  - 

@article{
author = "Stojanović, Sanja and Ristović, Marina and Stepanović, Jelena and Margetić, Aleksandra and Duduk, Bojan and Vujčić, Zoran and Dojnov, Biljana",
year = "2022",
abstract = "Production of fructooligosaccharides (FOS) is a trending topic due to their prebiotic effect becoming increasingly important for the modern human diet. The most suitable process for FOS production is the one using fungal inulinases. Introduction of new fungal inulinase producers and their implementation in production of inulinase enzymes is therefore gaining interest. This study provides a new approach to FOS synthesis by fungal enzyme complex without prior separation of any specific enzyme. Inulinase enzyme complexes could be used for the synthesis of FOS in two possible ways – hydrolysis of inulin (FOSh) and transfructosylation process of sucrose (FOSs), as demonstrated here. Depending on the fungal growth inducing substrate, a variety of inulinase enzyme complexes was obtained – one of which was most successful in production of FOSh and another one of FOSs. Substrates derived from crops: triticale, wheat bran, Jerusalem artichoke and Aspergillus welwitschiae isolate, previously proven as safe for use in food, were utilized for production of inulinase enzyme cocktails. The highest FOSs production was obtained by enzyme complex rich in β-fructofuranosidase, while the highest FOSh production was obtained by enzyme complex rich in endoinulinase. Both FOSh and FOSs showed antioxidant potential according to ABTS and ORAC, which classifies them as a suitable additive in functional food. Simultaneous zymographic detection of inulinase enzymes, which could contribute to expansion of the knowledge on fungal enzymes, was developed and applied here. It demonstrated the presence of different inulinase isoforms depending on fungal growth substrate. These findings, which rely on the innate ability of fungi to co-produce all inulinases from a cocktail, could be useful as a new, easy approach to FOS production by fungal enzymes without their separation and purification, contributing to cheaper and faster production processes.",
publisher = "Elsevier",
journal = "Food Research International, Food Research International",
title = "Aspergillus welwitschiae inulinase enzyme cocktails obtained on agro-material inducers for the purpose of fructooligosaccharides production",
volume = "160",
doi = "10.1016/j.foodres.2022.111755"
}

Stojanović, S., Ristović, M., Stepanović, J., Margetić, A., Duduk, B., Vujčić, Z.,& Dojnov, B.. (2022). Aspergillus welwitschiae inulinase enzyme cocktails obtained on agro-material inducers for the purpose of fructooligosaccharides production. in Food Research International
Elsevier., 160.
https://doi.org/10.1016/j.foodres.2022.111755

Stojanović S, Ristović M, Stepanović J, Margetić A, Duduk B, Vujčić Z, Dojnov B. Aspergillus welwitschiae inulinase enzyme cocktails obtained on agro-material inducers for the purpose of fructooligosaccharides production. in Food Research International. 2022;160.
doi:10.1016/j.foodres.2022.111755 .

Stojanović, Sanja, Ristović, Marina, Stepanović, Jelena, Margetić, Aleksandra, Duduk, Bojan, Vujčić, Zoran, Dojnov, Biljana, "Aspergillus welwitschiae inulinase enzyme cocktails obtained on agro-material inducers for the purpose of fructooligosaccharides production" in Food Research International, 160 (2022),
https://doi.org/10.1016/j.foodres.2022.111755 . .

TY  - CONF
AU  - Pavlović, Marija
AU  - Margetić, Aleksandra
AU  - Šokarda Slavić, Marinela
AU  - Ristović, Marina
AU  - Pavlović, Ratko
AU  - Nikolić, Stefan
AU  - Vujčić, Zoran
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5862
AB  - Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices1. One of the biggest problems in the production of fruit juices is the turbidity of the juice, which is mainly caused by the presence of pectin polysaccharides. Therefore, pectinase is used in juice clarification, which breaks down the pectin structure and reduces unwanted cloudiness and sediment2. In this work, the production of pectinases was optimized by solid state fermentation using Aspergillus tubingensis strain, which proved to be an efficient producer of these enzymes. Statistical method Design of Experiment was used to optimize the medium and conditions for enzyme production. The total pectinase activity obtained was determined by the DNS method (47 U/mL). Endo-pectinases activity is determined by reduction of viscosity of pectin solutions. The resulting complex of pectinase enzymes was used for the liquefaction of apricot and blueberry pulp, with a juice yield of 72% and 81%, respectively. Also, apricot juice treated with enzymes was clarified by 77% compared to juice that was not treated with enzymes. Blueberry juice obtained after treatment with pectinase enzymes has a higher antioxidant activity than the untreated juice, as determined by the DPPH assay.
PB  - University of Belgrade - Faculty of Chemistry
PB  - Belgrade : Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference: Scientific meeting of an international character  “Amazing Biochemistry”, September 22nd and 23rd, 2022, Novi Sad, Serbia
T1  - Production and application of pectinases in the liquefaction of apricot and blueberry juice
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5862
ER  - 

@conference{
author = "Pavlović, Marija and Margetić, Aleksandra and Šokarda Slavić, Marinela and Ristović, Marina and Pavlović, Ratko and Nikolić, Stefan and Vujčić, Zoran",
year = "2022",
abstract = "Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices1. One of the biggest problems in the production of fruit juices is the turbidity of the juice, which is mainly caused by the presence of pectin polysaccharides. Therefore, pectinase is used in juice clarification, which breaks down the pectin structure and reduces unwanted cloudiness and sediment2. In this work, the production of pectinases was optimized by solid state fermentation using Aspergillus tubingensis strain, which proved to be an efficient producer of these enzymes. Statistical method Design of Experiment was used to optimize the medium and conditions for enzyme production. The total pectinase activity obtained was determined by the DNS method (47 U/mL). Endo-pectinases activity is determined by reduction of viscosity of pectin solutions. The resulting complex of pectinase enzymes was used for the liquefaction of apricot and blueberry pulp, with a juice yield of 72% and 81%, respectively. Also, apricot juice treated with enzymes was clarified by 77% compared to juice that was not treated with enzymes. Blueberry juice obtained after treatment with pectinase enzymes has a higher antioxidant activity than the untreated juice, as determined by the DPPH assay.",
publisher = "University of Belgrade - Faculty of Chemistry, Belgrade : Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference: Scientific meeting of an international character  “Amazing Biochemistry”, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Production and application of pectinases in the liquefaction of apricot and blueberry juice",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5862"
}

Pavlović, M., Margetić, A., Šokarda Slavić, M., Ristović, M., Pavlović, R., Nikolić, S.,& Vujčić, Z.. (2022). Production and application of pectinases in the liquefaction of apricot and blueberry juice. in Serbian Biochemical Society Eleventh Conference: Scientific meeting of an international character  “Amazing Biochemistry”, September 22nd and 23rd, 2022, Novi Sad, Serbia
University of Belgrade - Faculty of Chemistry..
https://hdl.handle.net/21.15107/rcub_cherry_5862

Pavlović M, Margetić A, Šokarda Slavić M, Ristović M, Pavlović R, Nikolić S, Vujčić Z. Production and application of pectinases in the liquefaction of apricot and blueberry juice. in Serbian Biochemical Society Eleventh Conference: Scientific meeting of an international character  “Amazing Biochemistry”, September 22nd and 23rd, 2022, Novi Sad, Serbia. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5862 .

Pavlović, Marija, Margetić, Aleksandra, Šokarda Slavić, Marinela, Ristović, Marina, Pavlović, Ratko, Nikolić, Stefan, Vujčić, Zoran, "Production and application of pectinases in the liquefaction of apricot and blueberry juice" in Serbian Biochemical Society Eleventh Conference: Scientific meeting of an international character  “Amazing Biochemistry”, September 22nd and 23rd, 2022, Novi Sad, Serbia (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5862 .

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Nikolić, Stefan
AU  - Grgurić-Šipka, Sanja
AU  - Vujčić, Miroslava
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5859
AB  - The interaction of four arene ruthenium
complexes [(η6-p-cymene)Ru(Me2dppz)Cl]PF6 (1)
with Me2dppz
= 11,12-dimethyldipyrido[3,2-a:2′,3′-c]
phenazine, [(η6-p-cymene)Ru(aip)Cl]PF6 (2) with
aip = 2-(9-anthryl)-1H-imidazo[4,5-f][1,10] phenanthroline),
([(ƞ6-toluene)Ru(ppf)Cl]PF6) (3) and ([(ƞ6-pcymene)
Ru(ppf)Cl]PF6) (4) with ppf = pyrido[2′,3′:5,6]
pyrazino[2,3-f][1,10]phenanthroline with calf thymus
DNA were investigated. All of four complexes exhibit
DNA-binding activity. UV–Vis spectroscopic studies
revealed the intrinsic binding constants of the order
104
M−
1 of magnitude, indicating non-intercalative
mode. Fluorescence quenching analysis showed that all
complexes interfere with intercalator ethidium bromide
and minor groove binder Hoechst 33258 by a singular
non-intercalative mode with extent that differs by two
orders of magnitude. Gel electrophoresis results on DNA cleavage assay demonstrated that all complexes
produced conformational changes of supercoiled
circular plasmid pUC19 in concentration dependent
way. The results of fluorescence titration bovine
serum albumin by 1, 2, 3 and 4 showed that all complexes
significantly quench tryptophan residues fluorescence
through a static quenching mechanism. The
antimicrobial activity against both Gram-positive and
Gram-negative bacteria analyzed. Complex 1 was most
active, even on Escherichia coli was more active than
positive control compound.
T2  - Biometals
T1  - Interaction of organoruthenium(II)-polypyridyl complexes with DNA and BSA
VL  - 35
SP  - 813
EP  - 829
DO  - 10.1007/s10534-022-00404-6
ER  - 

@article{
author = "Margetić, Aleksandra and Nikolić, Stefan and Grgurić-Šipka, Sanja and Vujčić, Miroslava",
year = "2022",
abstract = "The interaction of four arene ruthenium
complexes [(η6-p-cymene)Ru(Me2dppz)Cl]PF6 (1)
with Me2dppz
= 11,12-dimethyldipyrido[3,2-a:2′,3′-c]
phenazine, [(η6-p-cymene)Ru(aip)Cl]PF6 (2) with
aip = 2-(9-anthryl)-1H-imidazo[4,5-f][1,10] phenanthroline),
([(ƞ6-toluene)Ru(ppf)Cl]PF6) (3) and ([(ƞ6-pcymene)
Ru(ppf)Cl]PF6) (4) with ppf = pyrido[2′,3′:5,6]
pyrazino[2,3-f][1,10]phenanthroline with calf thymus
DNA were investigated. All of four complexes exhibit
DNA-binding activity. UV–Vis spectroscopic studies
revealed the intrinsic binding constants of the order
104
M−
1 of magnitude, indicating non-intercalative
mode. Fluorescence quenching analysis showed that all
complexes interfere with intercalator ethidium bromide
and minor groove binder Hoechst 33258 by a singular
non-intercalative mode with extent that differs by two
orders of magnitude. Gel electrophoresis results on DNA cleavage assay demonstrated that all complexes
produced conformational changes of supercoiled
circular plasmid pUC19 in concentration dependent
way. The results of fluorescence titration bovine
serum albumin by 1, 2, 3 and 4 showed that all complexes
significantly quench tryptophan residues fluorescence
through a static quenching mechanism. The
antimicrobial activity against both Gram-positive and
Gram-negative bacteria analyzed. Complex 1 was most
active, even on Escherichia coli was more active than
positive control compound.",
journal = "Biometals",
title = "Interaction of organoruthenium(II)-polypyridyl complexes with DNA and BSA",
volume = "35",
pages = "813-829",
doi = "10.1007/s10534-022-00404-6"
}

Margetić, A., Nikolić, S., Grgurić-Šipka, S.,& Vujčić, M.. (2022). Interaction of organoruthenium(II)-polypyridyl complexes with DNA and BSA. in Biometals, 35, 813-829.
https://doi.org/10.1007/s10534-022-00404-6

Margetić A, Nikolić S, Grgurić-Šipka S, Vujčić M. Interaction of organoruthenium(II)-polypyridyl complexes with DNA and BSA. in Biometals. 2022;35:813-829.
doi:10.1007/s10534-022-00404-6 .

Margetić, Aleksandra, Nikolić, Stefan, Grgurić-Šipka, Sanja, Vujčić, Miroslava, "Interaction of organoruthenium(II)-polypyridyl complexes with DNA and BSA" in Biometals, 35 (2022):813-829,
https://doi.org/10.1007/s10534-022-00404-6 . .

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Stojanović, Sanja
AU  - Ristović, Marina
AU  - Vujčić, Zoran
AU  - Dojnov, Biljana
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4801
AB  - There is an urgent need to increase the daily intake of insoluble dietary fiber, and at the same time to find new sources and new production technologies. We hypothesized that fungal enzymes directly involved in lignocellulosic material hydrolysis (Aspergillus and Trichoderma enzyme cocktails) will change the fiber structure particularly efficiently after the action of laccase (Trametes versicolor enzyme cocktail). Enzymes production on an inducing substrate (same as starting material for obtainment of insoluble dietary fibers) and their usage resulted in obtainment of novel insoluble dietary fibers with better characteristics, 24% higher swelling, 43% higher WRC and 57% higher ORC compared to insoluble dietary fibers from triticale (already proven to be a good food additive). Changes in structure were analyzed by FTIR and microscopic analysis. Antioxidative performance of the obtained products, new insoluble and released soluble dietary fibers, was analyzed in detail. Newly obtained soluble dietary fibers demonstrated up to 20 times higher antioxidant activity compared to untreated fibers (ABTS and DPPH tests). These results suggest their good performance as a future food additive. At the same time, they prove the hypothesis that the use of enzyme cocktails rich in laccase is a good choice for biological pretreatment in this process.
PB  - Elsevier
T2  - LWT - Food Science and Technology
T1  - Fungal oxidative and hydrolyzing enzymes as designers in the biological production of dietary fibers from triticale
VL  - 145
SP  - 111291
DO  - 10.1016/j.lwt.2021.111291
ER  - 

@article{
author = "Margetić, Aleksandra and Stojanović, Sanja and Ristović, Marina and Vujčić, Zoran and Dojnov, Biljana",
year = "2021",
abstract = "There is an urgent need to increase the daily intake of insoluble dietary fiber, and at the same time to find new sources and new production technologies. We hypothesized that fungal enzymes directly involved in lignocellulosic material hydrolysis (Aspergillus and Trichoderma enzyme cocktails) will change the fiber structure particularly efficiently after the action of laccase (Trametes versicolor enzyme cocktail). Enzymes production on an inducing substrate (same as starting material for obtainment of insoluble dietary fibers) and their usage resulted in obtainment of novel insoluble dietary fibers with better characteristics, 24% higher swelling, 43% higher WRC and 57% higher ORC compared to insoluble dietary fibers from triticale (already proven to be a good food additive). Changes in structure were analyzed by FTIR and microscopic analysis. Antioxidative performance of the obtained products, new insoluble and released soluble dietary fibers, was analyzed in detail. Newly obtained soluble dietary fibers demonstrated up to 20 times higher antioxidant activity compared to untreated fibers (ABTS and DPPH tests). These results suggest their good performance as a future food additive. At the same time, they prove the hypothesis that the use of enzyme cocktails rich in laccase is a good choice for biological pretreatment in this process.",
publisher = "Elsevier",
journal = "LWT - Food Science and Technology",
title = "Fungal oxidative and hydrolyzing enzymes as designers in the biological production of dietary fibers from triticale",
volume = "145",
pages = "111291",
doi = "10.1016/j.lwt.2021.111291"
}

Margetić, A., Stojanović, S., Ristović, M., Vujčić, Z.,& Dojnov, B.. (2021). Fungal oxidative and hydrolyzing enzymes as designers in the biological production of dietary fibers from triticale. in LWT - Food Science and Technology
Elsevier., 145, 111291.
https://doi.org/10.1016/j.lwt.2021.111291

Margetić A, Stojanović S, Ristović M, Vujčić Z, Dojnov B. Fungal oxidative and hydrolyzing enzymes as designers in the biological production of dietary fibers from triticale. in LWT - Food Science and Technology. 2021;145:111291.
doi:10.1016/j.lwt.2021.111291 .

Margetić, Aleksandra, Stojanović, Sanja, Ristović, Marina, Vujčić, Zoran, Dojnov, Biljana, "Fungal oxidative and hydrolyzing enzymes as designers in the biological production of dietary fibers from triticale" in LWT - Food Science and Technology, 145 (2021):111291,
https://doi.org/10.1016/j.lwt.2021.111291 . .

TY  - DATA
AU  - Margetić, Aleksandra
AU  - Stojanović, Sanja
AU  - Ristović, Marina
AU  - Vujčić, Zoran
AU  - Dojnov, Biljana
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4802
PB  - Elsevier
T2  - LWT - Food Science and Technology
T1  - Supplementary data for the article: Margetić, A.; Stojanović, S.; Ristović, M.; Vujčić, Z.; Dojnov, B. Fungal Oxidative and Hydrolyzing Enzymes as Designers in the Biological Production of Dietary Fibers from Triticale. LWT 2021, 145, 111291. https://doi.org/10.1016/j.lwt.2021.111291.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4802
ER  - 

@misc{
author = "Margetić, Aleksandra and Stojanović, Sanja and Ristović, Marina and Vujčić, Zoran and Dojnov, Biljana",
year = "2021",
publisher = "Elsevier",
journal = "LWT - Food Science and Technology",
title = "Supplementary data for the article: Margetić, A.; Stojanović, S.; Ristović, M.; Vujčić, Z.; Dojnov, B. Fungal Oxidative and Hydrolyzing Enzymes as Designers in the Biological Production of Dietary Fibers from Triticale. LWT 2021, 145, 111291. https://doi.org/10.1016/j.lwt.2021.111291.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4802"
}

Margetić, A., Stojanović, S., Ristović, M., Vujčić, Z.,& Dojnov, B.. (2021). Supplementary data for the article: Margetić, A.; Stojanović, S.; Ristović, M.; Vujčić, Z.; Dojnov, B. Fungal Oxidative and Hydrolyzing Enzymes as Designers in the Biological Production of Dietary Fibers from Triticale. LWT 2021, 145, 111291. https://doi.org/10.1016/j.lwt.2021.111291.. in LWT - Food Science and Technology
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4802

Margetić A, Stojanović S, Ristović M, Vujčić Z, Dojnov B. Supplementary data for the article: Margetić, A.; Stojanović, S.; Ristović, M.; Vujčić, Z.; Dojnov, B. Fungal Oxidative and Hydrolyzing Enzymes as Designers in the Biological Production of Dietary Fibers from Triticale. LWT 2021, 145, 111291. https://doi.org/10.1016/j.lwt.2021.111291.. in LWT - Food Science and Technology. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4802 .

Margetić, Aleksandra, Stojanović, Sanja, Ristović, Marina, Vujčić, Zoran, Dojnov, Biljana, "Supplementary data for the article: Margetić, A.; Stojanović, S.; Ristović, M.; Vujčić, Z.; Dojnov, B. Fungal Oxidative and Hydrolyzing Enzymes as Designers in the Biological Production of Dietary Fibers from Triticale. LWT 2021, 145, 111291. https://doi.org/10.1016/j.lwt.2021.111291." in LWT - Food Science and Technology (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4802 .

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2433
AB  - Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Preparative Biochemistry and Biotechnology
T1  - Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae
VL  - 47
IS  - 3
SP  - 305
EP  - 311
DO  - 10.1080/10826068.2016.1244683
ER  - 

@article{
author = "Margetić, Aleksandra and Vujčić, Zoran",
year = "2017",
abstract = "Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60 degrees C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60 degrees C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70 degrees C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Preparative Biochemistry and Biotechnology",
title = "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae",
volume = "47",
number = "3",
pages = "305-311",
doi = "10.1080/10826068.2016.1244683"
}

Margetić, A.,& Vujčić, Z.. (2017). Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae. in Preparative Biochemistry and Biotechnology
Taylor & Francis Inc, Philadelphia., 47(3), 305-311.
https://doi.org/10.1080/10826068.2016.1244683

Margetić A, Vujčić Z. Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae. in Preparative Biochemistry and Biotechnology. 2017;47(3):305-311.
doi:10.1080/10826068.2016.1244683 .

Margetić, Aleksandra, Vujčić, Zoran, "Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae" in Preparative Biochemistry and Biotechnology, 47, no. 3 (2017):305-311,
https://doi.org/10.1080/10826068.2016.1244683 . .

TY  - JOUR
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2390
AB  - Cell wall invertase (CWI) from Saccharomyces cerevisiae was immobilized in polyacrylamide hydrogels. The aim of the development of a new biocatalyst was to obtain an improved enzyme for invert sugar production. The monomer concentration and enzyme amount in the immobilizate were optimized, and the obtained biocatalyst had an enzyme activity of 138 +/- 6 IU g(-1). The pH and temperature optima were 4.0 and 70 degrees C, respectively. The stability of immobilized enzyme was determined at several temperatures in the absence of substrate and the half-life obtained at 50 degrees C was 81 days, at 60 degrees C, 128 min and at 70 degrees C, 1.24 min. The biocatalyst was tested at low pH values, 3.0 and 3.5 were tested, and showed great stability. The KM values were 34.1 +/- 1.7 and 126.2 +/- 6.3 mM for free and immobilized CWI, respectively. The activation energies were 37.7 and 23.0 kJ mol(-1) for free and immobilized CWI, respectively. Cell wall invertase immobilized in polyacrylamide hydrogel (CWI-PAA) was tested for the production of high concentrated invert sugar in a batch and a packed bed reactor. After five days of continuous process, the quality and characteristics of the produced invert sugar remained unchanged.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Immobilization of cell wall invertase in a polyacrylamide hydrogel for invert sugar production
VL  - 81
IS  - 12
SP  - 1359
EP  - 1369
DO  - 10.2298/JSC160720094M
ER  - 

@article{
author = "Margetić, Aleksandra and Vujčić, Zoran",
year = "2016",
abstract = "Cell wall invertase (CWI) from Saccharomyces cerevisiae was immobilized in polyacrylamide hydrogels. The aim of the development of a new biocatalyst was to obtain an improved enzyme for invert sugar production. The monomer concentration and enzyme amount in the immobilizate were optimized, and the obtained biocatalyst had an enzyme activity of 138 +/- 6 IU g(-1). The pH and temperature optima were 4.0 and 70 degrees C, respectively. The stability of immobilized enzyme was determined at several temperatures in the absence of substrate and the half-life obtained at 50 degrees C was 81 days, at 60 degrees C, 128 min and at 70 degrees C, 1.24 min. The biocatalyst was tested at low pH values, 3.0 and 3.5 were tested, and showed great stability. The KM values were 34.1 +/- 1.7 and 126.2 +/- 6.3 mM for free and immobilized CWI, respectively. The activation energies were 37.7 and 23.0 kJ mol(-1) for free and immobilized CWI, respectively. Cell wall invertase immobilized in polyacrylamide hydrogel (CWI-PAA) was tested for the production of high concentrated invert sugar in a batch and a packed bed reactor. After five days of continuous process, the quality and characteristics of the produced invert sugar remained unchanged.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Immobilization of cell wall invertase in a polyacrylamide hydrogel for invert sugar production",
volume = "81",
number = "12",
pages = "1359-1369",
doi = "10.2298/JSC160720094M"
}

Margetić, A.,& Vujčić, Z.. (2016). Immobilization of cell wall invertase in a polyacrylamide hydrogel for invert sugar production. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 81(12), 1359-1369.
https://doi.org/10.2298/JSC160720094M

Margetić A, Vujčić Z. Immobilization of cell wall invertase in a polyacrylamide hydrogel for invert sugar production. in Journal of the Serbian Chemical Society. 2016;81(12):1359-1369.
doi:10.2298/JSC160720094M .

Margetić, Aleksandra, Vujčić, Zoran, "Immobilization of cell wall invertase in a polyacrylamide hydrogel for invert sugar production" in Journal of the Serbian Chemical Society, 81, no. 12 (2016):1359-1369,
https://doi.org/10.2298/JSC160720094M . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Janović, Barbara
AU  - Lončar, Nikola L.
AU  - Margetić, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1644
AB  - Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP CIA while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those isoenzymes for removal of recalcitrant pollutants such as reactive dyes. Results demonstrated that not only these enzymes can decolorize dyes but also in some cases anionic forms are more efficient than commercially produced cationic HRP form. Enzyme concentration of 0.14 U ml(-1) was found to provide maximum dye removal at optimized reaction conditions with dye concentration of 30 mg I-1. Majority of dyes tested were successfully decolorized at pH 5 or 7 while some dyes like Orange 2 and Reactive black 5 are decolorized most efficiently at pH 9. Anionic isoenzymes act by disrupting chromophore of Reactive black 5 while cationic HRP oxidize dye but leaves chromophore present. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization
VL  - 97
SP  - 124
EP  - 127
DO  - 10.1016/j.ibiod.2014.10.007
ER  - 

@article{
author = "Vujčić, Zoran and Janović, Barbara and Lončar, Nikola L. and Margetić, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava",
year = "2015",
abstract = "Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP CIA while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those isoenzymes for removal of recalcitrant pollutants such as reactive dyes. Results demonstrated that not only these enzymes can decolorize dyes but also in some cases anionic forms are more efficient than commercially produced cationic HRP form. Enzyme concentration of 0.14 U ml(-1) was found to provide maximum dye removal at optimized reaction conditions with dye concentration of 30 mg I-1. Majority of dyes tested were successfully decolorized at pH 5 or 7 while some dyes like Orange 2 and Reactive black 5 are decolorized most efficiently at pH 9. Anionic isoenzymes act by disrupting chromophore of Reactive black 5 while cationic HRP oxidize dye but leaves chromophore present. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization",
volume = "97",
pages = "124-127",
doi = "10.1016/j.ibiod.2014.10.007"
}

Vujčić, Z., Janović, B., Lončar, N. L., Margetić, A., Božić, N., Dojnov, B.,& Vujčić, M.. (2015). Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 97, 124-127.
https://doi.org/10.1016/j.ibiod.2014.10.007

Vujčić Z, Janović B, Lončar NL, Margetić A, Božić N, Dojnov B, Vujčić M. Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization. in International Biodeterioration and Biodegradation. 2015;97:124-127.
doi:10.1016/j.ibiod.2014.10.007 .

Vujčić, Zoran, Janović, Barbara, Lončar, Nikola L., Margetić, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, "Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization" in International Biodeterioration and Biodegradation, 97 (2015):124-127,
https://doi.org/10.1016/j.ibiod.2014.10.007 . .

TY  - JOUR
AU  - Tamaš, Nenad
AU  - Dojnov, Biljana
AU  - Margetić, Aleksandra
AU  - Vujčić, Miroslava
AU  - Spirović, Bojana
AU  - Miletić, Novica
AU  - Stević, Milan
AU  - Vujčić, Zoran
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1711
AB  - Introduction. Aphis pomi (De Geer) has developed resistance to organophosphate and carbamate insecticides, as a result of long-term application of these insecticides in conventional apple orchards. For many years, the only mechanism of resistance identified in aphids was overproduction of insecticide-detoxifying esterases. Materials and methods. Insecticide resistance of A. pomi, collected from two conventional apple orchards (localities of Radmilovac-RA and Bela Crkva-BC) and one organic apple orchard (locality of Surcin-SU), was tested by bioassays and biochemical assays. Results and discussion. Compared with LC50 values for the susceptible population (organic orchard), both populations from the conventional orchards were highly resistant to pirimicarb (234.5 and 52.9 times) and moderately resistant to dimethoate (10.7 and 9.0 times). Increased esterase activity was determined in these two resistant aphid populations. Each of them also produced one esterase isoform more than the susceptible population, when 1-naphthyl acetate was used as a substrate for zymographic detection; when 2-naphthyl acetate was used as a substrate, only one resistant population produced two new esterase isoforms. In one of the resistant populations acetylcholinesterase (AChE) was significantly less inhibited by pirimicarb than in the other resistant population and the susceptible population, which indicates that this population developed another resistance mechanism-Modification of AChE (MACE). Conclusion. Detoxification of insecticides by the metabolic resistance mechanism of esterase enzymes and mechanism of modification of AChE was proven in one aphid population (RA). The other population (BC) has developed only metabolic resistance (enhanced metabolism by esterases), without modification of the insecticide target site (AChE). Development of insecticide resistance was caused by long-term application of acetylcholinesterase inhibitors (organophosphates and carbamates) in these conventional orchards.
PB  - Edp Sciences S A, Les Ulis Cedex A
T2  - Fruits
T1  - Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)
VL  - 70
IS  - 3
SP  - 135
EP  - 142
DO  - 10.1051/fruits/2015005
ER  - 

@article{
author = "Tamaš, Nenad and Dojnov, Biljana and Margetić, Aleksandra and Vujčić, Miroslava and Spirović, Bojana and Miletić, Novica and Stević, Milan and Vujčić, Zoran",
year = "2015",
abstract = "Introduction. Aphis pomi (De Geer) has developed resistance to organophosphate and carbamate insecticides, as a result of long-term application of these insecticides in conventional apple orchards. For many years, the only mechanism of resistance identified in aphids was overproduction of insecticide-detoxifying esterases. Materials and methods. Insecticide resistance of A. pomi, collected from two conventional apple orchards (localities of Radmilovac-RA and Bela Crkva-BC) and one organic apple orchard (locality of Surcin-SU), was tested by bioassays and biochemical assays. Results and discussion. Compared with LC50 values for the susceptible population (organic orchard), both populations from the conventional orchards were highly resistant to pirimicarb (234.5 and 52.9 times) and moderately resistant to dimethoate (10.7 and 9.0 times). Increased esterase activity was determined in these two resistant aphid populations. Each of them also produced one esterase isoform more than the susceptible population, when 1-naphthyl acetate was used as a substrate for zymographic detection; when 2-naphthyl acetate was used as a substrate, only one resistant population produced two new esterase isoforms. In one of the resistant populations acetylcholinesterase (AChE) was significantly less inhibited by pirimicarb than in the other resistant population and the susceptible population, which indicates that this population developed another resistance mechanism-Modification of AChE (MACE). Conclusion. Detoxification of insecticides by the metabolic resistance mechanism of esterase enzymes and mechanism of modification of AChE was proven in one aphid population (RA). The other population (BC) has developed only metabolic resistance (enhanced metabolism by esterases), without modification of the insecticide target site (AChE). Development of insecticide resistance was caused by long-term application of acetylcholinesterase inhibitors (organophosphates and carbamates) in these conventional orchards.",
publisher = "Edp Sciences S A, Les Ulis Cedex A",
journal = "Fruits",
title = "Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)",
volume = "70",
number = "3",
pages = "135-142",
doi = "10.1051/fruits/2015005"
}

Tamaš, N., Dojnov, B., Margetić, A., Vujčić, M., Spirović, B., Miletić, N., Stević, M.,& Vujčić, Z.. (2015). Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae). in Fruits
Edp Sciences S A, Les Ulis Cedex A., 70(3), 135-142.
https://doi.org/10.1051/fruits/2015005

Tamaš N, Dojnov B, Margetić A, Vujčić M, Spirović B, Miletić N, Stević M, Vujčić Z. Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae). in Fruits. 2015;70(3):135-142.
doi:10.1051/fruits/2015005 .

Tamaš, Nenad, Dojnov, Biljana, Margetić, Aleksandra, Vujčić, Miroslava, Spirović, Bojana, Miletić, Novica, Stević, Milan, Vujčić, Zoran, "Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)" in Fruits, 70, no. 3 (2015):135-142,
https://doi.org/10.1051/fruits/2015005 . .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Pavlovic, Ratko
AU  - Božić, Nataša
AU  - Margetić, Aleksandra
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1627
AB  - The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
T1  - Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition
VL  - 164
IS  - 4
SP  - 259
EP  - 267
DO  - 10.1016/j.cbpb.2013.02.001
ER  - 

@article{
author = "Dojnov, Biljana and Pavlovic, Ratko and Božić, Nataša and Margetić, Aleksandra and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2013",
abstract = "The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology",
title = "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition",
volume = "164",
number = "4",
pages = "259-267",
doi = "10.1016/j.cbpb.2013.02.001"
}

Dojnov, B., Pavlovic, R., Božić, N., Margetić, A., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2013). Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 164(4), 259-267.
https://doi.org/10.1016/j.cbpb.2013.02.001

Dojnov B, Pavlovic R, Božić N, Margetić A, Nenadovic V, Ivanovic J, Vujčić Z. Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology. 2013;164(4):259-267.
doi:10.1016/j.cbpb.2013.02.001 .

Dojnov, Biljana, Pavlovic, Ratko, Božić, Nataša, Margetić, Aleksandra, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition" in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 164, no. 4 (2013):259-267,
https://doi.org/10.1016/j.cbpb.2013.02.001 . .

TY  - CONF
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1416
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Thermal stability and energy of deactivation of immobilized cell wall invertase in natural and synthetic hydrogel polymers
VL  - 280
SP  - 103
EP  - 103
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1416
ER  - 

@conference{
author = "Margetić, Aleksandra and Vujčić, Zoran",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Thermal stability and energy of deactivation of immobilized cell wall invertase in natural and synthetic hydrogel polymers",
volume = "280",
pages = "103-103",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1416"
}

Margetić, A.,& Vujčić, Z.. (2013). Thermal stability and energy of deactivation of immobilized cell wall invertase in natural and synthetic hydrogel polymers. in FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 280, 103-103.
https://hdl.handle.net/21.15107/rcub_cherry_1416

Margetić A, Vujčić Z. Thermal stability and energy of deactivation of immobilized cell wall invertase in natural and synthetic hydrogel polymers. in FEBS Journal / Federation of European of Biochemical Societies. 2013;280:103-103.
https://hdl.handle.net/21.15107/rcub_cherry_1416 .

Margetić, Aleksandra, Vujčić, Zoran, "Thermal stability and energy of deactivation of immobilized cell wall invertase in natural and synthetic hydrogel polymers" in FEBS Journal / Federation of European of Biochemical Societies, 280 (2013):103-103,
https://hdl.handle.net/21.15107/rcub_cherry_1416 .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Vujčić, Zoran
AU  - Božić, Nataša
AU  - Margetić, Aleksandra
AU  - Vujčić, Miroslava
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1263
AB  - Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.
PB  - Springer, Dordrecht
T2  - Journal of Insect Conservation
T1  - Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study
VL  - 16
IS  - 2
SP  - 239
EP  - 247
DO  - 10.1007/s10841-011-9411-x
ER  - 

@article{
author = "Dojnov, Biljana and Vujčić, Zoran and Božić, Nataša and Margetić, Aleksandra and Vujčić, Miroslava and Nenadovic, Vera and Ivanovic, Jelisaveta",
year = "2012",
abstract = "Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.",
publisher = "Springer, Dordrecht",
journal = "Journal of Insect Conservation",
title = "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study",
volume = "16",
number = "2",
pages = "239-247",
doi = "10.1007/s10841-011-9411-x"
}

Dojnov, B., Vujčić, Z., Božić, N., Margetić, A., Vujčić, M., Nenadovic, V.,& Ivanovic, J.. (2012). Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation
Springer, Dordrecht., 16(2), 239-247.
https://doi.org/10.1007/s10841-011-9411-x

Dojnov B, Vujčić Z, Božić N, Margetić A, Vujčić M, Nenadovic V, Ivanovic J. Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation. 2012;16(2):239-247.
doi:10.1007/s10841-011-9411-x .

Dojnov, Biljana, Vujčić, Zoran, Božić, Nataša, Margetić, Aleksandra, Vujčić, Miroslava, Nenadovic, Vera, Ivanovic, Jelisaveta, "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study" in Journal of Insect Conservation, 16, no. 2 (2012):239-247,
https://doi.org/10.1007/s10841-011-9411-x . .