TY  - JOUR
AU  - Kosić, Višnja
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Banković, Predrag
AU  - Jović-Jovičić, Nataša
AU  - Knežević-Jugović, Zorica
AU  - Milutinović Nikolić, Aleksandra
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7525
AB  - Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.
PB  - Elsevier
T2  - Applied Clay Science
T1  - Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite
VL  - 250
SP  - 107289
DO  - 10.1016/j.clay.2024.107289
ER  - 

@article{
author = "Kosić, Višnja and Božić, Nataša and Dojnov, Biljana and Banković, Predrag and Jović-Jovičić, Nataša and Knežević-Jugović, Zorica and Milutinović Nikolić, Aleksandra",
year = "2024",
abstract = "Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.",
publisher = "Elsevier",
journal = "Applied Clay Science",
title = "Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite",
volume = "250",
pages = "107289",
doi = "10.1016/j.clay.2024.107289"
}

Kosić, V., Božić, N., Dojnov, B., Banković, P., Jović-Jovičić, N., Knežević-Jugović, Z.,& Milutinović Nikolić, A.. (2024). Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. in Applied Clay Science
Elsevier., 250, 107289.
https://doi.org/10.1016/j.clay.2024.107289

Kosić V, Božić N, Dojnov B, Banković P, Jović-Jovičić N, Knežević-Jugović Z, Milutinović Nikolić A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. in Applied Clay Science. 2024;250:107289.
doi:10.1016/j.clay.2024.107289 .

Kosić, Višnja, Božić, Nataša, Dojnov, Biljana, Banković, Predrag, Jović-Jovičić, Nataša, Knežević-Jugović, Zorica, Milutinović Nikolić, Aleksandra, "Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite" in Applied Clay Science, 250 (2024):107289,
https://doi.org/10.1016/j.clay.2024.107289 . .

TY  - CONF
AU  - Kosić, Višnja
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Stevanović, Gordana
AU  - Banković, Predrag
AU  - Milutinović Nikolić, Aleksandra
AU  - Knežević-Jugović, Zorica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6846
AB  - Clays are naturally occurring, environmentally friendly, chemically inert, thermostable, inexpensive resources that are easily modified into materials with tailored properties. As such, they can be used as suitable supports for enzyme immobilization and application in the food industry. Natural polysaccharides starch, xylan, pullulan, and its derivatives obtained by the action of enzymes, have numerous potentials for food industrial applications. In this work the enzyme supports were prepared from bentonite from Coal mine "Bogovina", Serbia by acid activation (AA), pillaring (P), and pillaring followed by acid activation (PAA). The characterization of the obtained materials included chemical and phase composition, surface acidity, and textural properties. After characterization, -amylase from Bacillus paralicheniformis (BliAmy), commercial xylanase from Sigma-Aldrich (Xyl), and pullulanase from B. paralicheniformis (BliPull) were immobilized on bentonite based supports by 24 h adsorption at 25 °C. The obtained biocatalysts BliAmy-AA (106 IU/g), Xyl-P (74 IU/g), and BliPull-PAA (45 IU/g) showed very good storage stability with the activity preserved after 4 weeks of testing. Products of hydrolysis were detected by TLC and indicate a promising application in the food industry.
PB  - Belgrade : Serbian Chemical Society
C3  - Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia, 2023, 210-210
T1  - Stable, environmentally friendly and inexpensive biocatalysts for obtaining important ingredients applicable in the food industry
SP  - 210
EP  - 210
UR  - https://hdl.handle.net/21.15107/rcub_cer_6846
ER  - 

@conference{
author = "Kosić, Višnja and Božić, Nataša and Dojnov, Biljana and Stevanović, Gordana and Banković, Predrag and Milutinović Nikolić, Aleksandra and Knežević-Jugović, Zorica",
year = "2023",
abstract = "Clays are naturally occurring, environmentally friendly, chemically inert, thermostable, inexpensive resources that are easily modified into materials with tailored properties. As such, they can be used as suitable supports for enzyme immobilization and application in the food industry. Natural polysaccharides starch, xylan, pullulan, and its derivatives obtained by the action of enzymes, have numerous potentials for food industrial applications. In this work the enzyme supports were prepared from bentonite from Coal mine "Bogovina", Serbia by acid activation (AA), pillaring (P), and pillaring followed by acid activation (PAA). The characterization of the obtained materials included chemical and phase composition, surface acidity, and textural properties. After characterization, -amylase from Bacillus paralicheniformis (BliAmy), commercial xylanase from Sigma-Aldrich (Xyl), and pullulanase from B. paralicheniformis (BliPull) were immobilized on bentonite based supports by 24 h adsorption at 25 °C. The obtained biocatalysts BliAmy-AA (106 IU/g), Xyl-P (74 IU/g), and BliPull-PAA (45 IU/g) showed very good storage stability with the activity preserved after 4 weeks of testing. Products of hydrolysis were detected by TLC and indicate a promising application in the food industry.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia, 2023, 210-210",
title = "Stable, environmentally friendly and inexpensive biocatalysts for obtaining important ingredients applicable in the food industry",
pages = "210-210",
url = "https://hdl.handle.net/21.15107/rcub_cer_6846"
}

Kosić, V., Božić, N., Dojnov, B., Stevanović, G., Banković, P., Milutinović Nikolić, A.,& Knežević-Jugović, Z.. (2023). Stable, environmentally friendly and inexpensive biocatalysts for obtaining important ingredients applicable in the food industry. in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia, 2023, 210-210
Belgrade : Serbian Chemical Society., 210-210.
https://hdl.handle.net/21.15107/rcub_cer_6846

Kosić V, Božić N, Dojnov B, Stevanović G, Banković P, Milutinović Nikolić A, Knežević-Jugović Z. Stable, environmentally friendly and inexpensive biocatalysts for obtaining important ingredients applicable in the food industry. in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia, 2023, 210-210. 2023;:210-210.
https://hdl.handle.net/21.15107/rcub_cer_6846 .

Kosić, Višnja, Božić, Nataša, Dojnov, Biljana, Stevanović, Gordana, Banković, Predrag, Milutinović Nikolić, Aleksandra, Knežević-Jugović, Zorica, "Stable, environmentally friendly and inexpensive biocatalysts for obtaining important ingredients applicable in the food industry" in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia, 2023, 210-210 (2023):210-210,
https://hdl.handle.net/21.15107/rcub_cer_6846 .

TY  - CONF
AU  - Kosić, Višnja
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Stevanović, Gordana
AU  - Milutinović Nikolić, Aleksandra
AU  - Knežević-Jugović, Zorica
AU  - Banković, Predrag
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6030
AB  - Some coal mines suffer from problem of having huge deposits of bentonite that they regard as undesirable, since bentonite can cause problem due to its swelling property. Instead of piling stacks of bentonite and regarding it as ecological problem the bentonite can be used as enzyme support by immobilization of enzymes as the challenging new application in the field of biotechnology. The enzyme catalysts in the industrial application present lower energy costs and are more environmentally friendly in comparison to traditional chemical processes. The advantages of enzymes are even more prominent when enzymes are applied in immobilized form. In this work the enzyme supports were prepared from bentonite from Coal mine "Bogovina", Serbia where bentonite, although valuable resource, is still considered to be tailings. Bentonite was modified by common methods: acid activation (AA), pillaring (P), and pillaring followed by acid activation (PAA) and tested as enzyme support. All the obtained materials were characterized by the X-ray powder diffraction and FTIR spectroscopy. The amylase, xylanase, and pullulanase were immobilized on different bentonite based supports by 24 h adsorption at 25 °C. The experimental results revealed that under the investigated conditions AA, P, and PAA, were the most suitable for amylase (106 IU/g), xylanase (74 IU/g), and pullulanase (45 IU/g) immobilization, respectively.
PB  - European Federation of Biotechnology
C3  - Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online
T1  - The tailings from coal mine instead of waste became applicable as enzyme supports
SP  - 65
EP  - 65
UR  - https://hdl.handle.net/21.15107/rcub_cer_6030
ER  - 

@conference{
author = "Kosić, Višnja and Božić, Nataša and Dojnov, Biljana and Stevanović, Gordana and Milutinović Nikolić, Aleksandra and Knežević-Jugović, Zorica and Banković, Predrag",
year = "2023",
abstract = "Some coal mines suffer from problem of having huge deposits of bentonite that they regard as undesirable, since bentonite can cause problem due to its swelling property. Instead of piling stacks of bentonite and regarding it as ecological problem the bentonite can be used as enzyme support by immobilization of enzymes as the challenging new application in the field of biotechnology. The enzyme catalysts in the industrial application present lower energy costs and are more environmentally friendly in comparison to traditional chemical processes. The advantages of enzymes are even more prominent when enzymes are applied in immobilized form. In this work the enzyme supports were prepared from bentonite from Coal mine "Bogovina", Serbia where bentonite, although valuable resource, is still considered to be tailings. Bentonite was modified by common methods: acid activation (AA), pillaring (P), and pillaring followed by acid activation (PAA) and tested as enzyme support. All the obtained materials were characterized by the X-ray powder diffraction and FTIR spectroscopy. The amylase, xylanase, and pullulanase were immobilized on different bentonite based supports by 24 h adsorption at 25 °C. The experimental results revealed that under the investigated conditions AA, P, and PAA, were the most suitable for amylase (106 IU/g), xylanase (74 IU/g), and pullulanase (45 IU/g) immobilization, respectively.",
publisher = "European Federation of Biotechnology",
journal = "Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online",
title = "The tailings from coal mine instead of waste became applicable as enzyme supports",
pages = "65-65",
url = "https://hdl.handle.net/21.15107/rcub_cer_6030"
}

Kosić, V., Božić, N., Dojnov, B., Stevanović, G., Milutinović Nikolić, A., Knežević-Jugović, Z.,& Banković, P.. (2023). The tailings from coal mine instead of waste became applicable as enzyme supports. in Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online
European Federation of Biotechnology., 65-65.
https://hdl.handle.net/21.15107/rcub_cer_6030

Kosić V, Božić N, Dojnov B, Stevanović G, Milutinović Nikolić A, Knežević-Jugović Z, Banković P. The tailings from coal mine instead of waste became applicable as enzyme supports. in Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online. 2023;:65-65.
https://hdl.handle.net/21.15107/rcub_cer_6030 .

Kosić, Višnja, Božić, Nataša, Dojnov, Biljana, Stevanović, Gordana, Milutinović Nikolić, Aleksandra, Knežević-Jugović, Zorica, Banković, Predrag, "The tailings from coal mine instead of waste became applicable as enzyme supports" in Programme and abstract book - Biotechnology for a circular bioeconomy: carbon capture, waste recycling and mitigation of global warming, 28-29 March 2023, online (2023):65-65,
https://hdl.handle.net/21.15107/rcub_cer_6030 .

TY  - CONF
AU  - Kosić, Višnja
AU  - Pavlović, Stefan
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Stevanović, Gordana
AU  - Knežević-Jugović, Zorica
AU  - Milutinović Nikolić, Aleksandra
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5925
AB  - α-Amylase from Bacillus paralicheniformis (BliAmy) is a highly efficient raw starch digesting enzyme. Starch is an inexpensive source of many food industrial products. Naturally occurring clay are non-toxic, environmentally friendly and inexpensive. Therefore, immobilization of BliAmy by adsorption on three differently modified bentonites was studied. Modifications included common Na-exchange procedure, acid activation, and alkali activation. The modified clays were characterized by X-ray powder diffraction, mercury intrusion porosimetry and the points of zero charge were determined. The adsorption of the enzyme was significantly influenced by the type of modification of bentonite, being the highest for the acid-activated bentonite with the highest porosity. On the other hand, the highest enzyme activity for immobilized α-amylase was obtained with alkali-modified bentonite (98 U/g), suggesting it as a good candidate for immobilization of α-amylase for application in the food industry.
PB  - The Society of Physical Chemists of Serbia
C3  - Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia
T1  - Immobilization of α-amylase from bacillus paralicheniformis on bentonites
SP  - 161
EP  - 164
UR  - https://hdl.handle.net/21.15107/rcub_cer_5925
ER  - 

@conference{
author = "Kosić, Višnja and Pavlović, Stefan and Božić, Nataša and Dojnov, Biljana and Stevanović, Gordana and Knežević-Jugović, Zorica and Milutinović Nikolić, Aleksandra",
year = "2022",
abstract = "α-Amylase from Bacillus paralicheniformis (BliAmy) is a highly efficient raw starch digesting enzyme. Starch is an inexpensive source of many food industrial products. Naturally occurring clay are non-toxic, environmentally friendly and inexpensive. Therefore, immobilization of BliAmy by adsorption on three differently modified bentonites was studied. Modifications included common Na-exchange procedure, acid activation, and alkali activation. The modified clays were characterized by X-ray powder diffraction, mercury intrusion porosimetry and the points of zero charge were determined. The adsorption of the enzyme was significantly influenced by the type of modification of bentonite, being the highest for the acid-activated bentonite with the highest porosity. On the other hand, the highest enzyme activity for immobilized α-amylase was obtained with alkali-modified bentonite (98 U/g), suggesting it as a good candidate for immobilization of α-amylase for application in the food industry.",
publisher = "The Society of Physical Chemists of Serbia",
journal = "Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia",
title = "Immobilization of α-amylase from bacillus paralicheniformis on bentonites",
pages = "161-164",
url = "https://hdl.handle.net/21.15107/rcub_cer_5925"
}

Kosić, V., Pavlović, S., Božić, N., Dojnov, B., Stevanović, G., Knežević-Jugović, Z.,& Milutinović Nikolić, A.. (2022). Immobilization of α-amylase from bacillus paralicheniformis on bentonites. in Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia
The Society of Physical Chemists of Serbia., 161-164.
https://hdl.handle.net/21.15107/rcub_cer_5925

Kosić V, Pavlović S, Božić N, Dojnov B, Stevanović G, Knežević-Jugović Z, Milutinović Nikolić A. Immobilization of α-amylase from bacillus paralicheniformis on bentonites. in Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia. 2022;:161-164.
https://hdl.handle.net/21.15107/rcub_cer_5925 .

Kosić, Višnja, Pavlović, Stefan, Božić, Nataša, Dojnov, Biljana, Stevanović, Gordana, Knežević-Jugović, Zorica, Milutinović Nikolić, Aleksandra, "Immobilization of α-amylase from bacillus paralicheniformis on bentonites" in Proceedings - 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry, Physical Chemistry 2022, September, 26-30, 2022, Belgrade, Serbia (2022):161-164,
https://hdl.handle.net/21.15107/rcub_cer_5925 .

TY  - CONF
AU  - Pavlović, Stefan
AU  - Kosić, Višnja
AU  - Lončarević, Davor
AU  - Kostić, Milan
AU  - Marinković, Dalibor
PY  - 2022
UR  - https://www.fuelcenter.rwth-aachen.de/cms/Fuelcenter/Austausch/Internationale-Konferenz/~rwsva/10-Internationale-Konferenz-2022/?lidx=1
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5304
AB  - Waste-based CaO was synthesized from chicken eggshell, which calcined form (900 ºC, 5 ºC/min, 4 h) was hydrated (80 ºC, S:L=1:5, 24 h) and rehydrated/calcined (600 ºC, 5 ºC/min, 4 h). The obtained catalyst was characterized (Hg-porosimetry and TPD-CO2) and tested in biodiesel synthesis from off-grade sunflower oil by transesterification to analyse the influence of water addition on reaction intensification. Water content was varied in the range from 1 wt% to 9 wt% by weight of oil. It is shown that water addition positively affects the catalytic activity leading to a reduction in induction time and to faster achievement of the reaction equilibrium (fatty acid methyl esters content > 95%), which for a water content higher than 1 wt% is achieved in 90 min. On the other hand, the equilibrium for the reaction without water addition was achieved considerably later (after 150 min).
PB  - Aachen, Germany : Fuel Science Center, RWTH Aachen University
C3  - Conference report/Book of abstracts-10th International Conference "Fuel Science - From Production to Propulsion"
T1  - Acceleration of biodiesel production from off-grade oil over waste-based CaO catalyst
SP  - 83
EP  - 84
UR  - https://hdl.handle.net/21.15107/rcub_cer_5304
ER  - 

@conference{
author = "Pavlović, Stefan and Kosić, Višnja and Lončarević, Davor and Kostić, Milan and Marinković, Dalibor",
year = "2022",
abstract = "Waste-based CaO was synthesized from chicken eggshell, which calcined form (900 ºC, 5 ºC/min, 4 h) was hydrated (80 ºC, S:L=1:5, 24 h) and rehydrated/calcined (600 ºC, 5 ºC/min, 4 h). The obtained catalyst was characterized (Hg-porosimetry and TPD-CO2) and tested in biodiesel synthesis from off-grade sunflower oil by transesterification to analyse the influence of water addition on reaction intensification. Water content was varied in the range from 1 wt% to 9 wt% by weight of oil. It is shown that water addition positively affects the catalytic activity leading to a reduction in induction time and to faster achievement of the reaction equilibrium (fatty acid methyl esters content > 95%), which for a water content higher than 1 wt% is achieved in 90 min. On the other hand, the equilibrium for the reaction without water addition was achieved considerably later (after 150 min).",
publisher = "Aachen, Germany : Fuel Science Center, RWTH Aachen University",
journal = "Conference report/Book of abstracts-10th International Conference "Fuel Science - From Production to Propulsion"",
title = "Acceleration of biodiesel production from off-grade oil over waste-based CaO catalyst",
pages = "83-84",
url = "https://hdl.handle.net/21.15107/rcub_cer_5304"
}

Pavlović, S., Kosić, V., Lončarević, D., Kostić, M.,& Marinković, D.. (2022). Acceleration of biodiesel production from off-grade oil over waste-based CaO catalyst. in Conference report/Book of abstracts-10th International Conference "Fuel Science - From Production to Propulsion"
Aachen, Germany : Fuel Science Center, RWTH Aachen University., 83-84.
https://hdl.handle.net/21.15107/rcub_cer_5304

Pavlović S, Kosić V, Lončarević D, Kostić M, Marinković D. Acceleration of biodiesel production from off-grade oil over waste-based CaO catalyst. in Conference report/Book of abstracts-10th International Conference "Fuel Science - From Production to Propulsion". 2022;:83-84.
https://hdl.handle.net/21.15107/rcub_cer_5304 .

Pavlović, Stefan, Kosić, Višnja, Lončarević, Davor, Kostić, Milan, Marinković, Dalibor, "Acceleration of biodiesel production from off-grade oil over waste-based CaO catalyst" in Conference report/Book of abstracts-10th International Conference "Fuel Science - From Production to Propulsion" (2022):83-84,
https://hdl.handle.net/21.15107/rcub_cer_5304 .

TY  - CONF
AU  - Pavlović, Stefan
AU  - Kosić, Višnja
AU  - Marinković, Dalibor
AU  - Kostić, Milan
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5307
AB  - The waste fractionated chicken eggshell catalysts were utilized and used in biodiesel production from off-grade sunflower oil. It is confirmed that thermal modification treatment was suitable for conversion of calcite form of eggshell into lime. Fractionation was carried out in the wide particle diameter range from 20 μm. to 100 μm. It is shown that the highest catalytic activity (fatty acid methyl esters content-FAME >96%) was achieved using catalyst obtained from powder faction of >45<63 μm. Important differences in catalytic activity were observed for the boundary fractions (<20 μm, >20<36 μm, and >100 μm), where catalytic activity was greatly reduced. Such behaviour could be explained by mercury intrusion porosimetry results, which indicate the existence of apparent porosity (interparticle and intraparticle) in the mentioned boundary fractions, while in the central fraction (>45<63 μm) the porosity is constant. A poorly-developed system of pores and channels leads to difficult diffusion and inadequate distribution of active centres.
C3  - Proceedings - 2nd International Conference On Green Energy And Environmental Technology
T1  - Biodiesel Production From Off-Grade Oil By Transesterification Over Differently Granulated Waste-Based CaO Catalysts
UR  - https://hdl.handle.net/21.15107/rcub_cer_5307
ER  - 

@conference{
author = "Pavlović, Stefan and Kosić, Višnja and Marinković, Dalibor and Kostić, Milan",
year = "2022",
abstract = "The waste fractionated chicken eggshell catalysts were utilized and used in biodiesel production from off-grade sunflower oil. It is confirmed that thermal modification treatment was suitable for conversion of calcite form of eggshell into lime. Fractionation was carried out in the wide particle diameter range from 20 μm. to 100 μm. It is shown that the highest catalytic activity (fatty acid methyl esters content-FAME >96%) was achieved using catalyst obtained from powder faction of >45<63 μm. Important differences in catalytic activity were observed for the boundary fractions (<20 μm, >20<36 μm, and >100 μm), where catalytic activity was greatly reduced. Such behaviour could be explained by mercury intrusion porosimetry results, which indicate the existence of apparent porosity (interparticle and intraparticle) in the mentioned boundary fractions, while in the central fraction (>45<63 μm) the porosity is constant. A poorly-developed system of pores and channels leads to difficult diffusion and inadequate distribution of active centres.",
journal = "Proceedings - 2nd International Conference On Green Energy And Environmental Technology",
title = "Biodiesel Production From Off-Grade Oil By Transesterification Over Differently Granulated Waste-Based CaO Catalysts",
url = "https://hdl.handle.net/21.15107/rcub_cer_5307"
}

Pavlović, S., Kosić, V., Marinković, D.,& Kostić, M.. (2022). Biodiesel Production From Off-Grade Oil By Transesterification Over Differently Granulated Waste-Based CaO Catalysts. in Proceedings - 2nd International Conference On Green Energy And Environmental Technology.
https://hdl.handle.net/21.15107/rcub_cer_5307

Pavlović S, Kosić V, Marinković D, Kostić M. Biodiesel Production From Off-Grade Oil By Transesterification Over Differently Granulated Waste-Based CaO Catalysts. in Proceedings - 2nd International Conference On Green Energy And Environmental Technology. 2022;.
https://hdl.handle.net/21.15107/rcub_cer_5307 .

Pavlović, Stefan, Kosić, Višnja, Marinković, Dalibor, Kostić, Milan, "Biodiesel Production From Off-Grade Oil By Transesterification Over Differently Granulated Waste-Based CaO Catalysts" in Proceedings - 2nd International Conference On Green Energy And Environmental Technology (2022),
https://hdl.handle.net/21.15107/rcub_cer_5307 .