TY  - CONF
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Stojanović, Sanja
AU  - Pavlović, Marija
AU  - Šokarda Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Dojnov, Biljana
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7813
AB  - Recent technological development has focused on addressing two major global issues: environmental protection and conservation of natural resources. High levels of dye production and use have led to significant environmental concerns due to large quantities of unmanaged colored wastewater. Textile dyes, in particular, are highly reactive and problematic when released into the environment.
This study investigates the use of Aspergillus fungi biomass, a byproduct of enzyme production (xylanase, cellulase, amylase, and other hydrolytic enzymes), for removing textile dyes from wastewater. The strains Aspergillus niger, Aspergillus oryzae, Aspergillus welwitschiae, and Aspergillus tubingensis were cultivated on corn meal under optimized conditions for enzyme production. The adsorption capacity of the biomass was tested on eight textile dyes: Bezaktiv Gelb, Procion reactive yellow, Reactive yellow, Golden yellow, Procion amber, Congo red, Reactive black 5, and Remazol brilliant blue.
The best results were achieved with Aspergillus oryzae biomass, particularly for Reactive black 5. Optimal adsorption conditions identified by DoE were pH 4-5 and a temperature of 25°C. Within the first hour, approximately 90% of the dye (2.16 mg/g biomass) was adsorbed, and after 24 hours, over 99% was adsorbed (2.4 mg/g biomass).
The findings demonstrate that post-enzyme production biomass, typically considered waste, can effectively remove reactive dyes and other xenobiotics from wastewater. This dual benefit reduces waste and mitigates water pollution, contributing significantly to environmental protection.
PB  - Izmir Institute of Technology
C3  - V International Enzyme & Bioprocess Days, Abstract Book, August 27-29, 2024; İzmir, Türkiye
T1  - From Enzyme Production to Environmental Cleanup: The Dual Role of Aspergillus Biomass
SP  - PP40
UR  - https://hdl.handle.net/21.15107/rcub_cer_7813
ER  - 

@conference{
author = "Margetić, Aleksandra and Ristović, Marina and Stojanović, Sanja and Pavlović, Marija and Šokarda Slavić, Marinela and Vujčić, Zoran and Dojnov, Biljana",
year = "2024",
abstract = "Recent technological development has focused on addressing two major global issues: environmental protection and conservation of natural resources. High levels of dye production and use have led to significant environmental concerns due to large quantities of unmanaged colored wastewater. Textile dyes, in particular, are highly reactive and problematic when released into the environment.
This study investigates the use of Aspergillus fungi biomass, a byproduct of enzyme production (xylanase, cellulase, amylase, and other hydrolytic enzymes), for removing textile dyes from wastewater. The strains Aspergillus niger, Aspergillus oryzae, Aspergillus welwitschiae, and Aspergillus tubingensis were cultivated on corn meal under optimized conditions for enzyme production. The adsorption capacity of the biomass was tested on eight textile dyes: Bezaktiv Gelb, Procion reactive yellow, Reactive yellow, Golden yellow, Procion amber, Congo red, Reactive black 5, and Remazol brilliant blue.
The best results were achieved with Aspergillus oryzae biomass, particularly for Reactive black 5. Optimal adsorption conditions identified by DoE were pH 4-5 and a temperature of 25°C. Within the first hour, approximately 90% of the dye (2.16 mg/g biomass) was adsorbed, and after 24 hours, over 99% was adsorbed (2.4 mg/g biomass).
The findings demonstrate that post-enzyme production biomass, typically considered waste, can effectively remove reactive dyes and other xenobiotics from wastewater. This dual benefit reduces waste and mitigates water pollution, contributing significantly to environmental protection.",
publisher = "Izmir Institute of Technology",
journal = "V International Enzyme & Bioprocess Days, Abstract Book, August 27-29, 2024; İzmir, Türkiye",
title = "From Enzyme Production to Environmental Cleanup: The Dual Role of Aspergillus Biomass",
pages = "PP40",
url = "https://hdl.handle.net/21.15107/rcub_cer_7813"
}

Margetić, A., Ristović, M., Stojanović, S., Pavlović, M., Šokarda Slavić, M., Vujčić, Z.,& Dojnov, B.. (2024). From Enzyme Production to Environmental Cleanup: The Dual Role of Aspergillus Biomass. in V International Enzyme & Bioprocess Days, Abstract Book, August 27-29, 2024; İzmir, Türkiye
Izmir Institute of Technology., PP40.
https://hdl.handle.net/21.15107/rcub_cer_7813

Margetić A, Ristović M, Stojanović S, Pavlović M, Šokarda Slavić M, Vujčić Z, Dojnov B. From Enzyme Production to Environmental Cleanup: The Dual Role of Aspergillus Biomass. in V International Enzyme & Bioprocess Days, Abstract Book, August 27-29, 2024; İzmir, Türkiye. 2024;:PP40.
https://hdl.handle.net/21.15107/rcub_cer_7813 .

Margetić, Aleksandra, Ristović, Marina, Stojanović, Sanja, Pavlović, Marija, Šokarda Slavić, Marinela, Vujčić, Zoran, Dojnov, Biljana, "From Enzyme Production to Environmental Cleanup: The Dual Role of Aspergillus Biomass" in V International Enzyme & Bioprocess Days, Abstract Book, August 27-29, 2024; İzmir, Türkiye (2024):PP40,
https://hdl.handle.net/21.15107/rcub_cer_7813 .

TY  - CONF
AU  - Pavlović, Marija
AU  - Kojić, Milan
AU  - Ristović, Marina
AU  - Stojanović, Sanja
AU  - Margetić, Aleksandra
AU  - Vujčić, Zoran
AU  - Šokarda Slavić, Marinela
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7732
AB  - This research deals with the characterization of a thermostable endo-1,4-beta-xylanase enzyme from Anoxybacillus vranjensis ST4, a thermophilic bacterium isolated from Vranjska Banja hot spring, Serbia. The enzyme shows a high degree of identity with the same type of enzyme from other species of the genera Anoxybacillus (97%), Geobacillus (74%) and Paenibacillus (65%). The gene for endo-1,4-beta-xylanase from the thermophilic strain ST4 was cloned into the pQE_Ek expression vector and successfully expressed and purified from the Escherichia coli M15[pREP4]. The study encompasses recombinant production, purification, and the comprehensive characterization of the enzymatic properties of endo-1,4-beta-xylanase. This is the first successful overexpression, purification and characterization of a recombinant thermostable endo-1,4-beta-xylanase enzyme from Anoxybacillus. With a monomeric structure of 38.7 kDa, the enzyme demonstrates peak activity at 70°C and pH 6.5. Notably, it exhibits remarkable stability across a wide pH range and at high temperatures, rendering it suitable for diverse industrial applications. Investigation into the enzyme’s kinetic parameters, substrate specificity, and its ability to degrade xylan into high-energy value products further enhances understanding of its biotechnological potential. These findings underscore the significance of thermophilic bacteria and their thermostable enzymes in various industrial processes.
PB  - Serbian Society for Microbiology
C3  - XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia
T1  - Cloning, overexpression and characterization of a thermostable endo-1,4-beta-xylanase from Anoxybacillus vranjensis ST4
SP  - 31
EP  - 31
UR  - https://hdl.handle.net/21.15107/rcub_cer_7732
ER  - 

@conference{
author = "Pavlović, Marija and Kojić, Milan and Ristović, Marina and Stojanović, Sanja and Margetić, Aleksandra and Vujčić, Zoran and Šokarda Slavić, Marinela",
year = "2024",
abstract = "This research deals with the characterization of a thermostable endo-1,4-beta-xylanase enzyme from Anoxybacillus vranjensis ST4, a thermophilic bacterium isolated from Vranjska Banja hot spring, Serbia. The enzyme shows a high degree of identity with the same type of enzyme from other species of the genera Anoxybacillus (97%), Geobacillus (74%) and Paenibacillus (65%). The gene for endo-1,4-beta-xylanase from the thermophilic strain ST4 was cloned into the pQE_Ek expression vector and successfully expressed and purified from the Escherichia coli M15[pREP4]. The study encompasses recombinant production, purification, and the comprehensive characterization of the enzymatic properties of endo-1,4-beta-xylanase. This is the first successful overexpression, purification and characterization of a recombinant thermostable endo-1,4-beta-xylanase enzyme from Anoxybacillus. With a monomeric structure of 38.7 kDa, the enzyme demonstrates peak activity at 70°C and pH 6.5. Notably, it exhibits remarkable stability across a wide pH range and at high temperatures, rendering it suitable for diverse industrial applications. Investigation into the enzyme’s kinetic parameters, substrate specificity, and its ability to degrade xylan into high-energy value products further enhances understanding of its biotechnological potential. These findings underscore the significance of thermophilic bacteria and their thermostable enzymes in various industrial processes.",
publisher = "Serbian Society for Microbiology",
journal = "XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia",
title = "Cloning, overexpression and characterization of a thermostable endo-1,4-beta-xylanase from Anoxybacillus vranjensis ST4",
pages = "31-31",
url = "https://hdl.handle.net/21.15107/rcub_cer_7732"
}

Pavlović, M., Kojić, M., Ristović, M., Stojanović, S., Margetić, A., Vujčić, Z.,& Šokarda Slavić, M.. (2024). Cloning, overexpression and characterization of a thermostable endo-1,4-beta-xylanase from Anoxybacillus vranjensis ST4. in XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia
Serbian Society for Microbiology., 31-31.
https://hdl.handle.net/21.15107/rcub_cer_7732

Pavlović M, Kojić M, Ristović M, Stojanović S, Margetić A, Vujčić Z, Šokarda Slavić M. Cloning, overexpression and characterization of a thermostable endo-1,4-beta-xylanase from Anoxybacillus vranjensis ST4. in XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia. 2024;:31-31.
https://hdl.handle.net/21.15107/rcub_cer_7732 .

Pavlović, Marija, Kojić, Milan, Ristović, Marina, Stojanović, Sanja, Margetić, Aleksandra, Vujčić, Zoran, Šokarda Slavić, Marinela, "Cloning, overexpression and characterization of a thermostable endo-1,4-beta-xylanase from Anoxybacillus vranjensis ST4" in XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia (2024):31-31,
https://hdl.handle.net/21.15107/rcub_cer_7732 .

TY  - CONF
AU  - Pavlović, Marija
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Stojanović, Sanja
AU  - Nikolić, Stefan
AU  - Vujčić, Zoran
AU  - Šokarda Slavić, Marinela
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7731
AB  - Bacteria are an ideal source for producing pectin lyases (PNLs) due to their amenability to laboratory cultivation and genetic manipulation, which facilitates enhanced enzyme production. Predominantly originating from various thermophilic bacteria, bacterial PNLs usually exhibit alkaline properties, although cases of acidic variants have also been documented. In particular, a thermostable alkaline pectin lyase, displaying optimal activity at 60°C, has been characterized
from the thermophilic bacterium Brevibacillus borstelensis P35. Similarly, thermostable acidic PNLs have been identified in Geobacillus stearothermophilus
Ah22 and Bacillus subtilis SAV-21. Thermophilic bacterial species are emerging as significant and highly efficient sources, boasting diverse enzymatic repertoires, including pectinolytic enzymes, rendering them attractive candidates for various biotechnological applications. This mini-review focuses on the characterization
of pectin lyases from a thermophilic bacterium, shedding light on its biochemical
properties, substrate specificity, and potential industrial applications. Enzymes exhibit outstanding biochemical properties, with optimal pH and temperature ranges conducive to industrial processes, along with notable thermostability
and pH tolerance, augmenting their suitability for diverse biotechnological endeavours. Furthermore, the enzyme demonstrates specificity
towards pectin, efficiently cleaving glycosidic bonds within the polysaccharide backbone. Understanding the substrate specificity of pectin lyases is crucial for its effective utilization in industrial processes, especially considering its
preferences for high-methoxylated pectin while still demonstrating activity on low-methoxylated and amidated pectins, expanding its applicability.
Additionally, the synergy of pectin lyases with other pectinolytic enzymes enhances the efficiency of pectin degradation, facilitating the production
of valuable products such as biofuels, dietary fibers, and oligosaccharides. The versatility and efficiency of pectin lyases from thermophilic bacteria highlight its potential for application across various biotechnological sectors, including
food and beverage, textile, and pharmaceutical industries. Its capability to modify pectinaceous materials offers sustainable solutions for waste valorization and bioconversion processes.
PB  - Serbian Society for Microbiology
C3  - XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia
T1  - Exploring the biotechnological potential of thermophilic bacteria - derived pectin lyases: a mini-review
SP  - 44
EP  - 44
UR  - https://hdl.handle.net/21.15107/rcub_cer_7731
ER  - 

@conference{
author = "Pavlović, Marija and Margetić, Aleksandra and Ristović, Marina and Stojanović, Sanja and Nikolić, Stefan and Vujčić, Zoran and Šokarda Slavić, Marinela",
year = "2024",
abstract = "Bacteria are an ideal source for producing pectin lyases (PNLs) due to their amenability to laboratory cultivation and genetic manipulation, which facilitates enhanced enzyme production. Predominantly originating from various thermophilic bacteria, bacterial PNLs usually exhibit alkaline properties, although cases of acidic variants have also been documented. In particular, a thermostable alkaline pectin lyase, displaying optimal activity at 60°C, has been characterized
from the thermophilic bacterium Brevibacillus borstelensis P35. Similarly, thermostable acidic PNLs have been identified in Geobacillus stearothermophilus
Ah22 and Bacillus subtilis SAV-21. Thermophilic bacterial species are emerging as significant and highly efficient sources, boasting diverse enzymatic repertoires, including pectinolytic enzymes, rendering them attractive candidates for various biotechnological applications. This mini-review focuses on the characterization
of pectin lyases from a thermophilic bacterium, shedding light on its biochemical
properties, substrate specificity, and potential industrial applications. Enzymes exhibit outstanding biochemical properties, with optimal pH and temperature ranges conducive to industrial processes, along with notable thermostability
and pH tolerance, augmenting their suitability for diverse biotechnological endeavours. Furthermore, the enzyme demonstrates specificity
towards pectin, efficiently cleaving glycosidic bonds within the polysaccharide backbone. Understanding the substrate specificity of pectin lyases is crucial for its effective utilization in industrial processes, especially considering its
preferences for high-methoxylated pectin while still demonstrating activity on low-methoxylated and amidated pectins, expanding its applicability.
Additionally, the synergy of pectin lyases with other pectinolytic enzymes enhances the efficiency of pectin degradation, facilitating the production
of valuable products such as biofuels, dietary fibers, and oligosaccharides. The versatility and efficiency of pectin lyases from thermophilic bacteria highlight its potential for application across various biotechnological sectors, including
food and beverage, textile, and pharmaceutical industries. Its capability to modify pectinaceous materials offers sustainable solutions for waste valorization and bioconversion processes.",
publisher = "Serbian Society for Microbiology",
journal = "XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia",
title = "Exploring the biotechnological potential of thermophilic bacteria - derived pectin lyases: a mini-review",
pages = "44-44",
url = "https://hdl.handle.net/21.15107/rcub_cer_7731"
}

Pavlović, M., Margetić, A., Ristović, M., Stojanović, S., Nikolić, S., Vujčić, Z.,& Šokarda Slavić, M.. (2024). Exploring the biotechnological potential of thermophilic bacteria - derived pectin lyases: a mini-review. in XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia
Serbian Society for Microbiology., 44-44.
https://hdl.handle.net/21.15107/rcub_cer_7731

Pavlović M, Margetić A, Ristović M, Stojanović S, Nikolić S, Vujčić Z, Šokarda Slavić M. Exploring the biotechnological potential of thermophilic bacteria - derived pectin lyases: a mini-review. in XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia. 2024;:44-44.
https://hdl.handle.net/21.15107/rcub_cer_7731 .

Pavlović, Marija, Margetić, Aleksandra, Ristović, Marina, Stojanović, Sanja, Nikolić, Stefan, Vujčić, Zoran, Šokarda Slavić, Marinela, "Exploring the biotechnological potential of thermophilic bacteria - derived pectin lyases: a mini-review" in XIII Congress of microbiologists of Serbia, Book of abstracts, April 4-6, 2024, Belgrade, Serbia (2024):44-44,
https://hdl.handle.net/21.15107/rcub_cer_7731 .

TY  - JOUR
AU  - Pavlović, Marija
AU  - Margetić, Aleksandra
AU  - Leonardi, Adrijana
AU  - Križaj, Igor
AU  - Kojić, Milan
AU  - Vujčić, Zoran
AU  - Šokarda Slavić, Marinela
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7733
AB  - This study focuses on the isolation, purification, and characterisation of endo-polygalacturonase II from Aspergillus tubingensis FAT43, particularly emphasising its potential applications in the fruit juice industry. A comprehensive screening test revealed the temporal dynamics of endo-polygalacturonase production during a 96-hour fermentation process. The purification process, involving ammonium sulfate and ethanol precipitation followed by ion-exchange chromatography, resulted in a 3.3-fold purification of PG II with a yield of 16% and a specific activity of 6001.67 U mg-1. Molecular analysis confirmed the identity of PG II, its gene (pgaII), and a high degree of sequence identity with Aspergillus tubingensis in the SWISS-PROT database. The optimal pH for PG II activity was 3.5-4.5, with robust stability across a broad pH spectrum (3-7). The enzyme exhibited optimal temperature activity at 45 °C, with a retention of 90% activity at 50 °C. The calculated activation energy for PG II was 62.1 kJ mol-1, indicating good stability. Inactivation kinetics revealed a half-life of 13.7 h at 40 °C, 5.4 h at 50 °C, and 0.85 h at 60 °C, with an activation energy of denaturation of 32.8 kJ mol-1. Compared to literature-reported PGs, PG II from A. tubingensis FAT43 demonstrated superior thermal stability. Hydrolysis experiments on different pectins revealed the highest specificity for non-methylated substrates (polygalacturonic acid). In fruit juice processing, PG II significantly increased juice yield and clarity, with the highest impact observed in strawberry juice. Antioxidant activity assays indicated enhanced antioxidant potential in enzyme-treated juices, especially strawberry, quince, and apple juices. The study highlights PG II's potential as an industrially valuable enzyme for fruit juice processing, offering improved thermostability and versatility across various fruit types.
PB  - Royal Society of Chemistry
T2  - Food and Function
T1  - Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential
VL  - 15
SP  - 2906
EP  - 2919
DO  - 10.1039/d3fo05297d
ER  - 

@article{
author = "Pavlović, Marija and Margetić, Aleksandra and Leonardi, Adrijana and Križaj, Igor and Kojić, Milan and Vujčić, Zoran and Šokarda Slavić, Marinela",
year = "2024",
abstract = "This study focuses on the isolation, purification, and characterisation of endo-polygalacturonase II from Aspergillus tubingensis FAT43, particularly emphasising its potential applications in the fruit juice industry. A comprehensive screening test revealed the temporal dynamics of endo-polygalacturonase production during a 96-hour fermentation process. The purification process, involving ammonium sulfate and ethanol precipitation followed by ion-exchange chromatography, resulted in a 3.3-fold purification of PG II with a yield of 16% and a specific activity of 6001.67 U mg-1. Molecular analysis confirmed the identity of PG II, its gene (pgaII), and a high degree of sequence identity with Aspergillus tubingensis in the SWISS-PROT database. The optimal pH for PG II activity was 3.5-4.5, with robust stability across a broad pH spectrum (3-7). The enzyme exhibited optimal temperature activity at 45 °C, with a retention of 90% activity at 50 °C. The calculated activation energy for PG II was 62.1 kJ mol-1, indicating good stability. Inactivation kinetics revealed a half-life of 13.7 h at 40 °C, 5.4 h at 50 °C, and 0.85 h at 60 °C, with an activation energy of denaturation of 32.8 kJ mol-1. Compared to literature-reported PGs, PG II from A. tubingensis FAT43 demonstrated superior thermal stability. Hydrolysis experiments on different pectins revealed the highest specificity for non-methylated substrates (polygalacturonic acid). In fruit juice processing, PG II significantly increased juice yield and clarity, with the highest impact observed in strawberry juice. Antioxidant activity assays indicated enhanced antioxidant potential in enzyme-treated juices, especially strawberry, quince, and apple juices. The study highlights PG II's potential as an industrially valuable enzyme for fruit juice processing, offering improved thermostability and versatility across various fruit types.",
publisher = "Royal Society of Chemistry",
journal = "Food and Function",
title = "Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential",
volume = "15",
pages = "2906-2919",
doi = "10.1039/d3fo05297d"
}

Pavlović, M., Margetić, A., Leonardi, A., Križaj, I., Kojić, M., Vujčić, Z.,& Šokarda Slavić, M.. (2024). Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential. in Food and Function
Royal Society of Chemistry., 15, 2906-2919.
https://doi.org/10.1039/d3fo05297d

Pavlović M, Margetić A, Leonardi A, Križaj I, Kojić M, Vujčić Z, Šokarda Slavić M. Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential. in Food and Function. 2024;15:2906-2919.
doi:10.1039/d3fo05297d .

Pavlović, Marija, Margetić, Aleksandra, Leonardi, Adrijana, Križaj, Igor, Kojić, Milan, Vujčić, Zoran, Šokarda Slavić, Marinela, "Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential" in Food and Function, 15 (2024):2906-2919,
https://doi.org/10.1039/d3fo05297d . .

TY  - JOUR
AU  - Pavlović, Marija
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Drulović, Nenad
AU  - Vujčić, Zoran
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7734
AB  - Microbial pectinolytic enzymes are important in various industries, particularly food processing. This study focuses on uncovering insights into a novel pectin lyase, BvPelB, from Bacillus velezensis 16B, with the aim of enhancing fruit juice processing. The study examines the structural and functional characteristics of pectinolytic enzyme, underscoring the critical nature of substrate specificity and enzymatic reaction mechanisms. BvPelB was successfully expressed and purified, exhibiting robust activity under alkaline conditions and thermal stability. Structural analysis revealed similarities with other pectin lyases, despite limited sequence identity. Biochemical characterization showed BvPelB's preference for highly methylated pectins and its endo-acting mode of cleavage. Treatment with BvPelB significantly increased juice yield and clarity without generating excessive methanol, making it a promising candidate for fruit juice processing. Overall, this study provides valuable insights into the enzymatic properties of BvPelB and its potential industrial applications in improving fruit juice processing efficiency and quality.
PB  - Elsevier
T2  - Food Chemistry
T1  - Unveiling novel insights into Bacillus velezensis 16B pectin lyase for improved fruit juice processing
VL  - 456
SP  - 140030
DO  - 10.1016/j.foodchem.2024.140030
ER  - 

@article{
author = "Pavlović, Marija and Šokarda Slavić, Marinela and Kojić, Milan and Margetić, Aleksandra and Ristović, Marina and Drulović, Nenad and Vujčić, Zoran",
year = "2024",
abstract = "Microbial pectinolytic enzymes are important in various industries, particularly food processing. This study focuses on uncovering insights into a novel pectin lyase, BvPelB, from Bacillus velezensis 16B, with the aim of enhancing fruit juice processing. The study examines the structural and functional characteristics of pectinolytic enzyme, underscoring the critical nature of substrate specificity and enzymatic reaction mechanisms. BvPelB was successfully expressed and purified, exhibiting robust activity under alkaline conditions and thermal stability. Structural analysis revealed similarities with other pectin lyases, despite limited sequence identity. Biochemical characterization showed BvPelB's preference for highly methylated pectins and its endo-acting mode of cleavage. Treatment with BvPelB significantly increased juice yield and clarity without generating excessive methanol, making it a promising candidate for fruit juice processing. Overall, this study provides valuable insights into the enzymatic properties of BvPelB and its potential industrial applications in improving fruit juice processing efficiency and quality.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Unveiling novel insights into Bacillus velezensis 16B pectin lyase for improved fruit juice processing",
volume = "456",
pages = "140030",
doi = "10.1016/j.foodchem.2024.140030"
}

Pavlović, M., Šokarda Slavić, M., Kojić, M., Margetić, A., Ristović, M., Drulović, N.,& Vujčić, Z.. (2024). Unveiling novel insights into Bacillus velezensis 16B pectin lyase for improved fruit juice processing. in Food Chemistry
Elsevier., 456, 140030.
https://doi.org/10.1016/j.foodchem.2024.140030

Pavlović M, Šokarda Slavić M, Kojić M, Margetić A, Ristović M, Drulović N, Vujčić Z. Unveiling novel insights into Bacillus velezensis 16B pectin lyase for improved fruit juice processing. in Food Chemistry. 2024;456:140030.
doi:10.1016/j.foodchem.2024.140030 .

Pavlović, Marija, Šokarda Slavić, Marinela, Kojić, Milan, Margetić, Aleksandra, Ristović, Marina, Drulović, Nenad, Vujčić, Zoran, "Unveiling novel insights into Bacillus velezensis 16B pectin lyase for improved fruit juice processing" in Food Chemistry, 456 (2024):140030,
https://doi.org/10.1016/j.foodchem.2024.140030 . .

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  - https://cer.ihtm.bg.ac.rs/handle/123456789/6459
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  - 1
EP  - 10
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 = "1-10",
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), 1-10.
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):1-10.
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):1-10,
https://doi.org/10.1093/lambio/ovad083 . .

TY  - CONF
AU  - Ristović, Marina
AU  - Stojanović, Sanja
AU  - Pavlović, Marija
AU  - Margetić, Aleksandra
AU  - Šokarda Slavić, Marinela
AU  - Vujčić, Zoran
AU  - Dojnov, Biljana
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6243
AB  - Xylan makes a significant part of cereals and fruits, which are used in the food industry. Therefore, enzymes that hydrolyze xylan (xylanases) have found application in the modification of cereal-based food, improving the digestibility of animal feed, and improving the texture of bakery products. In the juice industry, the main problems are turbidity, viscosity, and sedimentation during standing, which are caused by polysaccharides present in fruit (pectins, cellulose, and hemicellulose (xylan)). Pineapple, apple, orange, and tomato have a high content of hemicellulose, so xylanases are suitable for improving the properties of these juices. The Aspergillus tubingensis FAT 35 strain (considered safe for use in the food industry) growing on SSF medium composed of corn cob produced a high level of xylanase enzyme (4.03 U∕mL) and not that high pectinase (1.02 U∕mL) and cellulase (1.43 U∕mL) activities at pH 3 which is pH of freshly prepared apple, pineapple and organge juice.. The fermentation extract was used for clarification of pineapple, apple, and orange juice and for increasing the filtration rate and yield of these juices. Results indicate that A. tubigensis xylanase could be used for clarification and improvement of properties of juices of fruits that contain hemicellulose in high proportion.
PB  - Serbian Chemical Society
C3  - Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia
T1  - Highly active xylanase used in juice clarification
SP  - 208
EP  - 208
UR  - https://hdl.handle.net/21.15107/rcub_cer_6243
ER  - 

@conference{
author = "Ristović, Marina and Stojanović, Sanja and Pavlović, Marija and Margetić, Aleksandra and Šokarda Slavić, Marinela and Vujčić, Zoran and Dojnov, Biljana",
year = "2023",
abstract = "Xylan makes a significant part of cereals and fruits, which are used in the food industry. Therefore, enzymes that hydrolyze xylan (xylanases) have found application in the modification of cereal-based food, improving the digestibility of animal feed, and improving the texture of bakery products. In the juice industry, the main problems are turbidity, viscosity, and sedimentation during standing, which are caused by polysaccharides present in fruit (pectins, cellulose, and hemicellulose (xylan)). Pineapple, apple, orange, and tomato have a high content of hemicellulose, so xylanases are suitable for improving the properties of these juices. The Aspergillus tubingensis FAT 35 strain (considered safe for use in the food industry) growing on SSF medium composed of corn cob produced a high level of xylanase enzyme (4.03 U∕mL) and not that high pectinase (1.02 U∕mL) and cellulase (1.43 U∕mL) activities at pH 3 which is pH of freshly prepared apple, pineapple and organge juice.. The fermentation extract was used for clarification of pineapple, apple, and orange juice and for increasing the filtration rate and yield of these juices. Results indicate that A. tubigensis xylanase could be used for clarification and improvement of properties of juices of fruits that contain hemicellulose in high proportion.",
publisher = "Serbian Chemical Society",
journal = "Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia",
title = "Highly active xylanase used in juice clarification",
pages = "208-208",
url = "https://hdl.handle.net/21.15107/rcub_cer_6243"
}

Ristović, M., Stojanović, S., Pavlović, M., Margetić, A., Šokarda Slavić, M., Vujčić, Z.,& Dojnov, B.. (2023). Highly active xylanase used in juice clarification. in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia
Serbian Chemical Society., 208-208.
https://hdl.handle.net/21.15107/rcub_cer_6243

Ristović M, Stojanović S, Pavlović M, Margetić A, Šokarda Slavić M, Vujčić Z, Dojnov B. Highly active xylanase used in juice clarification. in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia. 2023;:208-208.
https://hdl.handle.net/21.15107/rcub_cer_6243 .

Ristović, Marina, Stojanović, Sanja, Pavlović, Marija, Margetić, Aleksandra, Šokarda Slavić, Marinela, Vujčić, Zoran, Dojnov, Biljana, "Highly active xylanase used in juice clarification" in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia (2023):208-208,
https://hdl.handle.net/21.15107/rcub_cer_6243 .

TY  - CONF
AU  - Pavlović, Marija
AU  - Šokarda Slavić, Marinela
AU  - Ristović, Marina
AU  - Margetić, Aleksandra
AU  - Stojanović, Sanja
AU  - Momčilović, Miloš
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6241
AB  - Pectinases are a type of enzymes frequently used in the food industry to clarify, liquefy, and stabilize fruit juices. The main challenge in fruit juice production is the cloudiness of the juice, which is largely caused by the presence of pectic polysaccharides. Endo-pectinases are enzymes that hydrolyze the glycosidic bonds in pectic polymers. Commercial pectinolytic enzymes are typically produced by fungi, with Aspergillus spp. being the most commonly used.
The aim of this research was the production and characterization of a novel endo-pectinase from the Aspergillus tubingensis strain for use in liquefying and clarifying different types of fruit juice. To accomplish this, solid-state fermentation was conducted on agricultural waste, such as sugar beet pulp and wheat bran, to produce pectinolytic enzymes. The resulting crude extract was concentrated via ultrafiltration and used to isolate the endo-pectinase via ammonium sulfate and ethanol precipitation methods. Ion-exchange chromatography technique on DEAE Sephadex A-25 matrix was used for further purification of the endo-pectinase.
The purified enzyme was characterized by the determination of total pectinolytic activity, specific pectinolytic activity, and SDS-PAA gel electrophoresis. The activity of the endo-pectinase was confirmed by a diffusion test and zymography with Ruthenium Red visualization. The resulting enzyme was used to liquefy apricot, banana, apple, quince, strawberry, and orange pulp, with juice yields ranging from 71% to 83%, depending on the fruit used. The juices treated with endo-pectinase showed much higher clarification compared to untreated juices. Additionally, the treated juices demonstrated more pronounced antioxidant properties, as determined through the DPPH assay.
PB  - Serbian Chemical Society
C3  - Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia
T1  - Highly active endo-pectinases from Aspergillus tubingensis: A novel enzyme for fruit processing
SP  - 207
EP  - 207
UR  - https://hdl.handle.net/21.15107/rcub_cer_6241
ER  - 

@conference{
author = "Pavlović, Marija and Šokarda Slavić, Marinela and Ristović, Marina and Margetić, Aleksandra and Stojanović, Sanja and Momčilović, Miloš and Vujčić, Zoran",
year = "2023",
abstract = "Pectinases are a type of enzymes frequently used in the food industry to clarify, liquefy, and stabilize fruit juices. The main challenge in fruit juice production is the cloudiness of the juice, which is largely caused by the presence of pectic polysaccharides. Endo-pectinases are enzymes that hydrolyze the glycosidic bonds in pectic polymers. Commercial pectinolytic enzymes are typically produced by fungi, with Aspergillus spp. being the most commonly used.
The aim of this research was the production and characterization of a novel endo-pectinase from the Aspergillus tubingensis strain for use in liquefying and clarifying different types of fruit juice. To accomplish this, solid-state fermentation was conducted on agricultural waste, such as sugar beet pulp and wheat bran, to produce pectinolytic enzymes. The resulting crude extract was concentrated via ultrafiltration and used to isolate the endo-pectinase via ammonium sulfate and ethanol precipitation methods. Ion-exchange chromatography technique on DEAE Sephadex A-25 matrix was used for further purification of the endo-pectinase.
The purified enzyme was characterized by the determination of total pectinolytic activity, specific pectinolytic activity, and SDS-PAA gel electrophoresis. The activity of the endo-pectinase was confirmed by a diffusion test and zymography with Ruthenium Red visualization. The resulting enzyme was used to liquefy apricot, banana, apple, quince, strawberry, and orange pulp, with juice yields ranging from 71% to 83%, depending on the fruit used. The juices treated with endo-pectinase showed much higher clarification compared to untreated juices. Additionally, the treated juices demonstrated more pronounced antioxidant properties, as determined through the DPPH assay.",
publisher = "Serbian Chemical Society",
journal = "Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia",
title = "Highly active endo-pectinases from Aspergillus tubingensis: A novel enzyme for fruit processing",
pages = "207-207",
url = "https://hdl.handle.net/21.15107/rcub_cer_6241"
}

Pavlović, M., Šokarda Slavić, M., Ristović, M., Margetić, A., Stojanović, S., Momčilović, M.,& Vujčić, Z.. (2023). Highly active endo-pectinases from Aspergillus tubingensis: A novel enzyme for fruit processing. in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia
Serbian Chemical Society., 207-207.
https://hdl.handle.net/21.15107/rcub_cer_6241

Pavlović M, Šokarda Slavić M, Ristović M, Margetić A, Stojanović S, Momčilović M, Vujčić Z. Highly active endo-pectinases from Aspergillus tubingensis: A novel enzyme for fruit processing. in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia. 2023;:207-207.
https://hdl.handle.net/21.15107/rcub_cer_6241 .

Pavlović, Marija, Šokarda Slavić, Marinela, Ristović, Marina, Margetić, Aleksandra, Stojanović, Sanja, Momčilović, Miloš, Vujčić, Zoran, "Highly active endo-pectinases from Aspergillus tubingensis: A novel enzyme for fruit processing" in Abstract Book - XXII Congress EuroFoodChem, June 14-16, 2023, Belgrade, Serbia (2023):207-207,
https://hdl.handle.net/21.15107/rcub_cer_6241 .

TY  - CONF
AU  - Šokarda Slavić, Marinela
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Pavlović, Marija
AU  - Stojanović, Sanja
AU  - Drulović, Nenad
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6028
AB  - Fish processing generates a large amount of waste products; nearly 75 % of the total fish weight consists of scales, skins, heads, viscera, and bones. These waste by-products are often dumped in landfills or the ocean, contributing to environmental pollution. Solid fish waste has a high collagen content and can be utilized for the extraction of different products such as gelatine, which can be used in different food and pharmaceutical industries. Fish gelatine contains all biogenic amino acids and can be used as a dietary supplement, thus increasing the utilization of fish waste and reducing environmental pollution.
Recently, a strong worldwide focus has been directed towards the discovery of new microbial proteases for industrial applications. For that purpose, the Bacillus sp. strains from the laboratory bank were screened for the ability to secrete alkaline proteases. Bacterial strains that produced a larger clear zone on the gelatine agar plate were selected for further study. Selected bacterial strains were cultivated under submerged conditions for the purpose of producing proteases. The supernatant from each isolate was used as a crude enzyme extract for testing gelatine proteolytic activity and hydrolysis products. Bacillus sp. strains 12B, 16A, 17B and 24B showed a high degree of hydrolysis of the gelatine waste and the ability to form proteins of small molecular masses after one hour of hydrolysis. Of these, sp. 12B was the most potent, having twice the proteolytic activity determined by the TNBS method.
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  - Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation
SP  - 66
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cer_6028
ER  - 

@conference{
author = "Šokarda Slavić, Marinela and Margetić, Aleksandra and Ristović, Marina and Pavlović, Marija and Stojanović, Sanja and Drulović, Nenad and Vujčić, Zoran",
year = "2023",
abstract = "Fish processing generates a large amount of waste products; nearly 75 % of the total fish weight consists of scales, skins, heads, viscera, and bones. These waste by-products are often dumped in landfills or the ocean, contributing to environmental pollution. Solid fish waste has a high collagen content and can be utilized for the extraction of different products such as gelatine, which can be used in different food and pharmaceutical industries. Fish gelatine contains all biogenic amino acids and can be used as a dietary supplement, thus increasing the utilization of fish waste and reducing environmental pollution.
Recently, a strong worldwide focus has been directed towards the discovery of new microbial proteases for industrial applications. For that purpose, the Bacillus sp. strains from the laboratory bank were screened for the ability to secrete alkaline proteases. Bacterial strains that produced a larger clear zone on the gelatine agar plate were selected for further study. Selected bacterial strains were cultivated under submerged conditions for the purpose of producing proteases. The supernatant from each isolate was used as a crude enzyme extract for testing gelatine proteolytic activity and hydrolysis products. Bacillus sp. strains 12B, 16A, 17B and 24B showed a high degree of hydrolysis of the gelatine waste and the ability to form proteins of small molecular masses after one hour of hydrolysis. Of these, sp. 12B was the most potent, having twice the proteolytic activity determined by the TNBS method.",
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 = "Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation",
pages = "66-66",
url = "https://hdl.handle.net/21.15107/rcub_cer_6028"
}

Šokarda Slavić, M., Margetić, A., Ristović, M., Pavlović, M., Stojanović, S., Drulović, N.,& Vujčić, Z.. (2023). Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation. 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., 66-66.
https://hdl.handle.net/21.15107/rcub_cer_6028

Šokarda Slavić M, Margetić A, Ristović M, Pavlović M, Stojanović S, Drulović N, Vujčić Z. Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation. 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;:66-66.
https://hdl.handle.net/21.15107/rcub_cer_6028 .

Šokarda Slavić, Marinela, Margetić, Aleksandra, Ristović, Marina, Pavlović, Marija, Stojanović, Sanja, Drulović, Nenad, Vujčić, Zoran, "Screening of Bacillus sp. protease for hydrolysis of gelatine extracted from fish waste and potential applications for waste valorisation" 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):66-66,
https://hdl.handle.net/21.15107/rcub_cer_6028 .

TY  - CONF
AU  - Margetić, Aleksandra
AU  - Šokarda Slavić, Marinela
AU  - Ristović, Marina
AU  - Stojanović, Sanja
AU  - Pavlović, Marija
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6027
AB  - When textile dyes are released into the water, they can have a range of negative effects on the environment, for example, azo dyes can break down into carcinogenic compounds when exposed to sunlight. Remazol Brilliant Blue R (RBBR) and Reactive Black 5 (RB5) are reactive dyes. Unfortunately, the discharge of untreated effluents from these industries into nature can result in the contamination of water, which can have harmful effects on the environment.
Saccharomyces cerevisiae is widely used in different fields of biotechnology. In this work, the cell walls of used yeast were reused for the biosorption of textile dyes, and the possibility of their utilization in wastewater treatment was investigated. The response surface methodology approach was applied to determine the optimal levels of three input variables - pH, temperature, and time, and also to identify the relationship between the response functions and process variables. Five levels of three variables were used, pH range 2–13, temperature range 15–40°C and time 0.15–30 h. The decolorization processes were optimized using the Central Composite Design. A significant impact of pH and temperature
was found, while satisfactory results in decolorization (≥ 90%) were shown in a short time (up to 1 h). The maximum adsorption capacity (MAC) of the used Saccharomyces cerevisiae cell wall for removing RBBR and RB5 from wastewater was tested according to results obtained by CCD considering the economy of the process (pH 4, 25°C and 1 hour). Experimentally obtained MAC was 400 mg/g and 200 mg/g for RBBR and RB5, 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  - Reusing biomass in textile dyes removing from wastewater
SP  - 62
EP  - 62
UR  - https://hdl.handle.net/21.15107/rcub_cer_6027
ER  - 

@conference{
author = "Margetić, Aleksandra and Šokarda Slavić, Marinela and Ristović, Marina and Stojanović, Sanja and Pavlović, Marija and Vujčić, Zoran",
year = "2023",
abstract = "When textile dyes are released into the water, they can have a range of negative effects on the environment, for example, azo dyes can break down into carcinogenic compounds when exposed to sunlight. Remazol Brilliant Blue R (RBBR) and Reactive Black 5 (RB5) are reactive dyes. Unfortunately, the discharge of untreated effluents from these industries into nature can result in the contamination of water, which can have harmful effects on the environment.
Saccharomyces cerevisiae is widely used in different fields of biotechnology. In this work, the cell walls of used yeast were reused for the biosorption of textile dyes, and the possibility of their utilization in wastewater treatment was investigated. The response surface methodology approach was applied to determine the optimal levels of three input variables - pH, temperature, and time, and also to identify the relationship between the response functions and process variables. Five levels of three variables were used, pH range 2–13, temperature range 15–40°C and time 0.15–30 h. The decolorization processes were optimized using the Central Composite Design. A significant impact of pH and temperature
was found, while satisfactory results in decolorization (≥ 90%) were shown in a short time (up to 1 h). The maximum adsorption capacity (MAC) of the used Saccharomyces cerevisiae cell wall for removing RBBR and RB5 from wastewater was tested according to results obtained by CCD considering the economy of the process (pH 4, 25°C and 1 hour). Experimentally obtained MAC was 400 mg/g and 200 mg/g for RBBR and RB5, 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 = "Reusing biomass in textile dyes removing from wastewater",
pages = "62-62",
url = "https://hdl.handle.net/21.15107/rcub_cer_6027"
}

Margetić, A., Šokarda Slavić, M., Ristović, M., Stojanović, S., Pavlović, M.,& Vujčić, Z.. (2023). Reusing biomass in textile dyes removing from wastewater. 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., 62-62.
https://hdl.handle.net/21.15107/rcub_cer_6027

Margetić A, Šokarda Slavić M, Ristović M, Stojanović S, Pavlović M, Vujčić Z. Reusing biomass in textile dyes removing from wastewater. 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;:62-62.
https://hdl.handle.net/21.15107/rcub_cer_6027 .

Margetić, Aleksandra, Šokarda Slavić, Marinela, Ristović, Marina, Stojanović, Sanja, Pavlović, Marija, Vujčić, Zoran, "Reusing biomass in textile dyes removing from wastewater" 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):62-62,
https://hdl.handle.net/21.15107/rcub_cer_6027 .

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  - https://cer.ihtm.bg.ac.rs/handle/123456789/6518
AB  - The combination of b-oligosaccharides from enzymatically hydrolysed barley b-glucan has attracted interest
recently due to its positive effects on human health. This study aimed to assess the impact of the
endo-b-1,3-1,4-glucanase enzyme from Bacillus subtilis 168 on improving the nutritional and bioactive
properties of barley b-glucan. A new procedure for the isolation of b-glucan was developed, at a lower
temperature (45 °C), enabling purity from starch contamination, without affecting the yield (6 g b-glucan
from 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned into E. coli pQE_Ek enables the high
production and purification (82% yield, 1.8 mg mL
 1 and 440 U mg
 1) of an enzyme identical to the
natural one (25.5 kDa). The enzymatic reaction showed high efficiency of b-glucan degradation by recombinant
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 capacities
by 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicate
the possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barley bglucan
used as functional foods.
PB  - Wiley
T2  - International Journal of Food Science and Technology
T1  - Improvement of nutritional and bioactive properties of barley β-glucan-based food products using Bacillus subtilis 168 endo-β-1,3-1,4-glucanase
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 of b-oligosaccharides from enzymatically hydrolysed barley b-glucan has attracted interest
recently due to its positive effects on human health. This study aimed to assess the impact of the
endo-b-1,3-1,4-glucanase enzyme from Bacillus subtilis 168 on improving the nutritional and bioactive
properties of barley b-glucan. A new procedure for the isolation of b-glucan was developed, at a lower
temperature (45 °C), enabling purity from starch contamination, without affecting the yield (6 g b-glucan
from 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned into E. coli pQE_Ek enables the high
production and purification (82% yield, 1.8 mg mL
 1 and 440 U mg
 1) of an enzyme identical to the
natural one (25.5 kDa). The enzymatic reaction showed high efficiency of b-glucan degradation by recombinant
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 capacities
by 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicate
the possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barley bglucan
used as functional foods.",
publisher = "Wiley",
journal = "International Journal of Food Science and Technology",
title = "Improvement of nutritional and bioactive properties of barley β-glucan-based food products using Bacillus subtilis 168 endo-β-1,3-1,4-glucanase",
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 barley β-glucan-based food products using Bacillus subtilis 168 endo-β-1,3-1,4-glucanase. in International Journal of Food Science and Technology
Wiley..
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 barley β-glucan-based food products using Bacillus subtilis 168 endo-β-1,3-1,4-glucanase. in International Journal of Food Science and Technology. 2023;.
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 barley β-glucan-based food products using Bacillus subtilis 168 endo-β-1,3-1,4-glucanase" in International Journal of Food Science and Technology (2023),
https://doi.org/10.1111/ijfs.16647 . .

TY  - CONF
AU  - Pavlović, Marija
AU  - Momčilović, Miloš
AU  - Živković, Sanja
AU  - Šokarda Slavić, Marinela
AU  - Ristović, Marina
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7751
AB  - U ovom radu urađen je skrining sojeva Aspergillus spp. koji proizvode pektinaze fermentacijom u tečnom medijumu, a koje su efikasne u izbistravanju soka od jagode. Endo-pektinaze su detektovane difuzionim testom, a ukupna pektinazna aktivnost određena je DNS metodom. Izbistravanje soka nakon tretmana pektinazama određeno je merenjem transmitancije na 660 nm, a povećanje prinosa soka izmereno je centrifugiranjem. Dobijeni rezultati su pokazali da su ove pektinaze visokoefikasne za tretman soka od jagode u poređenju sa komercijalnim pektinaznim preparatom Lafase Fruit.
AB  - In this work, the screening of Aspergillus spp which produce pectinases by fermentation in a liquid medium was performed, as pectinases are effective in clarifying strawberry juice. Endo-pectinases were detected by the diffusion assay, and total pectinase activity was determined by the DNS method. The clarification of juice after pectinase treatment was determined by measuring the transmission at 660 nm, and an increase in juice yield was measured by centrifugation. The results obtained showed that these pectinases are very effective for the treatment of strawberry juice in comparison with the commercial pectinase preparation Lafase Fruit.
PB  - Belgrade : Serbian Chemical Society
C3  - 59th Meeting of the Serbian Chemical Society : Book of Abstracts, Proceedings
T1  - Skrining pektinaznih proizvođača Aspergillus spp. za upotrebu u izbistravanju soka od jagode
T1  - Screening of pectinase-producing Aspergillus spp. for use in strawberry juice clarification
SP  - 55
EP  - 55
UR  - https://hdl.handle.net/21.15107/rcub_cer_7751
ER  - 

@conference{
author = "Pavlović, Marija and Momčilović, Miloš and Živković, Sanja and Šokarda Slavić, Marinela and Ristović, Marina and Vujčić, Zoran",
year = "2023",
abstract = "U ovom radu urađen je skrining sojeva Aspergillus spp. koji proizvode pektinaze fermentacijom u tečnom medijumu, a koje su efikasne u izbistravanju soka od jagode. Endo-pektinaze su detektovane difuzionim testom, a ukupna pektinazna aktivnost određena je DNS metodom. Izbistravanje soka nakon tretmana pektinazama određeno je merenjem transmitancije na 660 nm, a povećanje prinosa soka izmereno je centrifugiranjem. Dobijeni rezultati su pokazali da su ove pektinaze visokoefikasne za tretman soka od jagode u poređenju sa komercijalnim pektinaznim preparatom Lafase Fruit., In this work, the screening of Aspergillus spp which produce pectinases by fermentation in a liquid medium was performed, as pectinases are effective in clarifying strawberry juice. Endo-pectinases were detected by the diffusion assay, and total pectinase activity was determined by the DNS method. The clarification of juice after pectinase treatment was determined by measuring the transmission at 660 nm, and an increase in juice yield was measured by centrifugation. The results obtained showed that these pectinases are very effective for the treatment of strawberry juice in comparison with the commercial pectinase preparation Lafase Fruit.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "59th Meeting of the Serbian Chemical Society : Book of Abstracts, Proceedings",
title = "Skrining pektinaznih proizvođača Aspergillus spp. za upotrebu u izbistravanju soka od jagode, Screening of pectinase-producing Aspergillus spp. for use in strawberry juice clarification",
pages = "55-55",
url = "https://hdl.handle.net/21.15107/rcub_cer_7751"
}

Pavlović, M., Momčilović, M., Živković, S., Šokarda Slavić, M., Ristović, M.,& Vujčić, Z.. (2023). Skrining pektinaznih proizvođača Aspergillus spp. za upotrebu u izbistravanju soka od jagode. in 59th Meeting of the Serbian Chemical Society : Book of Abstracts, Proceedings
Belgrade : Serbian Chemical Society., 55-55.
https://hdl.handle.net/21.15107/rcub_cer_7751

Pavlović M, Momčilović M, Živković S, Šokarda Slavić M, Ristović M, Vujčić Z. Skrining pektinaznih proizvođača Aspergillus spp. za upotrebu u izbistravanju soka od jagode. in 59th Meeting of the Serbian Chemical Society : Book of Abstracts, Proceedings. 2023;:55-55.
https://hdl.handle.net/21.15107/rcub_cer_7751 .

Pavlović, Marija, Momčilović, Miloš, Živković, Sanja, Šokarda Slavić, Marinela, Ristović, Marina, Vujčić, Zoran, "Skrining pektinaznih proizvođača Aspergillus spp. za upotrebu u izbistravanju soka od jagode" in 59th Meeting of the Serbian Chemical Society : Book of Abstracts, Proceedings (2023):55-55,
https://hdl.handle.net/21.15107/rcub_cer_7751 .

TY  - CONF
AU  - Pavlović, Marija
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Ristović, Marina
AU  - Momčilović, Miloš
AU  - Drulović, Nenad
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7136
AB  - Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices. Primarily, these enzymes are responsible for the breakdown of long and complex molecules in the fruit pulp (pectin). Unlike the combination of polygalacturonase (PG) and pectin esterase (PE) commonly found in commercial products, pectin lyase (PNL) is the only known pectinase capable of breaking down highly esterified pectins (such those found in fruits) into short molecules via a β-elimination mechanism without producing methanol. Methanol is toxic and can be harmful to health. Commercial preparations with PNL as the major component are preferable in juices and wine processing because it avoids the production of methanol, precipitation of pectin partially de-esterified with endogenous calcium, and damage of the volatile ester content responsible for the specific aroma of various fruits. This study reports the first cloning and characterization of a PNL gene, ppr, from Bacillus velezensis, and the deduced amino acid sequence is compared with those of other lyases. In this work, the gene encoding the pectin lyase (PNL; EC 4.2.2.10) from Bacillus velezensis was successfully expressed under optimized conditions for high soluble protein expressions as soluble PNL-6His in E. coli M15[pREP4]. After expression, purification of 6xHis-labeled PNL was performed according to QIAGEN instructions. IMAC fractions were analyzed using SDS-PAGE. After purification, 3-fold purification was observed with a yield of 82%. In this study, we report for the first time a method to express PNL in E. coli and purify it as a pure native enzyme. The cloned PLN was used to clarify and liquefy apple and orange juices and to improve the flavor of these juices. In this way, pulp waste after juice extraction is reduced. Methanol content was determined by gas-liquid chromatography and was not detectable in the clarified juices.
PB  - Elsevier
C3  - Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany
T1  - Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis
SP  - P3.015
UR  - https://hdl.handle.net/21.15107/rcub_cer_7136
ER  - 

@conference{
author = "Pavlović, Marija and Šokarda Slavić, Marinela and Kojić, Milan and Ristović, Marina and Momčilović, Miloš and Drulović, Nenad and Vujčić, Zoran",
year = "2023",
abstract = "Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices. Primarily, these enzymes are responsible for the breakdown of long and complex molecules in the fruit pulp (pectin). Unlike the combination of polygalacturonase (PG) and pectin esterase (PE) commonly found in commercial products, pectin lyase (PNL) is the only known pectinase capable of breaking down highly esterified pectins (such those found in fruits) into short molecules via a β-elimination mechanism without producing methanol. Methanol is toxic and can be harmful to health. Commercial preparations with PNL as the major component are preferable in juices and wine processing because it avoids the production of methanol, precipitation of pectin partially de-esterified with endogenous calcium, and damage of the volatile ester content responsible for the specific aroma of various fruits. This study reports the first cloning and characterization of a PNL gene, ppr, from Bacillus velezensis, and the deduced amino acid sequence is compared with those of other lyases. In this work, the gene encoding the pectin lyase (PNL; EC 4.2.2.10) from Bacillus velezensis was successfully expressed under optimized conditions for high soluble protein expressions as soluble PNL-6His in E. coli M15[pREP4]. After expression, purification of 6xHis-labeled PNL was performed according to QIAGEN instructions. IMAC fractions were analyzed using SDS-PAGE. After purification, 3-fold purification was observed with a yield of 82%. In this study, we report for the first time a method to express PNL in E. coli and purify it as a pure native enzyme. The cloned PLN was used to clarify and liquefy apple and orange juices and to improve the flavor of these juices. In this way, pulp waste after juice extraction is reduced. Methanol content was determined by gas-liquid chromatography and was not detectable in the clarified juices.",
publisher = "Elsevier",
journal = "Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany",
title = "Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis",
pages = "P3.015",
url = "https://hdl.handle.net/21.15107/rcub_cer_7136"
}

Pavlović, M., Šokarda Slavić, M., Kojić, M., Ristović, M., Momčilović, M., Drulović, N.,& Vujčić, Z.. (2023). Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis. in Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany
Elsevier., P3.015.
https://hdl.handle.net/21.15107/rcub_cer_7136

Pavlović M, Šokarda Slavić M, Kojić M, Ristović M, Momčilović M, Drulović N, Vujčić Z. Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis. in Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany. 2023;:P3.015.
https://hdl.handle.net/21.15107/rcub_cer_7136 .

Pavlović, Marija, Šokarda Slavić, Marinela, Kojić, Milan, Ristović, Marina, Momčilović, Miloš, Drulović, Nenad, Vujčić, Zoran, "Highly efficient clarification of fruit juices with new pectin lyase from Bacillus velezensis" in Book of Abstracts - 3rd Food Chemistry Conference, 10-12 October 2023, Dresden, Germany (2023):P3.015,
https://hdl.handle.net/21.15107/rcub_cer_7136 .

TY  - JOUR
AU  - Pavlović, Ratko
AU  - Dojnov, Biljana
AU  - Šokarda Slavić, Marinela
AU  - Pavlović, Marija
AU  - Slomo, Katarina
AU  - Ristović, Marina
AU  - Vujčić, Zoran
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5593
AB  - Finding a pollen substitute for honey bees that is nutritionally adequate and affordable is a scientific and practical challenge. We attempted a new rational approach and tried to exploit honey bees’ natural cannibalistic behavior. We tested processed insect larvae as a food source that is nutritionally similar to bee brood, and which can easily be produced on a large scale. In cage experiments, monitoring bee mortality, food consumption and changes in bee body parts’ weights showed that flour obtained by grinding dried yellow mealworm larvae has the potential to become an excellent component for pollen substitution. Bees from the cage group fed Tenebrio molitor patties (TG) demonstrated overall best results in comparison to sugar patties fed bee group (CG), yeast patties fed bee group (YG) and pollen patties fed bee group (PG). They did not lose weight as rapidly as the CG, did not defecate inside cages as the YG, nor show increased mortality as the PG. At the same time, TG consumed less food (mean 13.7 g/cage) than CG (16.8 g/cage), YG (20.4 g/cage) and PG (23.9 g/cage) within the period of 28 days. Bees’ gut increase in weight was lowest in the CG, followed by TG and PG and was the highest in the YG which resulted in diarrhea after 14 days. Bees from TG did not lag behind other bees in head, thorax and abdomen weight after 28 days. We demonstrated that processed yellow mealworm larvae (T. molitor) can be used as an ingredient for honey bee feed.
PB  - Informa UK Limited
T2  - Journal of Apicultural Research
T1  - In pursuit of the ultimate pollen substitute (insect larvae) for honey bee (Apis mellifera) feed
VL  - 62
IS  - 5
SP  - 1007
EP  - 1016
DO  - 10.1080/00218839.2022.2080950
ER  - 

@article{
author = "Pavlović, Ratko and Dojnov, Biljana and Šokarda Slavić, Marinela and Pavlović, Marija and Slomo, Katarina and Ristović, Marina and Vujčić, Zoran",
year = "2023",
abstract = "Finding a pollen substitute for honey bees that is nutritionally adequate and affordable is a scientific and practical challenge. We attempted a new rational approach and tried to exploit honey bees’ natural cannibalistic behavior. We tested processed insect larvae as a food source that is nutritionally similar to bee brood, and which can easily be produced on a large scale. In cage experiments, monitoring bee mortality, food consumption and changes in bee body parts’ weights showed that flour obtained by grinding dried yellow mealworm larvae has the potential to become an excellent component for pollen substitution. Bees from the cage group fed Tenebrio molitor patties (TG) demonstrated overall best results in comparison to sugar patties fed bee group (CG), yeast patties fed bee group (YG) and pollen patties fed bee group (PG). They did not lose weight as rapidly as the CG, did not defecate inside cages as the YG, nor show increased mortality as the PG. At the same time, TG consumed less food (mean 13.7 g/cage) than CG (16.8 g/cage), YG (20.4 g/cage) and PG (23.9 g/cage) within the period of 28 days. Bees’ gut increase in weight was lowest in the CG, followed by TG and PG and was the highest in the YG which resulted in diarrhea after 14 days. Bees from TG did not lag behind other bees in head, thorax and abdomen weight after 28 days. We demonstrated that processed yellow mealworm larvae (T. molitor) can be used as an ingredient for honey bee feed.",
publisher = "Informa UK Limited",
journal = "Journal of Apicultural Research",
title = "In pursuit of the ultimate pollen substitute (insect larvae) for honey bee (Apis mellifera) feed",
volume = "62",
number = "5",
pages = "1007-1016",
doi = "10.1080/00218839.2022.2080950"
}

Pavlović, R., Dojnov, B., Šokarda Slavić, M., Pavlović, M., Slomo, K., Ristović, M.,& Vujčić, Z.. (2023). In pursuit of the ultimate pollen substitute (insect larvae) for honey bee (Apis mellifera) feed. in Journal of Apicultural Research
Informa UK Limited., 62(5), 1007-1016.
https://doi.org/10.1080/00218839.2022.2080950

Pavlović R, Dojnov B, Šokarda Slavić M, Pavlović M, Slomo K, Ristović M, Vujčić Z. In pursuit of the ultimate pollen substitute (insect larvae) for honey bee (Apis mellifera) feed. in Journal of Apicultural Research. 2023;62(5):1007-1016.
doi:10.1080/00218839.2022.2080950 .

Pavlović, Ratko, Dojnov, Biljana, Šokarda Slavić, Marinela, Pavlović, Marija, Slomo, Katarina, Ristović, Marina, Vujčić, Zoran, "In pursuit of the ultimate pollen substitute (insect larvae) for honey bee (Apis mellifera) feed" in Journal of Apicultural Research, 62, no. 5 (2023):1007-1016,
https://doi.org/10.1080/00218839.2022.2080950 . .

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  - https://cer.ihtm.bg.ac.rs/handle/123456789/5840
AB  - Pectinases are widely used in the fruit juice industry for clarification, liquefaction and stabilization of juices. 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 sediment. 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  - Serbian Biochemical Society
C3  - Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia
T1  - Production and application of pectinases in the liquefaction of apricot and blueberry juice
SP  - 115
EP  - 116
UR  - https://hdl.handle.net/21.15107/rcub_cer_5840
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 juices. 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 sediment. 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, Serbian Biochemical Society",
journal = "Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia",
title = "Production and application of pectinases in the liquefaction of apricot and blueberry juice",
pages = "115-116",
url = "https://hdl.handle.net/21.15107/rcub_cer_5840"
}

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 Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia
University of Belgrade - Faculty of Chemistry., 115-116.
https://hdl.handle.net/21.15107/rcub_cer_5840

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 Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia. 2022;:115-116.
https://hdl.handle.net/21.15107/rcub_cer_5840 .

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 Proceedings - XI Conference of Serbian Biochemical Society "Amazing Biochemistry", 22.09.2022. Novi Sad, Serbia (2022):115-116,
https://hdl.handle.net/21.15107/rcub_cer_5840 .

TY  - CONF
AU  - Pavlović, Ratko
AU  - Dojnov, Biljana
AU  - Šokarda Slavić, Marinela
AU  - Pavlović, Marija
AU  - Tomić, Nevena
AU  - Mišić, Milan
AU  - Vujčić, Zoran
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5885
AB  - Feeding of honey bee (Apis mellifera) is a challenge for beekeepers and formulation of food supplements is improved continuously. When natural food sources are scarce or not available, supplemental foods are widely used to support and build up honey bee colonies. Influence of commercial (sugar) patty and the patties enriched with 12.5% pollen and 12.5% dried yeast on protease expression in honey bee adults is presented. This is part of a wider study aimed to compare the expression of digestive enzymes using different patties. Data collected in this study can be useful for development of higher quality of food supplements for honey bees.
Honey bees were kept in an incubator for 21 days, at a temperature of 35°C and at 80% humidity. In each cage there were one hundred bees and a piece of honeycomb. Midgut samples were taken after 7, 14 and 21 days, homogenized and analyzed for protein concentration and protease activity.
The highest protein concentration was detected in the midgut of pollen fed bees, and lowest in commercial patty fed group, determined by the Bradford method. Protease activity was the highest in bee’s midgut fed with pollen patties, and the lowest in bees fed commercial patties which is shown by enzyme assay and by zymograms. There were different protease isoforms present in bees fed pollen, yeast and commercial patties, but the major isoforms were the same.
The observed decrease in protease activity over time in all groups is probably due to the transition to foraging tasks. Reduced protease activity in the gut of bees fed commercial patties is due to a lack of proteins or some other inducers present in food.
Because pollen is honey bee natural food, we conclude that food supplements that induce similar enzyme expression as pollen (dried yeast) can be considered as appropriate food substitution, because it is superior to supplements which induce very different enzyme expression.
PB  - University of Belgrade – Faculty of Biology
C3  - Abstract Book - 9th European Congress of Apidology - EurBee 9, September 20-22, 2022, Belgrade, Serbia
T1  - Expression of protease in adult honey bees fed with different patties
SP  - 172
UR  - https://hdl.handle.net/21.15107/rcub_cer_5885
ER  - 

@conference{
author = "Pavlović, Ratko and Dojnov, Biljana and Šokarda Slavić, Marinela and Pavlović, Marija and Tomić, Nevena and Mišić, Milan and Vujčić, Zoran",
year = "2022",
abstract = "Feeding of honey bee (Apis mellifera) is a challenge for beekeepers and formulation of food supplements is improved continuously. When natural food sources are scarce or not available, supplemental foods are widely used to support and build up honey bee colonies. Influence of commercial (sugar) patty and the patties enriched with 12.5% pollen and 12.5% dried yeast on protease expression in honey bee adults is presented. This is part of a wider study aimed to compare the expression of digestive enzymes using different patties. Data collected in this study can be useful for development of higher quality of food supplements for honey bees.
Honey bees were kept in an incubator for 21 days, at a temperature of 35°C and at 80% humidity. In each cage there were one hundred bees and a piece of honeycomb. Midgut samples were taken after 7, 14 and 21 days, homogenized and analyzed for protein concentration and protease activity.
The highest protein concentration was detected in the midgut of pollen fed bees, and lowest in commercial patty fed group, determined by the Bradford method. Protease activity was the highest in bee’s midgut fed with pollen patties, and the lowest in bees fed commercial patties which is shown by enzyme assay and by zymograms. There were different protease isoforms present in bees fed pollen, yeast and commercial patties, but the major isoforms were the same.
The observed decrease in protease activity over time in all groups is probably due to the transition to foraging tasks. Reduced protease activity in the gut of bees fed commercial patties is due to a lack of proteins or some other inducers present in food.
Because pollen is honey bee natural food, we conclude that food supplements that induce similar enzyme expression as pollen (dried yeast) can be considered as appropriate food substitution, because it is superior to supplements which induce very different enzyme expression.",
publisher = "University of Belgrade – Faculty of Biology",
journal = "Abstract Book - 9th European Congress of Apidology - EurBee 9, September 20-22, 2022, Belgrade, Serbia",
title = "Expression of protease in adult honey bees fed with different patties",
pages = "172",
url = "https://hdl.handle.net/21.15107/rcub_cer_5885"
}

Pavlović, R., Dojnov, B., Šokarda Slavić, M., Pavlović, M., Tomić, N., Mišić, M.,& Vujčić, Z.. (2022). Expression of protease in adult honey bees fed with different patties. in Abstract Book - 9th European Congress of Apidology - EurBee 9, September 20-22, 2022, Belgrade, Serbia
University of Belgrade – Faculty of Biology., 172.
https://hdl.handle.net/21.15107/rcub_cer_5885

Pavlović R, Dojnov B, Šokarda Slavić M, Pavlović M, Tomić N, Mišić M, Vujčić Z. Expression of protease in adult honey bees fed with different patties. in Abstract Book - 9th European Congress of Apidology - EurBee 9, September 20-22, 2022, Belgrade, Serbia. 2022;:172.
https://hdl.handle.net/21.15107/rcub_cer_5885 .

Pavlović, Ratko, Dojnov, Biljana, Šokarda Slavić, Marinela, Pavlović, Marija, Tomić, Nevena, Mišić, Milan, Vujčić, Zoran, "Expression of protease in adult honey bees fed with different patties" in Abstract Book - 9th European Congress of Apidology - EurBee 9, September 20-22, 2022, Belgrade, Serbia (2022):172,
https://hdl.handle.net/21.15107/rcub_cer_5885 .

TY  - CONF
AU  - Pavlović, Marija
AU  - Stojanović, Sanja
AU  - Dojnov, Biljana
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Margetić, Aleksandra
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5834
AB  - Pectinolytic enzymes represent a large group of enzymes that catalyze the reactions of depolymerization and deesterification of pectin polysaccharides1. Saprophytic fungi produce pectinases on a large scale for industrial purposes. These enzymes have a various biotechnological application and their global annual production represents 25% of total industrial enzymes 1,2. Agro-waste is widely used as economical substrate for the production of pectinases by solid state fermentation 3. In this study, sugar beet pulp, as a good source of pectin3, was used as a substrate for enzyme production by Aspergillus tubingensis. This strain was isolated from the quince fruit and identified by the molecular DNA marker calmodulin (CaM). SSF was performed with this strain on sugar beet pulp (80%) in combination with wheat bran (20%), a potent substrate for pectinase production 3. The obtained high pectinolytic activity (15 U/mL), determined by 3,5-dinitrosalicylic acid reagent, was in the range of commercial pectinases. Zymography detection, using Ruthenium Red to visualize endo-pectinase activity and pectin-methyl esterase activity revealed several pectinase activity bands. Hydrolysis of different pectin substrates with the obtained pectinase complex was analyzed by thin layer chromatography in order to detect different products such as pectic oligosaccharides, which are emerging prebiotics superior to intact pectin.
PB  - University of Belgrade - Faculty of Chemistry
PB  - Serbian Biochemical Society
C3  - Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia
T1  - Highly active pectinases from newly isolated Aspergillus tubingensis strain
SP  - 124
EP  - 125
UR  - https://hdl.handle.net/21.15107/rcub_cer_5834
ER  - 

@conference{
author = "Pavlović, Marija and Stojanović, Sanja and Dojnov, Biljana and Božić, Nataša and Vujčić, Zoran and Margetić, Aleksandra",
year = "2021",
abstract = "Pectinolytic enzymes represent a large group of enzymes that catalyze the reactions of depolymerization and deesterification of pectin polysaccharides1. Saprophytic fungi produce pectinases on a large scale for industrial purposes. These enzymes have a various biotechnological application and their global annual production represents 25% of total industrial enzymes 1,2. Agro-waste is widely used as economical substrate for the production of pectinases by solid state fermentation 3. In this study, sugar beet pulp, as a good source of pectin3, was used as a substrate for enzyme production by Aspergillus tubingensis. This strain was isolated from the quince fruit and identified by the molecular DNA marker calmodulin (CaM). SSF was performed with this strain on sugar beet pulp (80%) in combination with wheat bran (20%), a potent substrate for pectinase production 3. The obtained high pectinolytic activity (15 U/mL), determined by 3,5-dinitrosalicylic acid reagent, was in the range of commercial pectinases. Zymography detection, using Ruthenium Red to visualize endo-pectinase activity and pectin-methyl esterase activity revealed several pectinase activity bands. Hydrolysis of different pectin substrates with the obtained pectinase complex was analyzed by thin layer chromatography in order to detect different products such as pectic oligosaccharides, which are emerging prebiotics superior to intact pectin.",
publisher = "University of Belgrade - Faculty of Chemistry, Serbian Biochemical Society",
journal = "Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia",
title = "Highly active pectinases from newly isolated Aspergillus tubingensis strain",
pages = "124-125",
url = "https://hdl.handle.net/21.15107/rcub_cer_5834"
}

Pavlović, M., Stojanović, S., Dojnov, B., Božić, N., Vujčić, Z.,& Margetić, A.. (2021). Highly active pectinases from newly isolated Aspergillus tubingensis strain. in Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia
University of Belgrade - Faculty of Chemistry., 124-125.
https://hdl.handle.net/21.15107/rcub_cer_5834

Pavlović M, Stojanović S, Dojnov B, Božić N, Vujčić Z, Margetić A. Highly active pectinases from newly isolated Aspergillus tubingensis strain. in Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia. 2021;:124-125.
https://hdl.handle.net/21.15107/rcub_cer_5834 .

Pavlović, Marija, Stojanović, Sanja, Dojnov, Biljana, Božić, Nataša, Vujčić, Zoran, Margetić, Aleksandra, "Highly active pectinases from newly isolated Aspergillus tubingensis strain" in Proceedings - X Conference of Serbian Biochemical Society with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia (2021):124-125,
https://hdl.handle.net/21.15107/rcub_cer_5834 .

TY  - CONF
AU  - Pavlović, Ratko
AU  - Dojnov, Biljana
AU  - Šokarda Slavić, Marinela
AU  - Pavlović, Marija
AU  - Slomo, Katarina
AU  - Ristović, Marina
AU  - Vujčić, Zoran
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5886
AB  - Fed of honey bee (Apis mellifera) is challenging for beekeepers and formulation of supplemental food is improved continuously. When natural food sources are scarce or not available, supplemental foods are widely used to support and build up honey bee colonies. Influence of commercial patty and patty enriched with 12.5% pollen on amylase expression in honey bee adults is presented. This
is part of a wider study aimed to compare the activity of digestive enzymes when using different patties. We assume that data collected in this way can be used for the development of better food supplements for honey bees.
Honey bees were kept in an incubator for 21 days, at a temperature of 35°C and at 80% humidity. In each cage, there were one hundred bees and a piece of honeycomb. Midgut and hindgut samples were taken after 7, 14 and 21 days and midgut without hindgut was taken after 21 days. Samples were homogenized and used for amylase zymogram, IEF and enzyme assays.
There was no mortality during the experiment. A high protein concentration was detected in the midgut in both groups of bees. Amylase activity was significantly higher in bees fed pollen enriched patties, which is shown by enzyme assay and by zymograms. There are different amylase isoforms present in bees fed by pollen enriched patties in comparison to bees fed by commercial patties, but
the major isoforms were the same.
The observed decrease in the amylase activity over time is probably due to dilution caused by the accumulation of water and undigested substances in the hindgut. Reduced amylase activity in the intestines of bees fed by commercial patties is due to a lack of starch or some other inducers present in pollen.
Because pollen is honey bee natural food, we conclude that food supplements that induce similar enzyme expression as pollen can be superior in comparison to supplements that induce very different enzyme expression.
PB  - Belgrade : University of Belgrade
C3  - Book of Abstracts - 2nd UNIFood International Conference - UNIFood2021, September 24-25, 2021, Belgrade, Serbia
T1  - Expression of amylases in adult honey bees fed with different patties
SP  - 196
UR  - https://hdl.handle.net/21.15107/rcub_cer_5886
ER  - 

@conference{
author = "Pavlović, Ratko and Dojnov, Biljana and Šokarda Slavić, Marinela and Pavlović, Marija and Slomo, Katarina and Ristović, Marina and Vujčić, Zoran",
year = "2021",
abstract = "Fed of honey bee (Apis mellifera) is challenging for beekeepers and formulation of supplemental food is improved continuously. When natural food sources are scarce or not available, supplemental foods are widely used to support and build up honey bee colonies. Influence of commercial patty and patty enriched with 12.5% pollen on amylase expression in honey bee adults is presented. This
is part of a wider study aimed to compare the activity of digestive enzymes when using different patties. We assume that data collected in this way can be used for the development of better food supplements for honey bees.
Honey bees were kept in an incubator for 21 days, at a temperature of 35°C and at 80% humidity. In each cage, there were one hundred bees and a piece of honeycomb. Midgut and hindgut samples were taken after 7, 14 and 21 days and midgut without hindgut was taken after 21 days. Samples were homogenized and used for amylase zymogram, IEF and enzyme assays.
There was no mortality during the experiment. A high protein concentration was detected in the midgut in both groups of bees. Amylase activity was significantly higher in bees fed pollen enriched patties, which is shown by enzyme assay and by zymograms. There are different amylase isoforms present in bees fed by pollen enriched patties in comparison to bees fed by commercial patties, but
the major isoforms were the same.
The observed decrease in the amylase activity over time is probably due to dilution caused by the accumulation of water and undigested substances in the hindgut. Reduced amylase activity in the intestines of bees fed by commercial patties is due to a lack of starch or some other inducers present in pollen.
Because pollen is honey bee natural food, we conclude that food supplements that induce similar enzyme expression as pollen can be superior in comparison to supplements that induce very different enzyme expression.",
publisher = "Belgrade : University of Belgrade",
journal = "Book of Abstracts - 2nd UNIFood International Conference - UNIFood2021, September 24-25, 2021, Belgrade, Serbia",
title = "Expression of amylases in adult honey bees fed with different patties",
pages = "196",
url = "https://hdl.handle.net/21.15107/rcub_cer_5886"
}

Pavlović, R., Dojnov, B., Šokarda Slavić, M., Pavlović, M., Slomo, K., Ristović, M.,& Vujčić, Z.. (2021). Expression of amylases in adult honey bees fed with different patties. in Book of Abstracts - 2nd UNIFood International Conference - UNIFood2021, September 24-25, 2021, Belgrade, Serbia
Belgrade : University of Belgrade., 196.
https://hdl.handle.net/21.15107/rcub_cer_5886

Pavlović R, Dojnov B, Šokarda Slavić M, Pavlović M, Slomo K, Ristović M, Vujčić Z. Expression of amylases in adult honey bees fed with different patties. in Book of Abstracts - 2nd UNIFood International Conference - UNIFood2021, September 24-25, 2021, Belgrade, Serbia. 2021;:196.
https://hdl.handle.net/21.15107/rcub_cer_5886 .

Pavlović, Ratko, Dojnov, Biljana, Šokarda Slavić, Marinela, Pavlović, Marija, Slomo, Katarina, Ristović, Marina, Vujčić, Zoran, "Expression of amylases in adult honey bees fed with different patties" in Book of Abstracts - 2nd UNIFood International Conference - UNIFood2021, September 24-25, 2021, Belgrade, Serbia (2021):196,
https://hdl.handle.net/21.15107/rcub_cer_5886 .