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  - http://intor.torlakinstitut.com/handle/123456789/936
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
EP  - 31
SP  - 31
UR  - https://hdl.handle.net/21.15107/rcub_intor_936
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_intor_936"
}

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_intor_936

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_intor_936 .

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_intor_936 .

TY  - JOUR
AU  - Pavlović, Marija
AU  - Slavić, Marinela Šokarda
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Drulović, Nenad
AU  - Vujčić, Zoran
PY  - 2024
UR  - http://intor.torlakinstitut.com/handle/123456789/888
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
SP  - 140030
DO  - 10.1016/j.foodchem.2024.140030
ER  - 

@article{
author = "Pavlović, Marija and Slavić, Marinela Šokarda 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",
pages = "140030",
doi = "10.1016/j.foodchem.2024.140030"
}

Pavlović, M., Slavić, M. Š., 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., 140030.
https://doi.org/10.1016/j.foodchem.2024.140030

Pavlović M, Slavić MŠ, 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;:140030.
doi:10.1016/j.foodchem.2024.140030 .

Pavlović, Marija, Slavić, Marinela Šokarda, 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 (2024):140030,
https://doi.org/10.1016/j.foodchem.2024.140030 . .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Pavlović, Marija
AU  - Nikolić, Stefan
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/635
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-cellotriosylD-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 b-glucan-based food products using Bacillus subtilis 168 endo-b-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-cellotriosylD-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 b-glucan-based food products using Bacillus subtilis 168 endo-b-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 b-glucan-based food products using Bacillus subtilis 168 endo-b-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 b-glucan-based food products using Bacillus subtilis 168 endo-b-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 b-glucan-based food products using Bacillus subtilis 168 endo-b-1,3-1,4-glucanase" in International Journal of Food Science and Technology (2023),
https://doi.org/10.1111/ijfs.16647 . .