Jović-Jovičić, Nataša

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Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite

Kosić, Višnja; Božić, Nataša; Dojnov, Biljana; Banković, Predrag; Jović-Jovičić, Nataša; Knežević-Jugović, Zorica; Milutinović-Nikolić, Aleksandra

(Elsevier Ltd., 2024-03)

TY  - JOUR
AU  - Kosić, Višnja
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Banković, Predrag
AU  - Jović-Jovičić, Nataša
AU  - Knežević-Jugović, Zorica
AU  - Milutinović-Nikolić, Aleksandra
PY  - 2024-03
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/7279
AB  - Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.
PB  - Elsevier Ltd.
T2  - Applied Clay Science
T1  - Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite
SP  - 107289
VL  - 250
DO  - 10.1016/j.clay.2024.107289
ER  - 
@article{
author = "Kosić, Višnja and Božić, Nataša and Dojnov, Biljana and Banković, Predrag and Jović-Jovičić, Nataša and Knežević-Jugović, Zorica and Milutinović-Nikolić, Aleksandra",
year = "2024-03",
abstract = "Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.",
publisher = "Elsevier Ltd.",
journal = "Applied Clay Science",
title = "Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite",
pages = "107289",
volume = "250",
doi = "10.1016/j.clay.2024.107289"
}
Kosić, V., Božić, N., Dojnov, B., Banković, P., Jović-Jovičić, N., Knežević-Jugović, Z.,& Milutinović-Nikolić, A.. (2024-03). Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. in Applied Clay Science
Elsevier Ltd.., 250, 107289.
https://doi.org/10.1016/j.clay.2024.107289
Kosić V, Božić N, Dojnov B, Banković P, Jović-Jovičić N, Knežević-Jugović Z, Milutinović-Nikolić A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. in Applied Clay Science. 2024;250:107289.
doi:10.1016/j.clay.2024.107289 .
Kosić, Višnja, Božić, Nataša, Dojnov, Biljana, Banković, Predrag, Jović-Jovičić, Nataša, Knežević-Jugović, Zorica, Milutinović-Nikolić, Aleksandra, "Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite" in Applied Clay Science, 250 (2024-03):107289,
https://doi.org/10.1016/j.clay.2024.107289 . .

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

Kosić, Višnja; Božić, Nataša; Dojnov, Biljana; Banković, Predrag; Jović-Jovičić, Nataša; Knežević-Jugović, Zorica; Milutinović-Nikolić, Aleksandra

(Elsevier Ltd., 2024)

TY  - DATA
AU  - Kosić, Višnja
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Banković, Predrag
AU  - Jović-Jovičić, Nataša
AU  - Knežević-Jugović, Zorica
AU  - Milutinović-Nikolić, Aleksandra
PY  - 2024
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/7330
AB  - Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.
PB  - Elsevier Ltd.
T2  - Applied Clay Science
T1  - Supplementary material for the article: Kosić, V.; Božić, B.; Dojnov, B.; Banković, P.; Jović-Jovičić, N.; Knežević-Jugović, Z.; Milutinović-Nikolić, A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. Applied Clay Science 2024, 250, 107289. https://doi.org/10.1016/j.clay.2024.107289
SP  - 107289
VL  - 250
UR  - https://hdl.handle.net/21.15107/rcub_technorep_7330
ER  - 
@misc{
author = "Kosić, Višnja and Božić, Nataša and Dojnov, Biljana and Banković, Predrag and Jović-Jovičić, Nataša and Knežević-Jugović, Zorica and Milutinović-Nikolić, Aleksandra",
year = "2024",
abstract = "Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.",
publisher = "Elsevier Ltd.",
journal = "Applied Clay Science",
title = "Supplementary material for the article: Kosić, V.; Božić, B.; Dojnov, B.; Banković, P.; Jović-Jovičić, N.; Knežević-Jugović, Z.; Milutinović-Nikolić, A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. Applied Clay Science 2024, 250, 107289. https://doi.org/10.1016/j.clay.2024.107289",
pages = "107289",
volume = "250",
url = "https://hdl.handle.net/21.15107/rcub_technorep_7330"
}
Kosić, V., Božić, N., Dojnov, B., Banković, P., Jović-Jovičić, N., Knežević-Jugović, Z.,& Milutinović-Nikolić, A.. (2024). Supplementary material for the article: Kosić, V.; Božić, B.; Dojnov, B.; Banković, P.; Jović-Jovičić, N.; Knežević-Jugović, Z.; Milutinović-Nikolić, A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. Applied Clay Science 2024, 250, 107289. https://doi.org/10.1016/j.clay.2024.107289. in Applied Clay Science
Elsevier Ltd.., 250, 107289.
https://hdl.handle.net/21.15107/rcub_technorep_7330
Kosić V, Božić N, Dojnov B, Banković P, Jović-Jovičić N, Knežević-Jugović Z, Milutinović-Nikolić A. Supplementary material for the article: Kosić, V.; Božić, B.; Dojnov, B.; Banković, P.; Jović-Jovičić, N.; Knežević-Jugović, Z.; Milutinović-Nikolić, A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. Applied Clay Science 2024, 250, 107289. https://doi.org/10.1016/j.clay.2024.107289. in Applied Clay Science. 2024;250:107289.
https://hdl.handle.net/21.15107/rcub_technorep_7330 .
Kosić, Višnja, Božić, Nataša, Dojnov, Biljana, Banković, Predrag, Jović-Jovičić, Nataša, Knežević-Jugović, Zorica, Milutinović-Nikolić, Aleksandra, "Supplementary material for the article: Kosić, V.; Božić, B.; Dojnov, B.; Banković, P.; Jović-Jovičić, N.; Knežević-Jugović, Z.; Milutinović-Nikolić, A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. Applied Clay Science 2024, 250, 107289. https://doi.org/10.1016/j.clay.2024.107289" in Applied Clay Science, 250 (2024):107289,
https://hdl.handle.net/21.15107/rcub_technorep_7330 .

Co(II) impregnated Al(III)-pillared montmorillonite–Synthesis, characterization and catalytic properties in Oxone® activation for dye degradation

Marković, Marija; Marinović, Sanja; Mudrinić, Tihana; Ajduković, Marija; Jović-Jovičić, Nataša; Mojović, Zorica; Orlić, Jovana; Milutinović Nikolić, Aleksandra; Banković, Predrag

(Elsevier, 2019)

TY  - JOUR
AU  - Marković, Marija
AU  - Marinović, Sanja
AU  - Mudrinić, Tihana
AU  - Ajduković, Marija
AU  - Jović-Jovičić, Nataša
AU  - Mojović, Zorica
AU  - Orlić, Jovana
AU  - Milutinović Nikolić, Aleksandra
AU  - Banković, Predrag
PY  - 2019
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5883
AB  - Aluminum pillared clay was synthesized and impregnated with Co2+ (CoAP), using incipient wetness impregnation method. The obtained CoAP was characterized by chemical analysis, XRPD, SEM with EDS, XPS and low temperature N2 physisorption. By these methods the incorporation of Co2+ was confirmed in both micro and mesoporous region. The synthesized material was investigated as a catalyst in catalytic oxidation of organic water pollutants – dyes – in the presence of Oxone® (peroxymonosulfate). Oxone® is a precursor of sulfate radicals. Tartrazine was chosen as a model dye pollutant. The influence of the mass of the catalyst, temperature and initial pH was investigated. Temperature increase was beneficial for dye degradation rate. The reaction rate was the highest for initial pH values around those corresponding to neutral conditions, somewhat slower for pH < 4 values, while for pH > 10 decolorization was significantly less expressed. Along with decolorization of tartrazine solution the formation and degradation of tartrazine catalytic oxidation products were monitored using UV–Vis spectroscopy. CoAP was found to be efficient catalyst in Oxone® induced catalytic degradation of both tartrazine and detected products of its degradation.
PB  - Elsevier
T2  - Applied Clay Science
T1  - Co(II) impregnated Al(III)-pillared montmorillonite–Synthesis, characterization and catalytic properties in Oxone® activation for dye degradation
SP  - 105276
VL  - 182
DO  - 10.1016/j.clay.2019.105276
ER  - 
@article{
author = "Marković, Marija and Marinović, Sanja and Mudrinić, Tihana and Ajduković, Marija and Jović-Jovičić, Nataša and Mojović, Zorica and Orlić, Jovana and Milutinović Nikolić, Aleksandra and Banković, Predrag",
year = "2019",
abstract = "Aluminum pillared clay was synthesized and impregnated with Co2+ (CoAP), using incipient wetness impregnation method. The obtained CoAP was characterized by chemical analysis, XRPD, SEM with EDS, XPS and low temperature N2 physisorption. By these methods the incorporation of Co2+ was confirmed in both micro and mesoporous region. The synthesized material was investigated as a catalyst in catalytic oxidation of organic water pollutants – dyes – in the presence of Oxone® (peroxymonosulfate). Oxone® is a precursor of sulfate radicals. Tartrazine was chosen as a model dye pollutant. The influence of the mass of the catalyst, temperature and initial pH was investigated. Temperature increase was beneficial for dye degradation rate. The reaction rate was the highest for initial pH values around those corresponding to neutral conditions, somewhat slower for pH < 4 values, while for pH > 10 decolorization was significantly less expressed. Along with decolorization of tartrazine solution the formation and degradation of tartrazine catalytic oxidation products were monitored using UV–Vis spectroscopy. CoAP was found to be efficient catalyst in Oxone® induced catalytic degradation of both tartrazine and detected products of its degradation.",
publisher = "Elsevier",
journal = "Applied Clay Science",
title = "Co(II) impregnated Al(III)-pillared montmorillonite–Synthesis, characterization and catalytic properties in Oxone® activation for dye degradation",
pages = "105276",
volume = "182",
doi = "10.1016/j.clay.2019.105276"
}
Marković, M., Marinović, S., Mudrinić, T., Ajduković, M., Jović-Jovičić, N., Mojović, Z., Orlić, J., Milutinović Nikolić, A.,& Banković, P.. (2019). Co(II) impregnated Al(III)-pillared montmorillonite–Synthesis, characterization and catalytic properties in Oxone® activation for dye degradation. in Applied Clay Science
Elsevier., 182, 105276.
https://doi.org/10.1016/j.clay.2019.105276
Marković M, Marinović S, Mudrinić T, Ajduković M, Jović-Jovičić N, Mojović Z, Orlić J, Milutinović Nikolić A, Banković P. Co(II) impregnated Al(III)-pillared montmorillonite–Synthesis, characterization and catalytic properties in Oxone® activation for dye degradation. in Applied Clay Science. 2019;182:105276.
doi:10.1016/j.clay.2019.105276 .
Marković, Marija, Marinović, Sanja, Mudrinić, Tihana, Ajduković, Marija, Jović-Jovičić, Nataša, Mojović, Zorica, Orlić, Jovana, Milutinović Nikolić, Aleksandra, Banković, Predrag, "Co(II) impregnated Al(III)-pillared montmorillonite–Synthesis, characterization and catalytic properties in Oxone® activation for dye degradation" in Applied Clay Science, 182 (2019):105276,
https://doi.org/10.1016/j.clay.2019.105276 . .
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