Bebić, Jelena

Link to this page

Authority KeyName Variants
60b2d25d-1d91-4abc-b8c6-18f08c4d09c4
  • Bebić, Jelena (2)
  • Bebić, Jelena M. (1)

Author's Bibliography

Immobilization of laccase from Trametes versicolor on Lifetech (TM) supports for applications in degradation of industrial dyes

Bebić, Jelena M.; Banjanac, Katarina M.; Ćorović, Marija M.; Milivojević, Ana D.; Simović, Milica B.; Vukoičić, Ana Ž.; Mitrović, Danica D.; Bezbradica, Dejan I.

(Savez hemijskih inženjera, 2020)

TY  - JOUR
AU  - Bebić, Jelena M.
AU  - Banjanac, Katarina M.
AU  - Ćorović, Marija M.
AU  - Milivojević, Ana D.
AU  - Simović, Milica B.
AU  - Vukoičić, Ana Ž.
AU  - Mitrović, Danica D.
AU  - Bezbradica, Dejan I.
PY  - 2020
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4374
AB  - In this study, immobilization of laccase from Trametes versicolor on eight Lifetech (TM) supports, with different characteristics (pore size, length of the spacer arm and functional groups), was studied and optimized for intended use in bioremediation for decolorization of industrial wastewaters. Out of six tested amino-functionalized supports, the most promising carrier was proved to be porous Lifetech (TM) ECR8309F with primary amino groups and a C2 spacer arm. Onto this support, laccase is attached by forming electrostatic interactions so that the most active preparation has shown the activity of 66876 U/g support. On the other hand, during immobilization of laccase on epoxy-functionalized Lifetech (TM) ECR8285F, via hydrophobic interactions and covalent bonding confirmed by a desorption assay, immobilization yield of 60 % and the activity of 118929 U/g were accomplished. Furthermore, immobilized enzyme on this support showed high capacity for decolorization of dyes (Lanaset (R) Violet B, Lanaset (R) Blue 2R, bromothymol blue and bromocresol green), by combination of both adsorption and enzyme degradation. Decolorization was in the range of 88 to 96 % after 4 h, with more than 80 % achieved after only 45 min. Also, this preparation demonstrated high operational stability during seven consecutive reuses in all examined dye reaction systems.
AB  - U ovom radu je ispitivana i optimizovana imobilizacija lakaze producenta Trametes
versicolor na osam Lifetech™nosača, različitih karakteristika (kao što su veličina pora,
dužina “nožice” i funkcionalne grupe), za predviđenu namenu u bioremedijaciji radi
obezbojavanja industrijskih otpadnih voda. Od šest ispitanih amino-funkcionalizovanih nosača, kao najadekvatniji se pokazao porozni Lifetech™ ECR8309F nosač sa
primarnim amino grupama i C2 “nožicom”. Na ovaj nosač lakaza se vezuje formiranjem
elektrostatičkih interakcija i dobijeni preparat je imao aktivnost od 66876 U/g nosača.
Nasuprot tome, prilikom imobilizacije lakaze na epoksi/butil metakrilatni nosač
Lifetech™ ECR8285F, hidrofobnim interakcijama i kovalentnim vezama, što je
potvrđeno tretmanom imobilisanog preparata desorpcionim sredstvima, postignut je
prinos imobilizacije proteina od 60 %, a dobijena je aktivnost od 118929 U/g. Pored
toga, preparat ECR8285F-lakaza pokazao je veliku aktivnost u obezbojavanju boja
(Lanaset® Violet B, Lanaset® Blue 2R, bromtimol plavo i bromkrezol zeleno)
kombinacijom adsorpcije i enzimske razgradnje, u opsegu obezbojavanja od 88 % do
96 % nakon 4 h, sa više od 80 % obezbojavanja postignutog nakon samo 45 min.
Takođe, ovaj preparat je pokazao veliku operativnu stabilnost tokom 7 uzastopnih
ponovnih upotreba u svim ispitanim reakcionim sistemima.
PB  - Savez hemijskih inženjera
T2  - Hemijska industrija
T1  - Immobilization of laccase from Trametes versicolor on Lifetech (TM) supports for applications in degradation of industrial dyes
T1  - Imobilizacija lakaze producenta Trametes versicolor na Lifetech (TM) nosače u cilju primene u razgradnji industrijskih boja
EP  - 209
IS  - 3
SP  - 197
VL  - 74
DO  - 10.2298/HEMIND200320016B
ER  - 
@article{
author = "Bebić, Jelena M. and Banjanac, Katarina M. and Ćorović, Marija M. and Milivojević, Ana D. and Simović, Milica B. and Vukoičić, Ana Ž. and Mitrović, Danica D. and Bezbradica, Dejan I.",
year = "2020",
abstract = "In this study, immobilization of laccase from Trametes versicolor on eight Lifetech (TM) supports, with different characteristics (pore size, length of the spacer arm and functional groups), was studied and optimized for intended use in bioremediation for decolorization of industrial wastewaters. Out of six tested amino-functionalized supports, the most promising carrier was proved to be porous Lifetech (TM) ECR8309F with primary amino groups and a C2 spacer arm. Onto this support, laccase is attached by forming electrostatic interactions so that the most active preparation has shown the activity of 66876 U/g support. On the other hand, during immobilization of laccase on epoxy-functionalized Lifetech (TM) ECR8285F, via hydrophobic interactions and covalent bonding confirmed by a desorption assay, immobilization yield of 60 % and the activity of 118929 U/g were accomplished. Furthermore, immobilized enzyme on this support showed high capacity for decolorization of dyes (Lanaset (R) Violet B, Lanaset (R) Blue 2R, bromothymol blue and bromocresol green), by combination of both adsorption and enzyme degradation. Decolorization was in the range of 88 to 96 % after 4 h, with more than 80 % achieved after only 45 min. Also, this preparation demonstrated high operational stability during seven consecutive reuses in all examined dye reaction systems., U ovom radu je ispitivana i optimizovana imobilizacija lakaze producenta Trametes
versicolor na osam Lifetech™nosača, različitih karakteristika (kao što su veličina pora,
dužina “nožice” i funkcionalne grupe), za predviđenu namenu u bioremedijaciji radi
obezbojavanja industrijskih otpadnih voda. Od šest ispitanih amino-funkcionalizovanih nosača, kao najadekvatniji se pokazao porozni Lifetech™ ECR8309F nosač sa
primarnim amino grupama i C2 “nožicom”. Na ovaj nosač lakaza se vezuje formiranjem
elektrostatičkih interakcija i dobijeni preparat je imao aktivnost od 66876 U/g nosača.
Nasuprot tome, prilikom imobilizacije lakaze na epoksi/butil metakrilatni nosač
Lifetech™ ECR8285F, hidrofobnim interakcijama i kovalentnim vezama, što je
potvrđeno tretmanom imobilisanog preparata desorpcionim sredstvima, postignut je
prinos imobilizacije proteina od 60 %, a dobijena je aktivnost od 118929 U/g. Pored
toga, preparat ECR8285F-lakaza pokazao je veliku aktivnost u obezbojavanju boja
(Lanaset® Violet B, Lanaset® Blue 2R, bromtimol plavo i bromkrezol zeleno)
kombinacijom adsorpcije i enzimske razgradnje, u opsegu obezbojavanja od 88 % do
96 % nakon 4 h, sa više od 80 % obezbojavanja postignutog nakon samo 45 min.
Takođe, ovaj preparat je pokazao veliku operativnu stabilnost tokom 7 uzastopnih
ponovnih upotreba u svim ispitanim reakcionim sistemima.",
publisher = "Savez hemijskih inženjera",
journal = "Hemijska industrija",
title = "Immobilization of laccase from Trametes versicolor on Lifetech (TM) supports for applications in degradation of industrial dyes, Imobilizacija lakaze producenta Trametes versicolor na Lifetech (TM) nosače u cilju primene u razgradnji industrijskih boja",
pages = "209-197",
number = "3",
volume = "74",
doi = "10.2298/HEMIND200320016B"
}
Bebić, J. M., Banjanac, K. M., Ćorović, M. M., Milivojević, A. D., Simović, M. B., Vukoičić, A. Ž., Mitrović, D. D.,& Bezbradica, D. I.. (2020). Immobilization of laccase from Trametes versicolor on Lifetech (TM) supports for applications in degradation of industrial dyes. in Hemijska industrija
Savez hemijskih inženjera., 74(3), 197-209.
https://doi.org/10.2298/HEMIND200320016B
Bebić JM, Banjanac KM, Ćorović MM, Milivojević AD, Simović MB, Vukoičić AŽ, Mitrović DD, Bezbradica DI. Immobilization of laccase from Trametes versicolor on Lifetech (TM) supports for applications in degradation of industrial dyes. in Hemijska industrija. 2020;74(3):197-209.
doi:10.2298/HEMIND200320016B .
Bebić, Jelena M., Banjanac, Katarina M., Ćorović, Marija M., Milivojević, Ana D., Simović, Milica B., Vukoičić, Ana Ž., Mitrović, Danica D., Bezbradica, Dejan I., "Immobilization of laccase from Trametes versicolor on Lifetech (TM) supports for applications in degradation of industrial dyes" in Hemijska industrija, 74, no. 3 (2020):197-209,
https://doi.org/10.2298/HEMIND200320016B . .
3
1

Immobilization of laccase from Myceliophthora thermophila on functionalized silica nanoparticles: Optimization and application in lindane degradation

Bebić, Jelena; Banjanac, Katarina; Ćorović, Marija; Milivojević, Ana; Simović, Milica; Marinković, Aleksandar; Bezbradica, Dejan

(Chemical Industry Press Co Ltd, Beijing, 2020)

TY  - JOUR
AU  - Bebić, Jelena
AU  - Banjanac, Katarina
AU  - Ćorović, Marija
AU  - Milivojević, Ana
AU  - Simović, Milica
AU  - Marinković, Aleksandar
AU  - Bezbradica, Dejan
PY  - 2020
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4384
AB  - This work is focused on immobilization of laccase from Myceliophthora thermophila expressed in Aspergillus oiyzae (Novozym 51003 (R) laccase) on amino modified fumed nano-silica (AFNS) and the possible use in bioremediation. Hereby, for the first time, factors affecting the immobilization of Novozym 51003 (R) laccase on AFNS were investigated for defining the immobilization mechanism and optimizing the utilization of AFNS as support for laccase immobilization. The highest specific activity (13.1 IU.mg(-1) proteins) was achieved at offered 160 mg per g of AFNS and for the same offered protein concentration the highest activity immobilization yield, reaching 68.3% after the equilibrium time, at optimum pH 5.0, was obtained. Laccase immobilization occurs by adsorption as monolayer enzyme binding in 40 min, following pseudo-first-order kinetics. The possible use of obtained immobilized preparation was investigated in degradation of pesticide lindane. Within 24 h, lindane concentration was reduced to 56.8% of initial concentration and after seven repeated reuses it retained 70% of the original activity.
PB  - Chemical Industry Press Co Ltd, Beijing
T2  - Chinese Journal of Chemical Engineering
T1  - Immobilization of laccase from Myceliophthora thermophila on functionalized silica nanoparticles: Optimization and application in lindane degradation
EP  - 1144
IS  - 4
SP  - 1136
VL  - 28
DO  - 10.1016/j.cjche.2019.12.025
ER  - 
@article{
author = "Bebić, Jelena and Banjanac, Katarina and Ćorović, Marija and Milivojević, Ana and Simović, Milica and Marinković, Aleksandar and Bezbradica, Dejan",
year = "2020",
abstract = "This work is focused on immobilization of laccase from Myceliophthora thermophila expressed in Aspergillus oiyzae (Novozym 51003 (R) laccase) on amino modified fumed nano-silica (AFNS) and the possible use in bioremediation. Hereby, for the first time, factors affecting the immobilization of Novozym 51003 (R) laccase on AFNS were investigated for defining the immobilization mechanism and optimizing the utilization of AFNS as support for laccase immobilization. The highest specific activity (13.1 IU.mg(-1) proteins) was achieved at offered 160 mg per g of AFNS and for the same offered protein concentration the highest activity immobilization yield, reaching 68.3% after the equilibrium time, at optimum pH 5.0, was obtained. Laccase immobilization occurs by adsorption as monolayer enzyme binding in 40 min, following pseudo-first-order kinetics. The possible use of obtained immobilized preparation was investigated in degradation of pesticide lindane. Within 24 h, lindane concentration was reduced to 56.8% of initial concentration and after seven repeated reuses it retained 70% of the original activity.",
publisher = "Chemical Industry Press Co Ltd, Beijing",
journal = "Chinese Journal of Chemical Engineering",
title = "Immobilization of laccase from Myceliophthora thermophila on functionalized silica nanoparticles: Optimization and application in lindane degradation",
pages = "1144-1136",
number = "4",
volume = "28",
doi = "10.1016/j.cjche.2019.12.025"
}
Bebić, J., Banjanac, K., Ćorović, M., Milivojević, A., Simović, M., Marinković, A.,& Bezbradica, D.. (2020). Immobilization of laccase from Myceliophthora thermophila on functionalized silica nanoparticles: Optimization and application in lindane degradation. in Chinese Journal of Chemical Engineering
Chemical Industry Press Co Ltd, Beijing., 28(4), 1136-1144.
https://doi.org/10.1016/j.cjche.2019.12.025
Bebić J, Banjanac K, Ćorović M, Milivojević A, Simović M, Marinković A, Bezbradica D. Immobilization of laccase from Myceliophthora thermophila on functionalized silica nanoparticles: Optimization and application in lindane degradation. in Chinese Journal of Chemical Engineering. 2020;28(4):1136-1144.
doi:10.1016/j.cjche.2019.12.025 .
Bebić, Jelena, Banjanac, Katarina, Ćorović, Marija, Milivojević, Ana, Simović, Milica, Marinković, Aleksandar, Bezbradica, Dejan, "Immobilization of laccase from Myceliophthora thermophila on functionalized silica nanoparticles: Optimization and application in lindane degradation" in Chinese Journal of Chemical Engineering, 28, no. 4 (2020):1136-1144,
https://doi.org/10.1016/j.cjche.2019.12.025 . .
35
9
30

Amino-modified kraft lignin microspheres as a support for enzyme immobilization

Bebić, Jelena; Banjanac, Katarina; Rusmirović, Jelena; Ćorović, Marija; Milivojević, Ana; Simović, Milica; Marinković, Aleksandar; Bezbradica, Dejan

(Royal Society of Chemistry, 2020)

TY  - JOUR
AU  - Bebić, Jelena
AU  - Banjanac, Katarina
AU  - Rusmirović, Jelena
AU  - Ćorović, Marija
AU  - Milivojević, Ana
AU  - Simović, Milica
AU  - Marinković, Aleksandar
AU  - Bezbradica, Dejan
PY  - 2020
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4510
AB  - In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing beta-galactosidase fromA. oryzaeand laccase fromM. thermophilaexpressed inA. oryzae(Novozym (R) 51003) onto A-LMS. Two types of A-LMS were investigated, with different emulsifier concentrations (5 wt% and 10 wt%), and microspheres produced using 5 wt% of emulsifier (A-LMS_5) showed adequate pore shape, size and distribution for enzyme attachment. The type of interactions formed between enzymes (beta-galactosidase and laccase) and A-LMS_5 microspheres demonstrated that beta-galactosidase is predominantly attachedviaelectrostatic interactions while attachment of laccase is equally governed by electrostatic and hydrophobic interactions. Furthermore, the A-LMS_5-beta-galactosidase exhibited specificity towards recognized prebiotics (galacto-oligosaccharides (GOS)) synthesis with 1.5-times higher GOS production than glucose production, while for environmental pollutant lindane degradation, the immobilized laccase preparation exhibited high activity with a minimum remaining lindane concentration of 22.4% after 6 days. Thus, this novel enzyme immobilization support A-LMS_5 has potential for use in green biotechnologies.
PB  - Royal Society of Chemistry
T2  - RSC Advances
T1  - Amino-modified kraft lignin microspheres as a support for enzyme immobilization
EP  - 21508
IS  - 36
SP  - 21495
VL  - 10
DO  - 10.1039/d0ra03439h
ER  - 
@article{
author = "Bebić, Jelena and Banjanac, Katarina and Rusmirović, Jelena and Ćorović, Marija and Milivojević, Ana and Simović, Milica and Marinković, Aleksandar and Bezbradica, Dejan",
year = "2020",
abstract = "In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing beta-galactosidase fromA. oryzaeand laccase fromM. thermophilaexpressed inA. oryzae(Novozym (R) 51003) onto A-LMS. Two types of A-LMS were investigated, with different emulsifier concentrations (5 wt% and 10 wt%), and microspheres produced using 5 wt% of emulsifier (A-LMS_5) showed adequate pore shape, size and distribution for enzyme attachment. The type of interactions formed between enzymes (beta-galactosidase and laccase) and A-LMS_5 microspheres demonstrated that beta-galactosidase is predominantly attachedviaelectrostatic interactions while attachment of laccase is equally governed by electrostatic and hydrophobic interactions. Furthermore, the A-LMS_5-beta-galactosidase exhibited specificity towards recognized prebiotics (galacto-oligosaccharides (GOS)) synthesis with 1.5-times higher GOS production than glucose production, while for environmental pollutant lindane degradation, the immobilized laccase preparation exhibited high activity with a minimum remaining lindane concentration of 22.4% after 6 days. Thus, this novel enzyme immobilization support A-LMS_5 has potential for use in green biotechnologies.",
publisher = "Royal Society of Chemistry",
journal = "RSC Advances",
title = "Amino-modified kraft lignin microspheres as a support for enzyme immobilization",
pages = "21508-21495",
number = "36",
volume = "10",
doi = "10.1039/d0ra03439h"
}
Bebić, J., Banjanac, K., Rusmirović, J., Ćorović, M., Milivojević, A., Simović, M., Marinković, A.,& Bezbradica, D.. (2020). Amino-modified kraft lignin microspheres as a support for enzyme immobilization. in RSC Advances
Royal Society of Chemistry., 10(36), 21495-21508.
https://doi.org/10.1039/d0ra03439h
Bebić J, Banjanac K, Rusmirović J, Ćorović M, Milivojević A, Simović M, Marinković A, Bezbradica D. Amino-modified kraft lignin microspheres as a support for enzyme immobilization. in RSC Advances. 2020;10(36):21495-21508.
doi:10.1039/d0ra03439h .
Bebić, Jelena, Banjanac, Katarina, Rusmirović, Jelena, Ćorović, Marija, Milivojević, Ana, Simović, Milica, Marinković, Aleksandar, Bezbradica, Dejan, "Amino-modified kraft lignin microspheres as a support for enzyme immobilization" in RSC Advances, 10, no. 36 (2020):21495-21508,
https://doi.org/10.1039/d0ra03439h . .
13
4
14