TY  - JOUR
AU  - Jonović, Marko
AU  - Jugović, Branimir
AU  - Žuža, Milena
AU  - Ðorđević, Verica
AU  - Milašinović, Nikola
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2022
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5165
AB  - The aim of this study was to investigate covalent immobilization of horseradish peroxidase (HRP) on magnetic nanoparticles (Mag) encapsulated in calcium alginate beads (MABs) for color degradation, combining easy and fast removal of biocatalyst from the reaction mixture due to its magnetic properties and strong binding due to surface alginate functional groups. MABs obtained by extrusion techniques were analyzed by optical microscopy, FEG-SEM and characterized regarding mechanical properties, magnetization and HRP binding. HRP with initial concentration of 10 mg/gcarrier was successfully covalently bonded on MABs (diameter ~1 mm, magnetite/alginate ratio 1:4), with protein loading of 8.9 mg/gcarrier, immobilization yield 96.9% and activity 32.8 U/g. Immobilized HRP on MABs (HRP-MABs) was then used to catalyze degradation of two anthraquinonic dyes, Acid Blue 225 (AB225) and Acid Violet 109 (AV109), as models for wastewater pollutants. HRP-MABs decolorized 77.3% and 76.1% of AV109 and AB225, respectively after 15 min under optimal conditions (0.097 mM H2O2, 200 mg of HRP-MABs (8.9 mg/gcarrier), 0.08 and 0.1 g/mg beads/dye ratio for AV109 and AB225, respectively). Biocatalyst was used for 7 repeated cycles retaining 75% and 51% of initial activity for AB225 and AV109, respectively, showing potential for use in large scale applications for colored wastewater treatment.
PB  - MDPI
T2  - Polymers
T1  - Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation
IS  - 13
SP  - 2614
VL  - 14
DO  - 10.3390/polym14132614
ER  - 

@article{
author = "Jonović, Marko and Jugović, Branimir and Žuža, Milena and Ðorđević, Verica and Milašinović, Nikola and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2022",
abstract = "The aim of this study was to investigate covalent immobilization of horseradish peroxidase (HRP) on magnetic nanoparticles (Mag) encapsulated in calcium alginate beads (MABs) for color degradation, combining easy and fast removal of biocatalyst from the reaction mixture due to its magnetic properties and strong binding due to surface alginate functional groups. MABs obtained by extrusion techniques were analyzed by optical microscopy, FEG-SEM and characterized regarding mechanical properties, magnetization and HRP binding. HRP with initial concentration of 10 mg/gcarrier was successfully covalently bonded on MABs (diameter ~1 mm, magnetite/alginate ratio 1:4), with protein loading of 8.9 mg/gcarrier, immobilization yield 96.9% and activity 32.8 U/g. Immobilized HRP on MABs (HRP-MABs) was then used to catalyze degradation of two anthraquinonic dyes, Acid Blue 225 (AB225) and Acid Violet 109 (AV109), as models for wastewater pollutants. HRP-MABs decolorized 77.3% and 76.1% of AV109 and AB225, respectively after 15 min under optimal conditions (0.097 mM H2O2, 200 mg of HRP-MABs (8.9 mg/gcarrier), 0.08 and 0.1 g/mg beads/dye ratio for AV109 and AB225, respectively). Biocatalyst was used for 7 repeated cycles retaining 75% and 51% of initial activity for AB225 and AV109, respectively, showing potential for use in large scale applications for colored wastewater treatment.",
publisher = "MDPI",
journal = "Polymers",
title = "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation",
number = "13",
pages = "2614",
volume = "14",
doi = "10.3390/polym14132614"
}

Jonović, M., Jugović, B., Žuža, M., Ðorđević, V., Milašinović, N., Bugarski, B.,& Knežević-Jugović, Z.. (2022). Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation. in Polymers
MDPI., 14(13), 2614.
https://doi.org/10.3390/polym14132614

Jonović M, Jugović B, Žuža M, Ðorđević V, Milašinović N, Bugarski B, Knežević-Jugović Z. Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation. in Polymers. 2022;14(13):2614.
doi:10.3390/polym14132614 .

Jonović, Marko, Jugović, Branimir, Žuža, Milena, Ðorđević, Verica, Milašinović, Nikola, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of Horseradish Peroxidase on Magnetite-Alginate Beads to Enable Effective Strong Binding and Enzyme Recycling during Anthraquinone Dyes’ Degradation" in Polymers, 14, no. 13 (2022):2614,
https://doi.org/10.3390/polym14132614 . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Milašinović, Nikola
AU  - Jonović, Marko M.
AU  - Jovanović, Jelena
AU  - Kalagasidis Krušić, Melina
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2017
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3544
AB  - In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Design and characterization of alcalase-chitosan conjugates as potential biocatalysts
EP  - 1723
IS  - 11
SP  - 1713
VL  - 40
DO  - 10.1007/s00449-017-1826-7
ER  - 

@article{
author = "Žuža, Milena and Milašinović, Nikola and Jonović, Marko M. and Jovanović, Jelena and Kalagasidis Krušić, Melina and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2017",
abstract = "In this study, alcalase (protease from Bacillus licheniformis) immobilization by adsorption, enzyme crosslinking and covalent enzyme binding to activated chitosan microbeads were examined. The biocatalysts highest activity was obtained by covalent immobilization of alcalase onto a solid support. The alcalase covalent immobilization onto different types of chitosan beads obtained by inverse emulsion technique and electrostatic extrusion was studied. Parameters examined under different conditions were beads diameter, enzyme loading, enzyme capacity yield, and biocatalyst activity. The highest activity and enzyme loading of 23.6 IU/mg protein and 340.2 mg/g, respectively, were achieved by the enzyme immobilized onto chitosan microbeads obtained by the electrostatic extrusion technique. FT-IR analysis was used to confirm formation of alcalase-chitosan conjugates. The activity of optimally produced alcalase-chitosan microbeads was then verified in the industrially feasible reaction systems of egg white and soy protein hydrolysis. The high degree of hydrolysis of 29.85 +/- 0.967% after 180 min and five successive reuses obtained under real conditions (50 A degrees C, pH 8) verified the covalently bound alcalase to chitosan beads a promising candidate for use in industrial egg white protein hydrolysis process.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Design and characterization of alcalase-chitosan conjugates as potential biocatalysts",
pages = "1723-1713",
number = "11",
volume = "40",
doi = "10.1007/s00449-017-1826-7"
}

Žuža, M., Milašinović, N., Jonović, M. M., Jovanović, J., Kalagasidis Krušić, M., Bugarski, B.,& Knežević-Jugović, Z.. (2017). Design and characterization of alcalase-chitosan conjugates as potential biocatalysts. in Bioprocess and Biosystems Engineering
Springer, New York., 40(11), 1713-1723.
https://doi.org/10.1007/s00449-017-1826-7

Žuža M, Milašinović N, Jonović MM, Jovanović J, Kalagasidis Krušić M, Bugarski B, Knežević-Jugović Z. Design and characterization of alcalase-chitosan conjugates as potential biocatalysts. in Bioprocess and Biosystems Engineering. 2017;40(11):1713-1723.
doi:10.1007/s00449-017-1826-7 .

Žuža, Milena, Milašinović, Nikola, Jonović, Marko M., Jovanović, Jelena, Kalagasidis Krušić, Melina, Bugarski, Branko, Knežević-Jugović, Zorica, "Design and characterization of alcalase-chitosan conjugates as potential biocatalysts" in Bioprocess and Biosystems Engineering, 40, no. 11 (2017):1713-1723,
https://doi.org/10.1007/s00449-017-1826-7 . .

TY  - JOUR
AU  - Elmalimadi, Mohamed B.
AU  - Stefanović, Andrea
AU  - Šekuljica, Nataša
AU  - Žuža, Milena
AU  - Luković, Nevena
AU  - Jovanović, Jelena
AU  - Knežević-Jugović, Zorica
PY  - 2017
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3625
AB  - In order to confirm the gluten potential for inclusion into functional foods, the synergistic effect of the heat treatment and controlled enzymatic hydrolysis on the functional and the antioxidant properties of alcalase-assisted wheat gluten hydrolysates (AWGHs) will be discussed. For this purpose, wheat gluten was heat-treated during 30min at 75 degrees C and intensively hydrolyzed with alcalase at degree of hydrolysis (DH) 16.1%, 22.9%, and 30.2%. All the hydrolysates had excellent solubility over a pH range of 2-12. Emulsifying activity and stability were also improved, while proteolysis was deleterious to foam capacity and stability, water-holding capacity, fat-binding capacity and did not show improvement at higher DH (22.9% and 30.2%). As well, controlled hydrolysis of heat-treated gluten resulted in a remarkable improvement in antioxidant activities. The results show that the heat-treated AWGHs were superior to the untreated hydrolysate in the functional and antioxidant properties tested. Practical applicationsThis report examines existing evidence regarding the wheat gluten proteins (WGP), which is a byproduct from wheat starch processing. It is known that enzymatic hydrolysis is frequently used to improve functional properties of protein hydrolysates and largely dependent on the degree of hydrolysis (DH), which needs to be controlled to elude redundant proteolysis that can deteriorate functionality and cause unfavorable effects. The DH is a substantial factor which affect the hydrolysates' performances and an appropriate selection of protease for WGP hydrolysis will result in maximum biological activity and improved functionalities. Heat treatment is often used to facilitate the proteolysis of proteins. Thus, functional and antioxidant properties of WGP hydrolysates, as a function of heat treatment and the DH were adequately examined in this study and results showed that by combining heat prehydrolysis treatment under controlled conditions, hydrolysates with improved properties can be produced enhancing utilization of WGP in food products.
PB  - Wiley, Hoboken
T2  - Journal of Food Processing and Preservation
T1  - The synergistic effect of heat treatment on alcalase-assisted hydrolysis of wheat gluten proteins: Functional and antioxidant properties
IS  - 5
VL  - 41
DO  - 10.1111/jfpp.13207
ER  - 

@article{
author = "Elmalimadi, Mohamed B. and Stefanović, Andrea and Šekuljica, Nataša and Žuža, Milena and Luković, Nevena and Jovanović, Jelena and Knežević-Jugović, Zorica",
year = "2017",
abstract = "In order to confirm the gluten potential for inclusion into functional foods, the synergistic effect of the heat treatment and controlled enzymatic hydrolysis on the functional and the antioxidant properties of alcalase-assisted wheat gluten hydrolysates (AWGHs) will be discussed. For this purpose, wheat gluten was heat-treated during 30min at 75 degrees C and intensively hydrolyzed with alcalase at degree of hydrolysis (DH) 16.1%, 22.9%, and 30.2%. All the hydrolysates had excellent solubility over a pH range of 2-12. Emulsifying activity and stability were also improved, while proteolysis was deleterious to foam capacity and stability, water-holding capacity, fat-binding capacity and did not show improvement at higher DH (22.9% and 30.2%). As well, controlled hydrolysis of heat-treated gluten resulted in a remarkable improvement in antioxidant activities. The results show that the heat-treated AWGHs were superior to the untreated hydrolysate in the functional and antioxidant properties tested. Practical applicationsThis report examines existing evidence regarding the wheat gluten proteins (WGP), which is a byproduct from wheat starch processing. It is known that enzymatic hydrolysis is frequently used to improve functional properties of protein hydrolysates and largely dependent on the degree of hydrolysis (DH), which needs to be controlled to elude redundant proteolysis that can deteriorate functionality and cause unfavorable effects. The DH is a substantial factor which affect the hydrolysates' performances and an appropriate selection of protease for WGP hydrolysis will result in maximum biological activity and improved functionalities. Heat treatment is often used to facilitate the proteolysis of proteins. Thus, functional and antioxidant properties of WGP hydrolysates, as a function of heat treatment and the DH were adequately examined in this study and results showed that by combining heat prehydrolysis treatment under controlled conditions, hydrolysates with improved properties can be produced enhancing utilization of WGP in food products.",
publisher = "Wiley, Hoboken",
journal = "Journal of Food Processing and Preservation",
title = "The synergistic effect of heat treatment on alcalase-assisted hydrolysis of wheat gluten proteins: Functional and antioxidant properties",
number = "5",
volume = "41",
doi = "10.1111/jfpp.13207"
}

Elmalimadi, M. B., Stefanović, A., Šekuljica, N., Žuža, M., Luković, N., Jovanović, J.,& Knežević-Jugović, Z.. (2017). The synergistic effect of heat treatment on alcalase-assisted hydrolysis of wheat gluten proteins: Functional and antioxidant properties. in Journal of Food Processing and Preservation
Wiley, Hoboken., 41(5).
https://doi.org/10.1111/jfpp.13207

Elmalimadi MB, Stefanović A, Šekuljica N, Žuža M, Luković N, Jovanović J, Knežević-Jugović Z. The synergistic effect of heat treatment on alcalase-assisted hydrolysis of wheat gluten proteins: Functional and antioxidant properties. in Journal of Food Processing and Preservation. 2017;41(5).
doi:10.1111/jfpp.13207 .

Elmalimadi, Mohamed B., Stefanović, Andrea, Šekuljica, Nataša, Žuža, Milena, Luković, Nevena, Jovanović, Jelena, Knežević-Jugović, Zorica, "The synergistic effect of heat treatment on alcalase-assisted hydrolysis of wheat gluten proteins: Functional and antioxidant properties" in Journal of Food Processing and Preservation, 41, no. 5 (2017),
https://doi.org/10.1111/jfpp.13207 . .

TY  - JOUR
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Žuža, Milena
AU  - Jakovetić, Sonja
AU  - Šekuljica, Nataša
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3317
AB  - The production of bioactive peptides from egg white proteins (EWPs) and their separation are emerging areas with many new applications. The objective of this study was to compare antioxidant activity of three distinct EWP hydrolysates and their peptide fractions prepared by membrane ultrafiltration using membranes with 30, 10 and 1 kDa molecular weight cut-off. The hydrolysates were obtained by thermal and ultrasound pretreated EWPs hydrolyzed with a bacterial protease, Alcalase. It appeared that the pretreatment significantly affected peptide profiles and antioxidant activity of the hydrolysates measured by ABTS, DPPH and FRAP methods. The hydrolysate prepared using alcalase and ultrasound pretreatment at 40 kHz - 15 min has shown to be the most effective in scavenging both DPPH and ABTS radicals (28.10 +/- 1.38 and 79.44 +/- 2.31%, respectively). It has been noticed that this hydrolysate had a nutritionally more adequate peptide profile than the other hydrolysates with a much lower amount of peptides  lt 1 kDa (11.19 +/- 0.53%) and the greatest content of the peptide fraction in the molecular weight (MW) range of 1-10 kDa (28.80 +/- 0.07%). This peptide fraction has shown the highest DPPH and ABTS antioxidant activity compared to all other fractions having a potential to be used as a functional food ingredient.
PB  - Savez hemijskih inženjera, Beograd
T2  - Hemijska industrija
T1  - Improvement of antioxidant properties of egg white protein enzymatic hydrolysates by membrane ultrafiltration
EP  - 428
IS  - 4
SP  - 419
VL  - 70
DO  - 10.2298/HEMIND150506047J
ER  - 

@article{
author = "Jovanović, Jelena and Stefanović, Andrea and Žuža, Milena and Jakovetić, Sonja and Šekuljica, Nataša and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2016",
abstract = "The production of bioactive peptides from egg white proteins (EWPs) and their separation are emerging areas with many new applications. The objective of this study was to compare antioxidant activity of three distinct EWP hydrolysates and their peptide fractions prepared by membrane ultrafiltration using membranes with 30, 10 and 1 kDa molecular weight cut-off. The hydrolysates were obtained by thermal and ultrasound pretreated EWPs hydrolyzed with a bacterial protease, Alcalase. It appeared that the pretreatment significantly affected peptide profiles and antioxidant activity of the hydrolysates measured by ABTS, DPPH and FRAP methods. The hydrolysate prepared using alcalase and ultrasound pretreatment at 40 kHz - 15 min has shown to be the most effective in scavenging both DPPH and ABTS radicals (28.10 +/- 1.38 and 79.44 +/- 2.31%, respectively). It has been noticed that this hydrolysate had a nutritionally more adequate peptide profile than the other hydrolysates with a much lower amount of peptides  lt 1 kDa (11.19 +/- 0.53%) and the greatest content of the peptide fraction in the molecular weight (MW) range of 1-10 kDa (28.80 +/- 0.07%). This peptide fraction has shown the highest DPPH and ABTS antioxidant activity compared to all other fractions having a potential to be used as a functional food ingredient.",
publisher = "Savez hemijskih inženjera, Beograd",
journal = "Hemijska industrija",
title = "Improvement of antioxidant properties of egg white protein enzymatic hydrolysates by membrane ultrafiltration",
pages = "428-419",
number = "4",
volume = "70",
doi = "10.2298/HEMIND150506047J"
}

Jovanović, J., Stefanović, A., Žuža, M., Jakovetić, S., Šekuljica, N., Bugarski, B.,& Knežević-Jugović, Z.. (2016). Improvement of antioxidant properties of egg white protein enzymatic hydrolysates by membrane ultrafiltration. in Hemijska industrija
Savez hemijskih inženjera, Beograd., 70(4), 419-428.
https://doi.org/10.2298/HEMIND150506047J

Jovanović J, Stefanović A, Žuža M, Jakovetić S, Šekuljica N, Bugarski B, Knežević-Jugović Z. Improvement of antioxidant properties of egg white protein enzymatic hydrolysates by membrane ultrafiltration. in Hemijska industrija. 2016;70(4):419-428.
doi:10.2298/HEMIND150506047J .

Jovanović, Jelena, Stefanović, Andrea, Žuža, Milena, Jakovetić, Sonja, Šekuljica, Nataša, Bugarski, Branko, Knežević-Jugović, Zorica, "Improvement of antioxidant properties of egg white protein enzymatic hydrolysates by membrane ultrafiltration" in Hemijska industrija, 70, no. 4 (2016):419-428,
https://doi.org/10.2298/HEMIND150506047J . .

TY  - JOUR
AU  - Knežević-Jugović, Zorica
AU  - Žuža, Milena
AU  - Jakovetić, Sonja
AU  - Stefanović, Andrea
AU  - Džunuzović, Enis
AU  - Jeremić, Katarina B.
AU  - Jovanović, Slobodan M.
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3457
AB  - The use of penicillin G acylase (PGA) covalently linked to insoluble carrier is expected to produce major advances in pharmaceutical processing industry and the enzyme stability enhancement is still a significant challenge. The objective of this study was to improve catalytic performance of the covalently immobilized PGA on a potential industrial carrier, macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) [poly(GMA-co-EGDMA)], by optimizing the copolymerization process and the enzyme attachment procedure. This synthetic copolymer could be a very promising alternative for the development of low-cost, easy-to-prepare, and stable biocatalyst compared to expensive commercially available epoxy carriers such as Eupergit or Sepabeads. The PGA immobilized on poly(GMA-co-EGDMA) in the shape of microbeads obtained by suspension copolymerization appeared to have higher activity yield compared to copolymerization in a cast. Optimal conditions for the immobilization of PGA on poly(GMA-co-EGDMA) microbeads were 1mg/mL of PGA in 0.75mol/L phosphate buffer pH 6.0 at 25 degrees C for 24h, leading to the active biocatalyst with the specific activity of 252.7U/g dry beads. Chemical amination of the immobilized PGA could contribute to the enhanced stability of the biocatalyst by inducing secondary interactions between the enzyme and the carrier, ensuring multipoint attachment. The best balance between the activity yield (51.5%), enzyme loading (25.6mg/g), and stability (stabilization factor 22.2) was achieved for the partially modified PGA.
PB  - Wiley, Hoboken
T2  - Biotechnology Progress
T1  - An approach for the improved immobilization of penicillin G acylase onto macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) as a potential industrial biocatalyst
EP  - 53
IS  - 1
SP  - 43
VL  - 32
DO  - 10.1002/btpr.2181
ER  - 

@article{
author = "Knežević-Jugović, Zorica and Žuža, Milena and Jakovetić, Sonja and Stefanović, Andrea and Džunuzović, Enis and Jeremić, Katarina B. and Jovanović, Slobodan M.",
year = "2016",
abstract = "The use of penicillin G acylase (PGA) covalently linked to insoluble carrier is expected to produce major advances in pharmaceutical processing industry and the enzyme stability enhancement is still a significant challenge. The objective of this study was to improve catalytic performance of the covalently immobilized PGA on a potential industrial carrier, macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) [poly(GMA-co-EGDMA)], by optimizing the copolymerization process and the enzyme attachment procedure. This synthetic copolymer could be a very promising alternative for the development of low-cost, easy-to-prepare, and stable biocatalyst compared to expensive commercially available epoxy carriers such as Eupergit or Sepabeads. The PGA immobilized on poly(GMA-co-EGDMA) in the shape of microbeads obtained by suspension copolymerization appeared to have higher activity yield compared to copolymerization in a cast. Optimal conditions for the immobilization of PGA on poly(GMA-co-EGDMA) microbeads were 1mg/mL of PGA in 0.75mol/L phosphate buffer pH 6.0 at 25 degrees C for 24h, leading to the active biocatalyst with the specific activity of 252.7U/g dry beads. Chemical amination of the immobilized PGA could contribute to the enhanced stability of the biocatalyst by inducing secondary interactions between the enzyme and the carrier, ensuring multipoint attachment. The best balance between the activity yield (51.5%), enzyme loading (25.6mg/g), and stability (stabilization factor 22.2) was achieved for the partially modified PGA.",
publisher = "Wiley, Hoboken",
journal = "Biotechnology Progress",
title = "An approach for the improved immobilization of penicillin G acylase onto macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) as a potential industrial biocatalyst",
pages = "53-43",
number = "1",
volume = "32",
doi = "10.1002/btpr.2181"
}

Knežević-Jugović, Z., Žuža, M., Jakovetić, S., Stefanović, A., Džunuzović, E., Jeremić, K. B.,& Jovanović, S. M.. (2016). An approach for the improved immobilization of penicillin G acylase onto macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) as a potential industrial biocatalyst. in Biotechnology Progress
Wiley, Hoboken., 32(1), 43-53.
https://doi.org/10.1002/btpr.2181

Knežević-Jugović Z, Žuža M, Jakovetić S, Stefanović A, Džunuzović E, Jeremić KB, Jovanović SM. An approach for the improved immobilization of penicillin G acylase onto macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) as a potential industrial biocatalyst. in Biotechnology Progress. 2016;32(1):43-53.
doi:10.1002/btpr.2181 .

Knežević-Jugović, Zorica, Žuža, Milena, Jakovetić, Sonja, Stefanović, Andrea, Džunuzović, Enis, Jeremić, Katarina B., Jovanović, Slobodan M., "An approach for the improved immobilization of penicillin G acylase onto macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) as a potential industrial biocatalyst" in Biotechnology Progress, 32, no. 1 (2016):43-53,
https://doi.org/10.1002/btpr.2181 . .

TY  - JOUR
AU  - Šekuljica, Nataša
AU  - Prlainović, Nevena
AU  - Stefanović, Andrea
AU  - Žuža, Milena
AU  - Čičkarić, Dragana Z.
AU  - Mijin, Dušan
AU  - Knežević-Jugović, Zorica
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2879
AB  - Two anthraquinonic dyes, C.I. Acid Blue 225 and C.I. Acid Violet 109, were used as models to explore the feasibility of using the horseradish peroxidase enzyme (HRP) in the practical decolorization of anthraquinonic dyes in wastewater. The influence of process parameters such as enzyme concentration, hydrogen peroxide concentration, temperature, dye concentration, and pH was examined. The pH and temperature activity profiles were similar for decolorization of both dyes. Under the optimal conditions, 94.7% of C.I. Acid Violet 109 from aqueous solution was decolorized (treatment time 15 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.4 mM, dye concentration 30 mg/L, pH 4, and temperature 24°C) and 89.36% of C.I. Acid Blue 225 (32 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.04 mM, dye concentration 30 mg/L, pH 5, and temperature 24°C). The mechanism of both reactions has been proven to follow the two substrate ping-pong mechanism with substrate inhibition, revealing the formation of a nonproductive or dead-end complex between dye and HRP or between Hand the oxidized form of the enzyme. Both chemical oxygen demand and total organic carbon values showed that there was a reduction in toxicity after the enzymatic treatment. This study verifies the viability of use of horseradish peroxidase for the wastewaters treatment of similar anthraquinonic dyes.
PB  - Hindawi Limited
T2  - Scientific World Journal
T1  - Decolorization of anthraquinonic dyes from textile effluent using horseradish peroxidase: Optimization and kinetic study
VL  - 2015
DO  - 10.1155/2015/371625
ER  - 

@article{
author = "Šekuljica, Nataša and Prlainović, Nevena and Stefanović, Andrea and Žuža, Milena and Čičkarić, Dragana Z. and Mijin, Dušan and Knežević-Jugović, Zorica",
year = "2015",
abstract = "Two anthraquinonic dyes, C.I. Acid Blue 225 and C.I. Acid Violet 109, were used as models to explore the feasibility of using the horseradish peroxidase enzyme (HRP) in the practical decolorization of anthraquinonic dyes in wastewater. The influence of process parameters such as enzyme concentration, hydrogen peroxide concentration, temperature, dye concentration, and pH was examined. The pH and temperature activity profiles were similar for decolorization of both dyes. Under the optimal conditions, 94.7% of C.I. Acid Violet 109 from aqueous solution was decolorized (treatment time 15 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.4 mM, dye concentration 30 mg/L, pH 4, and temperature 24°C) and 89.36% of C.I. Acid Blue 225 (32 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.04 mM, dye concentration 30 mg/L, pH 5, and temperature 24°C). The mechanism of both reactions has been proven to follow the two substrate ping-pong mechanism with substrate inhibition, revealing the formation of a nonproductive or dead-end complex between dye and HRP or between Hand the oxidized form of the enzyme. Both chemical oxygen demand and total organic carbon values showed that there was a reduction in toxicity after the enzymatic treatment. This study verifies the viability of use of horseradish peroxidase for the wastewaters treatment of similar anthraquinonic dyes.",
publisher = "Hindawi Limited",
journal = "Scientific World Journal",
title = "Decolorization of anthraquinonic dyes from textile effluent using horseradish peroxidase: Optimization and kinetic study",
volume = "2015",
doi = "10.1155/2015/371625"
}

Šekuljica, N., Prlainović, N., Stefanović, A., Žuža, M., Čičkarić, D. Z., Mijin, D.,& Knežević-Jugović, Z.. (2015). Decolorization of anthraquinonic dyes from textile effluent using horseradish peroxidase: Optimization and kinetic study. in Scientific World Journal
Hindawi Limited., 2015.
https://doi.org/10.1155/2015/371625

Šekuljica N, Prlainović N, Stefanović A, Žuža M, Čičkarić DZ, Mijin D, Knežević-Jugović Z. Decolorization of anthraquinonic dyes from textile effluent using horseradish peroxidase: Optimization and kinetic study. in Scientific World Journal. 2015;2015.
doi:10.1155/2015/371625 .

Šekuljica, Nataša, Prlainović, Nevena, Stefanović, Andrea, Žuža, Milena, Čičkarić, Dragana Z., Mijin, Dušan, Knežević-Jugović, Zorica, "Decolorization of anthraquinonic dyes from textile effluent using horseradish peroxidase: Optimization and kinetic study" in Scientific World Journal, 2015 (2015),
https://doi.org/10.1155/2015/371625 . .

TY  - CONF
AU  - Knežević-Jugović, Zorica
AU  - Gluvić, Ana
AU  - Žuža, Milena
AU  - Stefanović, Andrea
AU  - Gvozdenović, Milica
AU  - Jugović, Branimir
AU  - Antov, Mirjana
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2279
AB  - Enzymatic hydrolysis of egg white proteins has shown great potential to improve their functional properties such as increased solubility, stability, and digestibility, and to reduce protein allergenicity while still retaining their nutrition value. However, the enzymatic hydrolysis process is still poorly defined and difficult to control at the industrial scale resulting in peptide mixtures poorly characterized and with unpleasant bitter taste that make them unsuitable for human consumption. Thus, the hydrolysis reaction must be carefully controlled in order to produce new value-added egg white hydrolysates with improved properties and specialized functionality. In this paper egg white protein solution was hydrolysed with several enzymes using both, one-step and two-step hydrolysis. The hydrolysate was then tested on antioxidant activity, flavour, solubility, digestibility emulsifying activity, foaming capacity and stability. All protein hydrolysates showed higher solubility and digestibility than intact proteins, especially at pHs near isoelectric point of egg white proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the native protein solution.
PB  - Tatranské Matliare : Slovak Society of Chemical Engineering
C3  - Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering
T1  - Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates
EP  - 1439
SP  - 1433
UR  - https://hdl.handle.net/21.15107/rcub_technorep_2279
ER  - 

@conference{
author = "Knežević-Jugović, Zorica and Gluvić, Ana and Žuža, Milena and Stefanović, Andrea and Gvozdenović, Milica and Jugović, Branimir and Antov, Mirjana",
year = "2013",
abstract = "Enzymatic hydrolysis of egg white proteins has shown great potential to improve their functional properties such as increased solubility, stability, and digestibility, and to reduce protein allergenicity while still retaining their nutrition value. However, the enzymatic hydrolysis process is still poorly defined and difficult to control at the industrial scale resulting in peptide mixtures poorly characterized and with unpleasant bitter taste that make them unsuitable for human consumption. Thus, the hydrolysis reaction must be carefully controlled in order to produce new value-added egg white hydrolysates with improved properties and specialized functionality. In this paper egg white protein solution was hydrolysed with several enzymes using both, one-step and two-step hydrolysis. The hydrolysate was then tested on antioxidant activity, flavour, solubility, digestibility emulsifying activity, foaming capacity and stability. All protein hydrolysates showed higher solubility and digestibility than intact proteins, especially at pHs near isoelectric point of egg white proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the native protein solution.",
publisher = "Tatranské Matliare : Slovak Society of Chemical Engineering",
journal = "Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering",
title = "Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates",
pages = "1439-1433",
url = "https://hdl.handle.net/21.15107/rcub_technorep_2279"
}

Knežević-Jugović, Z., Gluvić, A., Žuža, M., Stefanović, A., Gvozdenović, M., Jugović, B.,& Antov, M.. (2013). Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates. in Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering
Tatranské Matliare : Slovak Society of Chemical Engineering., 1433-1439.
https://hdl.handle.net/21.15107/rcub_technorep_2279

Knežević-Jugović Z, Gluvić A, Žuža M, Stefanović A, Gvozdenović M, Jugović B, Antov M. Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates. in Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering. 2013;:1433-1439.
https://hdl.handle.net/21.15107/rcub_technorep_2279 .

Knežević-Jugović, Zorica, Gluvić, Ana, Žuža, Milena, Stefanović, Andrea, Gvozdenović, Milica, Jugović, Branimir, Antov, Mirjana, "Effects of hydrolysis degree and type of protease on antioxidant activity and functionality of egg white protein hydrolysates" in Proceedings of the 40th International Conference of Slovak Society of Chemical Engineering (2013):1433-1439,
https://hdl.handle.net/21.15107/rcub_technorep_2279 .

TY  - JOUR
AU  - Knežević-Jugović, Zorica
AU  - Stefanović, Andrea
AU  - Žuža, Milena
AU  - Milovanović, Stoja
AU  - Jakovetić, Sonja
AU  - Manojlović, Verica
AU  - Bugarski, Branko
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2042
AB  - The objectives of this study were to examine the effect of sonication and high-pressure carbon dioxide processing on proteolytic hydrolysis of egg white proteins and antioxidant activity of the obtained hydrolysates. It appeared that the ultrasound pretreatment resulted in an increase in the degree of hydrolysis of the enzymatic reaction while the high-pressure carbon dioxide processing showed an inhibition effect on the enzymatic hydrolysis of egg white proteins to some extent. The antioxidant activity of the obtained hydrolysates was improved by ultrasound pretreatment of egg white proteins at the pH 8.3. Thus, the combination of ultrasound pretreatment at the pH 8.3 and subsequent enzymatic hydrolysis with alcalase at 50°C and pH 8.0 could offer a new approach to the improvement of the functional properties of egg white proteins and their biological activity.
AB  - Proteini belanceta spadaju u veoma kvalitetne proteine zbog svog jedinstvenog aminokiselinskog sastava. Međutim, veća komercijalna primena hidrolizata proteina belanceta je ograničena usled neadekvatnog procesnog tretmana pri obradi i sterilizaciji belanceta termičkim tretmanom kao i hemijskoj hidrolizi proteina, koji dovode do značajne promene boje, ukusa, funkcionalnosti i nutritivnih svojstava proizvoda. Cilj ovog rada je bio da se ispita mogućnost primene netermičkih tretmanima, kao što su sonikacija i tretman visokim pritiskom, da bi se unapredila enzimska hidroliza proteina belanceta i omogućilo dobijanje hidrolizata sa antioksidativnom aktivnošću. Pokazano je da tretiranje proteina belanceta ultrazvukom pod određenim uslovima dovodi do njihove kasnije poboljšane hidrolize alkalazom, dok procesiranje belanceta visokim pritiskom ima negativan uticaj na aktivnost alkalaze. Antioksidativna aktivnost dobijenih hidrolizata je povećana nakon pretretmana ultrazvukom na pH 8,3. Tako, kombinacija pretretmana proteina belanceta ultrazvukom na pH 8,3 i njihova sukcesivna hidroliza alkalazom na 50°C i pri pH 8,0 se pokazala kao efikasna alternativna metoda za dobijanje hidrolizata proteina belanceta sa unapređenim funkcionalnim svojstvima i biološkom aktivnošću.
PB  - Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins
T1  - Uticaj sonikacije i pretretmana visokim pritiskom na enzimsku hidrolizu proteina belanceta
EP  - 41
IS  - 43
SP  - 33
DO  - 10.2298/APT1243033K
ER  - 

@article{
author = "Knežević-Jugović, Zorica and Stefanović, Andrea and Žuža, Milena and Milovanović, Stoja and Jakovetić, Sonja and Manojlović, Verica and Bugarski, Branko",
year = "2012",
abstract = "The objectives of this study were to examine the effect of sonication and high-pressure carbon dioxide processing on proteolytic hydrolysis of egg white proteins and antioxidant activity of the obtained hydrolysates. It appeared that the ultrasound pretreatment resulted in an increase in the degree of hydrolysis of the enzymatic reaction while the high-pressure carbon dioxide processing showed an inhibition effect on the enzymatic hydrolysis of egg white proteins to some extent. The antioxidant activity of the obtained hydrolysates was improved by ultrasound pretreatment of egg white proteins at the pH 8.3. Thus, the combination of ultrasound pretreatment at the pH 8.3 and subsequent enzymatic hydrolysis with alcalase at 50°C and pH 8.0 could offer a new approach to the improvement of the functional properties of egg white proteins and their biological activity., Proteini belanceta spadaju u veoma kvalitetne proteine zbog svog jedinstvenog aminokiselinskog sastava. Međutim, veća komercijalna primena hidrolizata proteina belanceta je ograničena usled neadekvatnog procesnog tretmana pri obradi i sterilizaciji belanceta termičkim tretmanom kao i hemijskoj hidrolizi proteina, koji dovode do značajne promene boje, ukusa, funkcionalnosti i nutritivnih svojstava proizvoda. Cilj ovog rada je bio da se ispita mogućnost primene netermičkih tretmanima, kao što su sonikacija i tretman visokim pritiskom, da bi se unapredila enzimska hidroliza proteina belanceta i omogućilo dobijanje hidrolizata sa antioksidativnom aktivnošću. Pokazano je da tretiranje proteina belanceta ultrazvukom pod određenim uslovima dovodi do njihove kasnije poboljšane hidrolize alkalazom, dok procesiranje belanceta visokim pritiskom ima negativan uticaj na aktivnost alkalaze. Antioksidativna aktivnost dobijenih hidrolizata je povećana nakon pretretmana ultrazvukom na pH 8,3. Tako, kombinacija pretretmana proteina belanceta ultrazvukom na pH 8,3 i njihova sukcesivna hidroliza alkalazom na 50°C i pri pH 8,0 se pokazala kao efikasna alternativna metoda za dobijanje hidrolizata proteina belanceta sa unapređenim funkcionalnim svojstvima i biološkom aktivnošću.",
publisher = "Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins, Uticaj sonikacije i pretretmana visokim pritiskom na enzimsku hidrolizu proteina belanceta",
pages = "41-33",
number = "43",
doi = "10.2298/APT1243033K"
}

Knežević-Jugović, Z., Stefanović, A., Žuža, M., Milovanović, S., Jakovetić, S., Manojlović, V.,& Bugarski, B.. (2012). Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins. in Acta periodica technologica
Faculty of Technology, Novi Sad.(43), 33-41.
https://doi.org/10.2298/APT1243033K

Knežević-Jugović Z, Stefanović A, Žuža M, Milovanović S, Jakovetić S, Manojlović V, Bugarski B. Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins. in Acta periodica technologica. 2012;(43):33-41.
doi:10.2298/APT1243033K .

Knežević-Jugović, Zorica, Stefanović, Andrea, Žuža, Milena, Milovanović, Stoja, Jakovetić, Sonja, Manojlović, Verica, Bugarski, Branko, "Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins" in Acta periodica technologica, no. 43 (2012):33-41,
https://doi.org/10.2298/APT1243033K . .

TY  - JOUR
AU  - Damnjanović, Jasmina J.
AU  - Žuža, Milena
AU  - Savanović, Jova K.
AU  - Bezbradica, Dejan
AU  - Mijin, Dušan
AU  - Bošković-Vragolović, Nevenka
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2236
AB  - Three commercially available polymers (Sepabeads (R) EC-EP, Sepabeads (R) EC-HA and Purolite (R) A-109) were tested for potential application as supports for covalent immobilization of lipase from Candida rugosa by analyzing some critical properties of immobilized enzymes such as enzyme loading, activity and activity immobilization yield. Among them, lipase covalently immobilized on Sepabeads (R) EC-EP via epoxy groups appeared to show the best performance in a standard hydrolytic reaction. Therefore, it was selected and assayed in the esterification of butyric acid and geraniol to produce geranyl butyrate, first in a batch system followed by continuous geranyl butyrate synthesis in a fluidized bed reactor, as one being potentially applicable for large-scale production. Based on statistical analysis, optimal conditions for the production of geranyl butyrate by selected, immobilized lipase in the batch system are recommended as: temperature at 25-30 degrees C, water concentration at 3.6% (v/v) and acid/alcohol molar ratio at 2.5. A set of optimal conditions for the ester synthesis in a fluidized bed reactor system has also been determined, specifically, flow rate at 10 mL min(-1), temperature at 35 degrees C, water concentration at 2% (v/v), substrate concentration at 0.1 M and acid/alcohol ratio at 2.0. Implementation of the optimized parameters in a batch system and in a fluidized bed reactor enabled production of target ester with high molar conversion, at  gt  99.9% for 48 h in the batch process, and 78.9% for 10 h in fluidized bed reactor. Although when assayed at their optimal conditions, lower molar conversion was achieved in the fluidized bed reactor system compared to the batch system, the volumetric productivity in fluidized bed reactor was more than five fold higher than that obtained in the batch system.
PB  - Elsevier, Amsterdam
T2  - Journal of Molecular Catalysis B-Enzymatic
T1  - Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor
EP  - 59
SP  - 50
VL  - 75
DO  - 10.1016/j.molcatb.2011.11.009
ER  - 

@article{
author = "Damnjanović, Jasmina J. and Žuža, Milena and Savanović, Jova K. and Bezbradica, Dejan and Mijin, Dušan and Bošković-Vragolović, Nevenka and Knežević-Jugović, Zorica",
year = "2012",
abstract = "Three commercially available polymers (Sepabeads (R) EC-EP, Sepabeads (R) EC-HA and Purolite (R) A-109) were tested for potential application as supports for covalent immobilization of lipase from Candida rugosa by analyzing some critical properties of immobilized enzymes such as enzyme loading, activity and activity immobilization yield. Among them, lipase covalently immobilized on Sepabeads (R) EC-EP via epoxy groups appeared to show the best performance in a standard hydrolytic reaction. Therefore, it was selected and assayed in the esterification of butyric acid and geraniol to produce geranyl butyrate, first in a batch system followed by continuous geranyl butyrate synthesis in a fluidized bed reactor, as one being potentially applicable for large-scale production. Based on statistical analysis, optimal conditions for the production of geranyl butyrate by selected, immobilized lipase in the batch system are recommended as: temperature at 25-30 degrees C, water concentration at 3.6% (v/v) and acid/alcohol molar ratio at 2.5. A set of optimal conditions for the ester synthesis in a fluidized bed reactor system has also been determined, specifically, flow rate at 10 mL min(-1), temperature at 35 degrees C, water concentration at 2% (v/v), substrate concentration at 0.1 M and acid/alcohol ratio at 2.0. Implementation of the optimized parameters in a batch system and in a fluidized bed reactor enabled production of target ester with high molar conversion, at  gt  99.9% for 48 h in the batch process, and 78.9% for 10 h in fluidized bed reactor. Although when assayed at their optimal conditions, lower molar conversion was achieved in the fluidized bed reactor system compared to the batch system, the volumetric productivity in fluidized bed reactor was more than five fold higher than that obtained in the batch system.",
publisher = "Elsevier, Amsterdam",
journal = "Journal of Molecular Catalysis B-Enzymatic",
title = "Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor",
pages = "59-50",
volume = "75",
doi = "10.1016/j.molcatb.2011.11.009"
}

Damnjanović, J. J., Žuža, M., Savanović, J. K., Bezbradica, D., Mijin, D., Bošković-Vragolović, N.,& Knežević-Jugović, Z.. (2012). Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor. in Journal of Molecular Catalysis B-Enzymatic
Elsevier, Amsterdam., 75, 50-59.
https://doi.org/10.1016/j.molcatb.2011.11.009

Damnjanović JJ, Žuža M, Savanović JK, Bezbradica D, Mijin D, Bošković-Vragolović N, Knežević-Jugović Z. Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor. in Journal of Molecular Catalysis B-Enzymatic. 2012;75:50-59.
doi:10.1016/j.molcatb.2011.11.009 .

Damnjanović, Jasmina J., Žuža, Milena, Savanović, Jova K., Bezbradica, Dejan, Mijin, Dušan, Bošković-Vragolović, Nevenka, Knežević-Jugović, Zorica, "Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor" in Journal of Molecular Catalysis B-Enzymatic, 75 (2012):50-59,
https://doi.org/10.1016/j.molcatb.2011.11.009 . .

TY  - JOUR
AU  - Moftah, Omar A.S.
AU  - Grbavčić, Sanja
AU  - Žuža, Milena
AU  - Luković, Nevena
AU  - Bezbradica, Dejan
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2227
AB  - Olive oil cake is a by-product from the olive oil processing industry and can be used for the lipase and protease production by Candida utilis in solid state fermentation. Different carbon and nitrogen sources were evaluated, and the results showed that the supplementation of the substrate with maltose and starch as carbon sources and yeast extract as a nitrogen source significantly increased the lipase production. The best results were obtained with maltose, whereas rather low lipase and protease activities were found with glucose and oleic acid. Response surface methodology and a five-level-three-factor central composite rotatable design were used to evaluate the effects of the initial moisture content, inoculum size and fermentation time on both lipase and protease activity levels. A lipase activity value of approximate to 25 Ug(-1) and a protease activity value of 110 Ug(-1) were obtained under the optimized fermentation conditions. An alkaline treatment of the substrate appeared to be efficient, leading to increases of 39% and 133% in the lipase and protease production, respectively. The results showed that the olive cake could be a good source for enzyme production by solid state fermentation.
PB  - Springer, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Adding Value to the Oil Cake as a Waste from Oil Processing Industry: Production of Lipase and Protease by Candida utilis in Solid State Fermentation
EP  - 364
IS  - 2
SP  - 348
VL  - 166
DO  - 10.1007/s12010-011-9429-2
ER  - 

@article{
author = "Moftah, Omar A.S. and Grbavčić, Sanja and Žuža, Milena and Luković, Nevena and Bezbradica, Dejan and Knežević-Jugović, Zorica",
year = "2012",
abstract = "Olive oil cake is a by-product from the olive oil processing industry and can be used for the lipase and protease production by Candida utilis in solid state fermentation. Different carbon and nitrogen sources were evaluated, and the results showed that the supplementation of the substrate with maltose and starch as carbon sources and yeast extract as a nitrogen source significantly increased the lipase production. The best results were obtained with maltose, whereas rather low lipase and protease activities were found with glucose and oleic acid. Response surface methodology and a five-level-three-factor central composite rotatable design were used to evaluate the effects of the initial moisture content, inoculum size and fermentation time on both lipase and protease activity levels. A lipase activity value of approximate to 25 Ug(-1) and a protease activity value of 110 Ug(-1) were obtained under the optimized fermentation conditions. An alkaline treatment of the substrate appeared to be efficient, leading to increases of 39% and 133% in the lipase and protease production, respectively. The results showed that the olive cake could be a good source for enzyme production by solid state fermentation.",
publisher = "Springer, New York",
journal = "Applied Biochemistry and Biotechnology",
title = "Adding Value to the Oil Cake as a Waste from Oil Processing Industry: Production of Lipase and Protease by Candida utilis in Solid State Fermentation",
pages = "364-348",
number = "2",
volume = "166",
doi = "10.1007/s12010-011-9429-2"
}

Moftah, O. A.S., Grbavčić, S., Žuža, M., Luković, N., Bezbradica, D.,& Knežević-Jugović, Z.. (2012). Adding Value to the Oil Cake as a Waste from Oil Processing Industry: Production of Lipase and Protease by Candida utilis in Solid State Fermentation. in Applied Biochemistry and Biotechnology
Springer, New York., 166(2), 348-364.
https://doi.org/10.1007/s12010-011-9429-2

Moftah OA, Grbavčić S, Žuža M, Luković N, Bezbradica D, Knežević-Jugović Z. Adding Value to the Oil Cake as a Waste from Oil Processing Industry: Production of Lipase and Protease by Candida utilis in Solid State Fermentation. in Applied Biochemistry and Biotechnology. 2012;166(2):348-364.
doi:10.1007/s12010-011-9429-2 .

Moftah, Omar A.S., Grbavčić, Sanja, Žuža, Milena, Luković, Nevena, Bezbradica, Dejan, Knežević-Jugović, Zorica, "Adding Value to the Oil Cake as a Waste from Oil Processing Industry: Production of Lipase and Protease by Candida utilis in Solid State Fermentation" in Applied Biochemistry and Biotechnology, 166, no. 2 (2012):348-364,
https://doi.org/10.1007/s12010-011-9429-2 . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Obradović, Bojana
AU  - Knežević-Jugović, Zorica
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1874
AB  - The kinetic parameters for penicillin G hydrolysis in systems with penicillin G acylase from Escherichia coli (free and immobilized on activated chitosan microbeads produced by electrostatic extrusion) were determined. The obtained kinetic results indicated that both systems (free and immobilized) are inhibited by high concentrations of the substrate (penicillin G) as well as by products of the reaction (6-aminopenicillanic acid and phenylacetic acid). The microbeads appeared convenient for penicillin G acylase immobilization reducing negative inhibitory effects. The hydrolysis was also investigated in a packed bed reactor. The derived kinetic model predicted good hydrolysis rates in the reactor while the system with recirculation of the reaction mixture proved to be a potentially favorable solution providing operation at low shear stresses and possibly higher hydrolysis rates than in the packed bed reactor alone.
PB  - Wiley-VCH Verlag Gmbh, Weinheim
T2  - Chemical Engineering & Technology
T1  - Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems
EP  - 1714
IS  - 10
SP  - 1706
VL  - 34
DO  - 10.1002/ceat.201100297
ER  - 

@article{
author = "Žuža, Milena and Obradović, Bojana and Knežević-Jugović, Zorica",
year = "2011",
abstract = "The kinetic parameters for penicillin G hydrolysis in systems with penicillin G acylase from Escherichia coli (free and immobilized on activated chitosan microbeads produced by electrostatic extrusion) were determined. The obtained kinetic results indicated that both systems (free and immobilized) are inhibited by high concentrations of the substrate (penicillin G) as well as by products of the reaction (6-aminopenicillanic acid and phenylacetic acid). The microbeads appeared convenient for penicillin G acylase immobilization reducing negative inhibitory effects. The hydrolysis was also investigated in a packed bed reactor. The derived kinetic model predicted good hydrolysis rates in the reactor while the system with recirculation of the reaction mixture proved to be a potentially favorable solution providing operation at low shear stresses and possibly higher hydrolysis rates than in the packed bed reactor alone.",
publisher = "Wiley-VCH Verlag Gmbh, Weinheim",
journal = "Chemical Engineering & Technology",
title = "Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems",
pages = "1714-1706",
number = "10",
volume = "34",
doi = "10.1002/ceat.201100297"
}

Žuža, M., Obradović, B.,& Knežević-Jugović, Z.. (2011). Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems. in Chemical Engineering & Technology
Wiley-VCH Verlag Gmbh, Weinheim., 34(10), 1706-1714.
https://doi.org/10.1002/ceat.201100297

Žuža M, Obradović B, Knežević-Jugović Z. Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems. in Chemical Engineering & Technology. 2011;34(10):1706-1714.
doi:10.1002/ceat.201100297 .

Žuža, Milena, Obradović, Bojana, Knežević-Jugović, Zorica, "Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems" in Chemical Engineering & Technology, 34, no. 10 (2011):1706-1714,
https://doi.org/10.1002/ceat.201100297 . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Milosavić, Nenad
AU  - Knežević-Jugović, Zorica
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1810
AB  - Penicillin acylase (PAC) is an important industrial enzyme for the production of many β-lactam antibiotics. It is capable of catalyzing the hydrolysis of penicillin G (Pen G) to generate phenylacetic acid (PAA) and 6-aminopenicillanic acid (6-APA). In this paper, in order to prevent enzyme inactivation, an attempt of coupling enzyme modification and immobilization is presented. Chemical modification was promoted to introduce carbohydrate moiety into the PAC molecule, capable of being covalently linked to an amino support. This seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause a loss of activity. PAC molecules were modified by cross-linking with polyaldehyde derivatives of alginate in order to add them new and useful functions. Immobilization of alginate-PAC on Sepabeads EC-HA was used as a model system in order to demonstrate the potential of this strategy. Optimal conditions for covalent immobilization of alginate-PAC from Escherichia coli on support Sepabeads EC-HA were investigated. The immobilized enzyme was then characterized by evaluating the potential effects of immobilization on its thermal stability, temperature and pH profile in comparison with native non-modified PAC and modified non-immobilized PAC. The maximum amount of the alginate-PAC coupled on the dry support of 99 mg/g was satisfactory. Deactivation rate constants at 50°C for free PAC, alginate-PAC and alginate-PAC immobilized on Sepabeads EC-HA were 2.32, 50.65 and 1.68 h-1, respectively. Alginate-PAC and alginate-PAC immobilized on Sepabeads EC-HA had the same pH and temperature optimum as the native non-modified PAC.
AB  - U ovom radu započeto je sistematsko ispitivanje imobilizacije enzima modifikovanih derivatima alginata. Penicilin-acilaza (PAC) modifikovana je polialdehidnim derivatom alginata i zatim imobilisana na Sepabeads EC-HA nosač. Ispitani su optimalni uslovi za kovalentnu imobilizaciju modifikovane PAC i imobilisani enzim je okarakterisan u pogledu efekata imobilizacije na njegovu termalnu stabilnost, pH i temperaturni profil. Dodatno, imobilisani enzim je po pitanju ovih parametara upoređen kako sa nativnom tako i sa modifikovanom (alginat-PAC) formom enzima. Konstante brzine dezaktivacije za PAC, alginat-PAC i modifikovan enzim imobilisan na Sepabeads EC-HA (alginat-PAC-Sepabeads EC-HA) iznosile su redom 2,03, 36,48 i 1,23 h-1 na 40°C, odnosno 2,32, 50,65 i 1,68 h-1 na 50°C. Pokazano je da alginat-PAC i alginat-PAC-Sepabeads EC-HA imaju isti pH i temperaturni optimum kao i nativna PAC.
PB  - Association of Chemical Engineers of Serbia
T2  - Hemijska industrija
T1  - Immobilization of alginate-PAC on sepabeads EC-HA support
T1  - Imobilizacija penicilin-acilaze modifikovane derivatom alginata na sepabeads EC-HA nosač
EP  - 437
IS  - 4
SP  - 431
VL  - 65
DO  - 10.2298/HEMIND110318041Z
ER  - 

@article{
author = "Žuža, Milena and Milosavić, Nenad and Knežević-Jugović, Zorica",
year = "2011",
abstract = "Penicillin acylase (PAC) is an important industrial enzyme for the production of many β-lactam antibiotics. It is capable of catalyzing the hydrolysis of penicillin G (Pen G) to generate phenylacetic acid (PAA) and 6-aminopenicillanic acid (6-APA). In this paper, in order to prevent enzyme inactivation, an attempt of coupling enzyme modification and immobilization is presented. Chemical modification was promoted to introduce carbohydrate moiety into the PAC molecule, capable of being covalently linked to an amino support. This seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause a loss of activity. PAC molecules were modified by cross-linking with polyaldehyde derivatives of alginate in order to add them new and useful functions. Immobilization of alginate-PAC on Sepabeads EC-HA was used as a model system in order to demonstrate the potential of this strategy. Optimal conditions for covalent immobilization of alginate-PAC from Escherichia coli on support Sepabeads EC-HA were investigated. The immobilized enzyme was then characterized by evaluating the potential effects of immobilization on its thermal stability, temperature and pH profile in comparison with native non-modified PAC and modified non-immobilized PAC. The maximum amount of the alginate-PAC coupled on the dry support of 99 mg/g was satisfactory. Deactivation rate constants at 50°C for free PAC, alginate-PAC and alginate-PAC immobilized on Sepabeads EC-HA were 2.32, 50.65 and 1.68 h-1, respectively. Alginate-PAC and alginate-PAC immobilized on Sepabeads EC-HA had the same pH and temperature optimum as the native non-modified PAC., U ovom radu započeto je sistematsko ispitivanje imobilizacije enzima modifikovanih derivatima alginata. Penicilin-acilaza (PAC) modifikovana je polialdehidnim derivatom alginata i zatim imobilisana na Sepabeads EC-HA nosač. Ispitani su optimalni uslovi za kovalentnu imobilizaciju modifikovane PAC i imobilisani enzim je okarakterisan u pogledu efekata imobilizacije na njegovu termalnu stabilnost, pH i temperaturni profil. Dodatno, imobilisani enzim je po pitanju ovih parametara upoređen kako sa nativnom tako i sa modifikovanom (alginat-PAC) formom enzima. Konstante brzine dezaktivacije za PAC, alginat-PAC i modifikovan enzim imobilisan na Sepabeads EC-HA (alginat-PAC-Sepabeads EC-HA) iznosile su redom 2,03, 36,48 i 1,23 h-1 na 40°C, odnosno 2,32, 50,65 i 1,68 h-1 na 50°C. Pokazano je da alginat-PAC i alginat-PAC-Sepabeads EC-HA imaju isti pH i temperaturni optimum kao i nativna PAC.",
publisher = "Association of Chemical Engineers of Serbia",
journal = "Hemijska industrija",
title = "Immobilization of alginate-PAC on sepabeads EC-HA support, Imobilizacija penicilin-acilaze modifikovane derivatom alginata na sepabeads EC-HA nosač",
pages = "437-431",
number = "4",
volume = "65",
doi = "10.2298/HEMIND110318041Z"
}

Žuža, M., Milosavić, N.,& Knežević-Jugović, Z.. (2011). Immobilization of alginate-PAC on sepabeads EC-HA support. in Hemijska industrija
Association of Chemical Engineers of Serbia., 65(4), 431-437.
https://doi.org/10.2298/HEMIND110318041Z

Žuža M, Milosavić N, Knežević-Jugović Z. Immobilization of alginate-PAC on sepabeads EC-HA support. in Hemijska industrija. 2011;65(4):431-437.
doi:10.2298/HEMIND110318041Z .

Žuža, Milena, Milosavić, Nenad, Knežević-Jugović, Zorica, "Immobilization of alginate-PAC on sepabeads EC-HA support" in Hemijska industrija, 65, no. 4 (2011):431-437,
https://doi.org/10.2298/HEMIND110318041Z . .

TY  - JOUR
AU  - Šaponjić, Svetlana V.
AU  - Knežević-Jugović, Zorica
AU  - Bezbradica, Dejan
AU  - Žuža, Milena
AU  - Saied, Omar Ali
AU  - Bošković-Vragolović, Nevenka
AU  - Mijin, Dušan
PY  - 2010
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1691
AB  - Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion ( gt  99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g(-1) dry support and in a relatively short time (24 hrs) at 37 degrees C, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.
PB  - University of Catolica De Valparaiso, Valparaiso
T2  - Electronic Journal of Biotechnology
T1  - Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
IS  - 6
VL  - 13
DO  - 10.2225/vol13-issue6-fulltext-8
ER  - 

@article{
author = "Šaponjić, Svetlana V. and Knežević-Jugović, Zorica and Bezbradica, Dejan and Žuža, Milena and Saied, Omar Ali and Bošković-Vragolović, Nevenka and Mijin, Dušan",
year = "2010",
abstract = "Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion ( gt  99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g(-1) dry support and in a relatively short time (24 hrs) at 37 degrees C, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.",
publisher = "University of Catolica De Valparaiso, Valparaiso",
journal = "Electronic Journal of Biotechnology",
title = "Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study",
number = "6",
volume = "13",
doi = "10.2225/vol13-issue6-fulltext-8"
}

Šaponjić, S. V., Knežević-Jugović, Z., Bezbradica, D., Žuža, M., Saied, O. A., Bošković-Vragolović, N.,& Mijin, D.. (2010). Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study. in Electronic Journal of Biotechnology
University of Catolica De Valparaiso, Valparaiso., 13(6).
https://doi.org/10.2225/vol13-issue6-fulltext-8

Šaponjić SV, Knežević-Jugović Z, Bezbradica D, Žuža M, Saied OA, Bošković-Vragolović N, Mijin D. Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study. in Electronic Journal of Biotechnology. 2010;13(6).
doi:10.2225/vol13-issue6-fulltext-8 .

Šaponjić, Svetlana V., Knežević-Jugović, Zorica, Bezbradica, Dejan, Žuža, Milena, Saied, Omar Ali, Bošković-Vragolović, Nevenka, Mijin, Dušan, "Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study" in Electronic Journal of Biotechnology, 13, no. 6 (2010),
https://doi.org/10.2225/vol13-issue6-fulltext-8 . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Milosavić, Nenad
AU  - Knežević-Jugović, Zorica
PY  - 2009
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1447
AB  - An approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads(R) carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads(R) EC EA and Sepabeads(R) EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5-fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme.
PB  - Versita, Warsaw
T2  - Chemical Papers
T1  - Immobilization of modified penicillin G acylase on Sepabeads carriers
EP  - 124
IS  - 2
SP  - 117
VL  - 63
DO  - 10.2478/s11696-009-0012-z
ER  - 

@article{
author = "Žuža, Milena and Milosavić, Nenad and Knežević-Jugović, Zorica",
year = "2009",
abstract = "An approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads(R) carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads(R) EC EA and Sepabeads(R) EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5-fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme.",
publisher = "Versita, Warsaw",
journal = "Chemical Papers",
title = "Immobilization of modified penicillin G acylase on Sepabeads carriers",
pages = "124-117",
number = "2",
volume = "63",
doi = "10.2478/s11696-009-0012-z"
}

Žuža, M., Milosavić, N.,& Knežević-Jugović, Z.. (2009). Immobilization of modified penicillin G acylase on Sepabeads carriers. in Chemical Papers
Versita, Warsaw., 63(2), 117-124.
https://doi.org/10.2478/s11696-009-0012-z

Žuža M, Milosavić N, Knežević-Jugović Z. Immobilization of modified penicillin G acylase on Sepabeads carriers. in Chemical Papers. 2009;63(2):117-124.
doi:10.2478/s11696-009-0012-z .

Žuža, Milena, Milosavić, Nenad, Knežević-Jugović, Zorica, "Immobilization of modified penicillin G acylase on Sepabeads carriers" in Chemical Papers, 63, no. 2 (2009):117-124,
https://doi.org/10.2478/s11696-009-0012-z . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Šiler-Marinković, Slavica
AU  - Knežević, Zorica
PY  - 2007
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1061
AB  - This paper reports the covalent immobilization of penicillin G acylase from E. coli on Sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes the properties of the immobilized enzyme. Due to its versatility to mediate hydrolysis of penicillins and semi-synthetic B-lactam antibiotics synthesis reactions, the selected enzyme belongs to a class of biocatalysts of great industrial interest. The immobilized enzyme was characterized in its pH and thermal stability and reaction kinetics. The immobilization of penicillin acylase resulted in a slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted the structural and conformational stability to this enzyme. The immobilized enzyme also retained a high catalytic activity and showed the increased thermal stability compared with a free enzyme. By comparison of decimal reduction time values obtained at 50°C, it can be concluded that the immobilized enzyme was approximately 5-fold more stable than a free enzyme. The immobilization procedure developed is quite simple and easily reproduced, and provides a promising solution for the application of penicillin acylase for the purpose of 6-aminopenicillanic acid production.
PB  - Association of the Chemical Engineers of Serbia
T2  - Chemical Industry & Chemical Engineering Quarterly
T1  - Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier
EP  - 210
IS  - 4
SP  - 205
VL  - 13
DO  - 10.2298/CICEQ0704205Z
ER  - 

@article{
author = "Žuža, Milena and Šiler-Marinković, Slavica and Knežević, Zorica",
year = "2007",
abstract = "This paper reports the covalent immobilization of penicillin G acylase from E. coli on Sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes the properties of the immobilized enzyme. Due to its versatility to mediate hydrolysis of penicillins and semi-synthetic B-lactam antibiotics synthesis reactions, the selected enzyme belongs to a class of biocatalysts of great industrial interest. The immobilized enzyme was characterized in its pH and thermal stability and reaction kinetics. The immobilization of penicillin acylase resulted in a slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted the structural and conformational stability to this enzyme. The immobilized enzyme also retained a high catalytic activity and showed the increased thermal stability compared with a free enzyme. By comparison of decimal reduction time values obtained at 50°C, it can be concluded that the immobilized enzyme was approximately 5-fold more stable than a free enzyme. The immobilization procedure developed is quite simple and easily reproduced, and provides a promising solution for the application of penicillin acylase for the purpose of 6-aminopenicillanic acid production.",
publisher = "Association of the Chemical Engineers of Serbia",
journal = "Chemical Industry & Chemical Engineering Quarterly",
title = "Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier",
pages = "210-205",
number = "4",
volume = "13",
doi = "10.2298/CICEQ0704205Z"
}

Žuža, M., Šiler-Marinković, S.,& Knežević, Z.. (2007). Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier. in Chemical Industry & Chemical Engineering Quarterly
Association of the Chemical Engineers of Serbia., 13(4), 205-210.
https://doi.org/10.2298/CICEQ0704205Z

Žuža M, Šiler-Marinković S, Knežević Z. Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier. in Chemical Industry & Chemical Engineering Quarterly. 2007;13(4):205-210.
doi:10.2298/CICEQ0704205Z .

Žuža, Milena, Šiler-Marinković, Slavica, Knežević, Zorica, "Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier" in Chemical Industry & Chemical Engineering Quarterly, 13, no. 4 (2007):205-210,
https://doi.org/10.2298/CICEQ0704205Z . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Šiler-Marinković, Slavica
AU  - Knežević, Zorica
PY  - 2007
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1068
AB  - This paper describes the covalent immobilization of penicillin G acylase from Escherichia coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier and kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillins and semi-synthetic β-lactam antibiotics synthesis reactions. About 2.7 mg of the pure enzyme was immobilized onto each gram of sepabeads with an enzyme coupling yield of 96.9%. However, it seems that the activity coupling yield is not correlated with the amount of enzyme bound and the maximum yield of 89.4% can be achieved working at low enzyme loading (0.14 mg g-1). Immobilization of the penicillin acylase resulted in slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted structural and conformational stability of this enzyme. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems.
AB  - U radu je ispitana kovalentna imobilizacija penicilin-acilaze iz Escherichia coli na komercijalnom polimetakrilatnom nosaču sa epoksidnim funkcionalnim grupama (Sepabeads EC-EP) i dobijeni imobilisani enzim je okarakterisan u reakciji hidrolize penicilina. Izabrani enzim je od velikog industrijskog značaja jer katalizuje reakcije hidrolize prirodnih penicilina i sinteze polu-sintetskih β-laktamskih antibiotika. Ispitan je uticaj početne koncentracije enzima na masu i aktivnost imobilisanog enzima, kao i na maseni prinos imobilizacije i prinos aktivnosti. Najveća masa imobilisanog enzima je iznosila 2,5 mg po jedinici mase nosača, što odgovara masenom prinosu od 96,9%. Međutim, prinos aktivnosti je obrnuto proporcionalan masi imobilisanog enzima tako da se maksimalni prinos od 89,4% postiže pri imobilizaciji najmanje mase enzima (0,14 mg/g nosača). Imobilizacija enzima je prouzrokovala manje promene u pH profilu aktivnosti i optimalnim vrednostima temperature biokatalizatora, što ukazuje na neznatnu stabilizaciju enzima usled imobilizacije. Kinetika reakcije hidrolize prirodnog penicilina slobodnim i imobilisanim enzimom može se opisati Mihaelis- Mentenovom jednačinom i određene su vrednosti kinetičkih konstanti za oba sistema.
PB  - Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier
T1  - Imobilizacija penicilin-acilaze iz Escherichia coli na komercijalnom sepabeads nosaču
EP  - 182
IS  - 38
SP  - 173
DO  - 10.2298/APT0738173Z
ER  - 

@article{
author = "Žuža, Milena and Šiler-Marinković, Slavica and Knežević, Zorica",
year = "2007",
abstract = "This paper describes the covalent immobilization of penicillin G acylase from Escherichia coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier and kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillins and semi-synthetic β-lactam antibiotics synthesis reactions. About 2.7 mg of the pure enzyme was immobilized onto each gram of sepabeads with an enzyme coupling yield of 96.9%. However, it seems that the activity coupling yield is not correlated with the amount of enzyme bound and the maximum yield of 89.4% can be achieved working at low enzyme loading (0.14 mg g-1). Immobilization of the penicillin acylase resulted in slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted structural and conformational stability of this enzyme. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems., U radu je ispitana kovalentna imobilizacija penicilin-acilaze iz Escherichia coli na komercijalnom polimetakrilatnom nosaču sa epoksidnim funkcionalnim grupama (Sepabeads EC-EP) i dobijeni imobilisani enzim je okarakterisan u reakciji hidrolize penicilina. Izabrani enzim je od velikog industrijskog značaja jer katalizuje reakcije hidrolize prirodnih penicilina i sinteze polu-sintetskih β-laktamskih antibiotika. Ispitan je uticaj početne koncentracije enzima na masu i aktivnost imobilisanog enzima, kao i na maseni prinos imobilizacije i prinos aktivnosti. Najveća masa imobilisanog enzima je iznosila 2,5 mg po jedinici mase nosača, što odgovara masenom prinosu od 96,9%. Međutim, prinos aktivnosti je obrnuto proporcionalan masi imobilisanog enzima tako da se maksimalni prinos od 89,4% postiže pri imobilizaciji najmanje mase enzima (0,14 mg/g nosača). Imobilizacija enzima je prouzrokovala manje promene u pH profilu aktivnosti i optimalnim vrednostima temperature biokatalizatora, što ukazuje na neznatnu stabilizaciju enzima usled imobilizacije. Kinetika reakcije hidrolize prirodnog penicilina slobodnim i imobilisanim enzimom može se opisati Mihaelis- Mentenovom jednačinom i određene su vrednosti kinetičkih konstanti za oba sistema.",
publisher = "Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier, Imobilizacija penicilin-acilaze iz Escherichia coli na komercijalnom sepabeads nosaču",
pages = "182-173",
number = "38",
doi = "10.2298/APT0738173Z"
}

Žuža, M., Šiler-Marinković, S.,& Knežević, Z.. (2007). Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier. in Acta periodica technologica
Faculty of Technology, Novi Sad.(38), 173-182.
https://doi.org/10.2298/APT0738173Z

Žuža M, Šiler-Marinković S, Knežević Z. Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier. in Acta periodica technologica. 2007;(38):173-182.
doi:10.2298/APT0738173Z .

Žuža, Milena, Šiler-Marinković, Slavica, Knežević, Zorica, "Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier" in Acta periodica technologica, no. 38 (2007):173-182,
https://doi.org/10.2298/APT0738173Z . .

TY  - JOUR
AU  - Žuža, Milena
AU  - Šiler-Marinković, Slavica
AU  - Knežević, Zorica
PY  - 2007
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1195
AB  - This paper reports the covalent immobilization of penicillin G acylase from E. coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillin and semi-synthetic b-lactam antibiotics synthesis reactions. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems. .
PB  - Univerzitet u Nišu - Tehnološki fakultet, Leskovac
T2  - Zbornik radova Tehnološkog fakulteta, Leskovac
T1  - Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier
EP  - 42
IS  - 16
SP  - 33
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1195
ER  - 

@article{
author = "Žuža, Milena and Šiler-Marinković, Slavica and Knežević, Zorica",
year = "2007",
abstract = "This paper reports the covalent immobilization of penicillin G acylase from E. coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillin and semi-synthetic b-lactam antibiotics synthesis reactions. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems. .",
publisher = "Univerzitet u Nišu - Tehnološki fakultet, Leskovac",
journal = "Zbornik radova Tehnološkog fakulteta, Leskovac",
title = "Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier",
pages = "42-33",
number = "16",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1195"
}

Žuža, M., Šiler-Marinković, S.,& Knežević, Z.. (2007). Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier. in Zbornik radova Tehnološkog fakulteta, Leskovac
Univerzitet u Nišu - Tehnološki fakultet, Leskovac.(16), 33-42.
https://hdl.handle.net/21.15107/rcub_technorep_1195

Žuža M, Šiler-Marinković S, Knežević Z. Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier. in Zbornik radova Tehnološkog fakulteta, Leskovac. 2007;(16):33-42.
https://hdl.handle.net/21.15107/rcub_technorep_1195 .

Žuža, Milena, Šiler-Marinković, Slavica, Knežević, Zorica, "Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier" in Zbornik radova Tehnološkog fakulteta, Leskovac, no. 16 (2007):33-42,
https://hdl.handle.net/21.15107/rcub_technorep_1195 .