Knezevic-Jugović, Zorica D

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orcid::0000-0003-3009-1698
  • Knezevic-Jugović, Zorica D (2)
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Author's Bibliography

Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates

Moftah, Omar Ali Saied; Grbavcic, Sanja Z; Moftah, Walid AS; Luković, Nevena D; Prodanović, Olivera; Jakovetic, Sonja M; Knezevic-Jugović, Zorica D

(Srpsko hemijsko društvo, Beograd, 2013)

TY  - JOUR
AU  - Moftah, Omar Ali Saied
AU  - Grbavcic, Sanja Z
AU  - Moftah, Walid AS
AU  - Luković, Nevena D
AU  - Prodanović, Olivera
AU  - Jakovetic, Sonja M
AU  - Knezevic-Jugović, Zorica D
PY  - 2013
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/694
AB  - In this study, the solid and liquid wastes from the olive oil processing industry were evaluated as substrates for Yarrowia lipolytica growth with the aim of lipase production. Olive mill wastewater and olive oil cake seemed to provide the necessary nutrients and physical support for yeast growth and enzyme production. The highest lipolytic activity of 850 IU dm(3) was achieved after 4 days of submerged cultivation in supplemented olive mill wastewater. In addition, olive oil cake appeared to be a convenient substrate for lipase production under a solid-state fermentation mode. Lipase production was further improved by media supplementation and/or change in the physical settings of the experiment. However, the most significant improvement of lipase production under solid-state fermentation was achieved by an alkaline treatment of the substrate (more than 10-fold), when the amount of produced lipase reached up to approximate to 40 IU g(-1) of substrate.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates
EP  - 794
IS  - 6
SP  - 781
VL  - 78
DO  - 10.2298/JSC120905005M
ER  - 
@article{
author = "Moftah, Omar Ali Saied and Grbavcic, Sanja Z and Moftah, Walid AS and Luković, Nevena D and Prodanović, Olivera and Jakovetic, Sonja M and Knezevic-Jugović, Zorica D",
year = "2013",
abstract = "In this study, the solid and liquid wastes from the olive oil processing industry were evaluated as substrates for Yarrowia lipolytica growth with the aim of lipase production. Olive mill wastewater and olive oil cake seemed to provide the necessary nutrients and physical support for yeast growth and enzyme production. The highest lipolytic activity of 850 IU dm(3) was achieved after 4 days of submerged cultivation in supplemented olive mill wastewater. In addition, olive oil cake appeared to be a convenient substrate for lipase production under a solid-state fermentation mode. Lipase production was further improved by media supplementation and/or change in the physical settings of the experiment. However, the most significant improvement of lipase production under solid-state fermentation was achieved by an alkaline treatment of the substrate (more than 10-fold), when the amount of produced lipase reached up to approximate to 40 IU g(-1) of substrate.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates",
pages = "794-781",
number = "6",
volume = "78",
doi = "10.2298/JSC120905005M"
}
Moftah, O. A. S., Grbavcic, S. Z., Moftah, W. A., Luković, N. D., Prodanović, O., Jakovetic, S. M.,& Knezevic-Jugović, Z. D.. (2013). Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 78(6), 781-794.
https://doi.org/10.2298/JSC120905005M
Moftah OAS, Grbavcic SZ, Moftah WA, Luković ND, Prodanović O, Jakovetic SM, Knezevic-Jugović ZD. Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates. in Journal of the Serbian Chemical Society. 2013;78(6):781-794.
doi:10.2298/JSC120905005M .
Moftah, Omar Ali Saied, Grbavcic, Sanja Z, Moftah, Walid AS, Luković, Nevena D, Prodanović, Olivera, Jakovetic, Sonja M, Knezevic-Jugović, Zorica D, "Lipase production by Yarrowia lipolytica using olive oil processing wastes as substrates" in Journal of the Serbian Chemical Society, 78, no. 6 (2013):781-794,
https://doi.org/10.2298/JSC120905005M . .
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Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers

Prodanović, Olivera; Prokopijević, Miloš; Spasojević, Dragica; Stojanović, Zeljko P; Radotić, Ksenija; Knezevic-Jugović, Zorica D; Prodanović, Radivoje

(Springer, New York, 2012)

TY  - JOUR
AU  - Prodanović, Olivera
AU  - Prokopijević, Miloš
AU  - Spasojević, Dragica
AU  - Stojanović, Zeljko P
AU  - Radotić, Ksenija
AU  - Knezevic-Jugović, Zorica D
AU  - Prodanović, Radivoje
PY  - 2012
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/586
AB  - A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.
PB  - Springer, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers
EP  - 1301
IS  - 5
SP  - 1288
VL  - 168
DO  - 10.1007/s12010-012-9857-7
ER  - 
@article{
author = "Prodanović, Olivera and Prokopijević, Miloš and Spasojević, Dragica and Stojanović, Zeljko P and Radotić, Ksenija and Knezevic-Jugović, Zorica D and Prodanović, Radivoje",
year = "2012",
abstract = "A macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.",
publisher = "Springer, New York",
journal = "Applied Biochemistry and Biotechnology",
title = "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers",
pages = "1301-1288",
number = "5",
volume = "168",
doi = "10.1007/s12010-012-9857-7"
}
Prodanović, O., Prokopijević, M., Spasojević, D., Stojanović, Z. P., Radotić, K., Knezevic-Jugović, Z. D.,& Prodanović, R.. (2012). Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology
Springer, New York., 168(5), 1288-1301.
https://doi.org/10.1007/s12010-012-9857-7
Prodanović O, Prokopijević M, Spasojević D, Stojanović ZP, Radotić K, Knezevic-Jugović ZD, Prodanović R. Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers. in Applied Biochemistry and Biotechnology. 2012;168(5):1288-1301.
doi:10.1007/s12010-012-9857-7 .
Prodanović, Olivera, Prokopijević, Miloš, Spasojević, Dragica, Stojanović, Zeljko P, Radotić, Ksenija, Knezevic-Jugović, Zorica D, Prodanović, Radivoje, "Improved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymers" in Applied Biochemistry and Biotechnology, 168, no. 5 (2012):1288-1301,
https://doi.org/10.1007/s12010-012-9857-7 . .
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