TY  - JOUR
AU  - Ilic-Durdic, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Durdevic-Delmas, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1488
AB  - The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) fromPhanerochaete chrysosporiumis a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 10(4) independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.
PB  - Higher Education Press, Beijing
T2  - Frontiers of Environmental Science & Engineering
T1  - Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls
IS  - 2
VL  - 15
DO  - 10.1007/s11783-020-1311-4
ER  - 

@article{
author = "Ilic-Durdic, Karla and Ostafe, Raluca and Prodanović, Olivera and Durdevic-Delmas, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
abstract = "The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) fromPhanerochaete chrysosporiumis a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 10(4) independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.",
publisher = "Higher Education Press, Beijing",
journal = "Frontiers of Environmental Science & Engineering",
title = "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls",
number = "2",
volume = "15",
doi = "10.1007/s11783-020-1311-4"
}

Ilic-Durdic, K., Ostafe, R., Prodanović, O., Durdevic-Delmas, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering
Higher Education Press, Beijing., 15(2).
https://doi.org/10.1007/s11783-020-1311-4

Ilic-Durdic K, Ostafe R, Prodanović O, Durdevic-Delmas A, Popović N, Fischer R, Schillberg S, Prodanović R. Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering. 2021;15(2).
doi:10.1007/s11783-020-1311-4 .

Ilic-Durdic, Karla, Ostafe, Raluca, Prodanović, Olivera, Durdevic-Delmas, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls" in Frontiers of Environmental Science & Engineering, 15, no. 2 (2021),
https://doi.org/10.1007/s11783-020-1311-4 . .

TY  - JOUR
AU  - Balaž, Ana Marija
AU  - BLazic, Marija B.
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1297
AB  - Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZ alpha plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion-exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s(-1) for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM(-1) s(-1). All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain
EP  - 35
IS  - 1
SP  - 25
VL  - 85
DO  - 10.2298/JSC190320058B
ER  - 

@article{
author = "Balaž, Ana Marija and BLazic, Marija B. and Popović, Nikolina and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZ alpha plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion-exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s(-1) for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM(-1) s(-1). All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain",
pages = "35-25",
number = "1",
volume = "85",
doi = "10.2298/JSC190320058B"
}

Balaž, A. M., BLazic, M. B., Popović, N., Prodanović, O., Ostafe, R., Fischer, R.,& Prodanović, R.. (2020). Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 85(1), 25-35.
https://doi.org/10.2298/JSC190320058B

Balaž AM, BLazic MB, Popović N, Prodanović O, Ostafe R, Fischer R, Prodanović R. Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society. 2020;85(1):25-35.
doi:10.2298/JSC190320058B .

Balaž, Ana Marija, BLazic, Marija B., Popović, Nikolina, Prodanović, Olivera, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain" in Journal of the Serbian Chemical Society, 85, no. 1 (2020):25-35,
https://doi.org/10.2298/JSC190320058B . .

TY  - CONF
AU  - Balaz, Ana Marija
AU  - Popov, Neda
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/3043
AB  - Phanerochaete chrysosporium is a white rot fungi and it has been known to secrete
flavocytochrome enzyme cellobiose dehydrogenase (CDH, EC 1.1.99.18) which contains
two domains, a flavine domain and cytochrome domain. Flavine domain contains FAD as
prostetic group and its catalytically active domain, whereas cytochrome domain serves as
electrone acceptor. Cellobiose and lactose, as well as other β – 1,4 – linked disaccharides
and oligosaccharides, have been oxidized by the cellobiose dehydrogenase to their
corresponding lactones. CDH can be used for constructing biosensors and therefore
directed evolution has been used to produce more active and stable variants of the enzyme.
Wild type CDH enzyme was expressed in S.cerevisiae INVSc1 cells and used for creation
of saturation mutagenesis libraries at M65, M685 and M738 and screening for increased
oxidative stability. More stable mutants that were found were recloned into Pichia pastoris
KM71H strain for higher expression yield. They were afterwards, expressed in Pichia,
purified and kineticaly characterized.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
T1  - Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain
EP  - 75
SP  - 74
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_3043
ER  - 

@conference{
author = "Balaz, Ana Marija and Popov, Neda and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Phanerochaete chrysosporium is a white rot fungi and it has been known to secrete
flavocytochrome enzyme cellobiose dehydrogenase (CDH, EC 1.1.99.18) which contains
two domains, a flavine domain and cytochrome domain. Flavine domain contains FAD as
prostetic group and its catalytically active domain, whereas cytochrome domain serves as
electrone acceptor. Cellobiose and lactose, as well as other β – 1,4 – linked disaccharides
and oligosaccharides, have been oxidized by the cellobiose dehydrogenase to their
corresponding lactones. CDH can be used for constructing biosensors and therefore
directed evolution has been used to produce more active and stable variants of the enzyme.
Wild type CDH enzyme was expressed in S.cerevisiae INVSc1 cells and used for creation
of saturation mutagenesis libraries at M65, M685 and M738 and screening for increased
oxidative stability. More stable mutants that were found were recloned into Pichia pastoris
KM71H strain for higher expression yield. They were afterwards, expressed in Pichia,
purified and kineticaly characterized.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry",
title = "Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain",
pages = "75-74",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3043"
}

Balaz, A. M., Popov, N., Prodanović, O., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
Faculty of Chemistry, Serbian Biochemical Society., 74-75.
https://hdl.handle.net/21.15107/rcub_rimsi_3043

Balaz AM, Popov N, Prodanović O, Ostafe R, Fischer R, Prodanović R. Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry. 2019;:74-75.
https://hdl.handle.net/21.15107/rcub_rimsi_3043 .

Balaz, Ana Marija, Popov, Neda, Prodanović, Olivera, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain" in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry (2019):74-75,
https://hdl.handle.net/21.15107/rcub_rimsi_3043 .

TY  - CONF
AU  - Stanišić, Marija
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/2912
AB  - Pectins belong to a group of a plant polysaccharides that are structural components of plant
cell walls. These polysaccharides have big potential for use in the food industry as a
gelling agents and biomedical application due their biocompatibility, biodegradability, low
price, etc. Chemical modifications of pectin are useful methods for introducing various
functional groups, which give pectin hydrogels novel properties. In this study, pectin was
modified by oxidation with sodium periodate at molar ratios of 5, 10 and 15 mol% and
reductive amination with dopamine and sodium cyanoborohydride afterwards. This
modification of pectin was confirmed by UV-VIS and NMR spectroscopy. Dopaminepectins showed gelling properties in the presence of laccase and oxygen. These pectin
derivatives were tested as carriers for laccase immobilization within microbeads formed in
an emulsion based enzymatic polymerization reaction. Laccase was expressed in functional
form in E. coli, isolated and additionally purified. We determined optimal conditions for
immobilization andobtained microbeads with specific activity of 0.0006 IU/mg and 40%
yield of immobilization. The immobilized laccase could be used for various application,
such as decolorization of textile dyes 
.
PB  - Serbian Biochemical Society
C3  - The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
T1  - Dopamine-modified pectins for laccase induced hydrogel formation and immobilization
EP  - 168
SP  - 168
UR  - https://hdl.handle.net/21.15107/rcub_rimsi_2912
ER  - 

@conference{
author = "Stanišić, Marija and Popović, Nikolina and Prodanović, Olivera and Prodanović, Radivoje",
year = "2019",
abstract = "Pectins belong to a group of a plant polysaccharides that are structural components of plant
cell walls. These polysaccharides have big potential for use in the food industry as a
gelling agents and biomedical application due their biocompatibility, biodegradability, low
price, etc. Chemical modifications of pectin are useful methods for introducing various
functional groups, which give pectin hydrogels novel properties. In this study, pectin was
modified by oxidation with sodium periodate at molar ratios of 5, 10 and 15 mol% and
reductive amination with dopamine and sodium cyanoborohydride afterwards. This
modification of pectin was confirmed by UV-VIS and NMR spectroscopy. Dopaminepectins showed gelling properties in the presence of laccase and oxygen. These pectin
derivatives were tested as carriers for laccase immobilization within microbeads formed in
an emulsion based enzymatic polymerization reaction. Laccase was expressed in functional
form in E. coli, isolated and additionally purified. We determined optimal conditions for
immobilization andobtained microbeads with specific activity of 0.0006 IU/mg and 40%
yield of immobilization. The immobilized laccase could be used for various application,
such as decolorization of textile dyes 
.",
publisher = "Serbian Biochemical Society",
journal = "The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry",
title = "Dopamine-modified pectins for laccase induced hydrogel formation and immobilization",
pages = "168-168",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_2912"
}

Stanišić, M., Popović, N., Prodanović, O.,& Prodanović, R.. (2019). Dopamine-modified pectins for laccase induced hydrogel formation and immobilization. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry
Serbian Biochemical Society., 168-168.
https://hdl.handle.net/21.15107/rcub_rimsi_2912

Stanišić M, Popović N, Prodanović O, Prodanović R. Dopamine-modified pectins for laccase induced hydrogel formation and immobilization. in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry. 2019;:168-168.
https://hdl.handle.net/21.15107/rcub_rimsi_2912 .

Stanišić, Marija, Popović, Nikolina, Prodanović, Olivera, Prodanović, Radivoje, "Dopamine-modified pectins for laccase induced hydrogel formation and immobilization" in The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry (2019):168-168,
https://hdl.handle.net/21.15107/rcub_rimsi_2912 .

TY  - JOUR
AU  - Drvenica, Ivana T.
AU  - Stancic, Ana Z.
AU  - Kalusević, Ana M.
AU  - Marković, Smilja
AU  - Dragišić Maksimović, Jelena
AU  - Nedović, Viktor A.
AU  - Bugarski, Branko M.
AU  - Ilic, Vesna Lj
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1270
AB  - Slaughterhouse blood represents a valuable source of hemoglobin, which can be used in the production of heme-iron based supplements for the prevention/treatment of iron-deficiency anemia. In order to obtain a stable solid-state formulation, the effect of maltose addition (30 %) on the stability and storage of bovine and porcine hemoglobin in powders obtained by spray-and freeze-drying (without maltose: Hb; with maltose: HbM) were investigated. Differential scanning calorimetry of spray- and freeze-dried powders indicated satisfying quality of the formulation prepared with maltose on dissolving back into solution. After two-year storage at room temperature (20 +/- 5 degrees C) in solid forms, protected from moisture and light, rehydrated spray- and freeze- dried HbM were red, while Hb were brown. Dynamic light scattering showed the presence of native hemoglobin monomers in rehydrated spray- and freeze- dried HbM, but their agglomerates in Hb samples. UV-Vis spectrophotometry confirmed an absence of significant hemoglobin denaturation and methemoglobin formation in HbM freeze-dried powders. In spray-dried HbM, an increased level of methemoglobin was detected. The results confirmed the stabilizing effect of maltose, and suggested its use in the production of long-term stable solid-state formulations of hemoglobin, along with drying processes optimization.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Maltose-mediated, long-term stabilization of freeze- and spray-dried forms of bovine and porcine hemoglobin
EP  - 1117
IS  - 10
SP  - 1105
VL  - 84
DO  - 10.2298/JSC190513067D
ER  - 

@article{
author = "Drvenica, Ivana T. and Stancic, Ana Z. and Kalusević, Ana M. and Marković, Smilja and Dragišić Maksimović, Jelena and Nedović, Viktor A. and Bugarski, Branko M. and Ilic, Vesna Lj",
year = "2019",
abstract = "Slaughterhouse blood represents a valuable source of hemoglobin, which can be used in the production of heme-iron based supplements for the prevention/treatment of iron-deficiency anemia. In order to obtain a stable solid-state formulation, the effect of maltose addition (30 %) on the stability and storage of bovine and porcine hemoglobin in powders obtained by spray-and freeze-drying (without maltose: Hb; with maltose: HbM) were investigated. Differential scanning calorimetry of spray- and freeze-dried powders indicated satisfying quality of the formulation prepared with maltose on dissolving back into solution. After two-year storage at room temperature (20 +/- 5 degrees C) in solid forms, protected from moisture and light, rehydrated spray- and freeze- dried HbM were red, while Hb were brown. Dynamic light scattering showed the presence of native hemoglobin monomers in rehydrated spray- and freeze- dried HbM, but their agglomerates in Hb samples. UV-Vis spectrophotometry confirmed an absence of significant hemoglobin denaturation and methemoglobin formation in HbM freeze-dried powders. In spray-dried HbM, an increased level of methemoglobin was detected. The results confirmed the stabilizing effect of maltose, and suggested its use in the production of long-term stable solid-state formulations of hemoglobin, along with drying processes optimization.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Maltose-mediated, long-term stabilization of freeze- and spray-dried forms of bovine and porcine hemoglobin",
pages = "1117-1105",
number = "10",
volume = "84",
doi = "10.2298/JSC190513067D"
}

Drvenica, I. T., Stancic, A. Z., Kalusević, A. M., Marković, S., Dragišić Maksimović, J., Nedović, V. A., Bugarski, B. M.,& Ilic, V. L.. (2019). Maltose-mediated, long-term stabilization of freeze- and spray-dried forms of bovine and porcine hemoglobin. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 84(10), 1105-1117.
https://doi.org/10.2298/JSC190513067D

Drvenica IT, Stancic AZ, Kalusević AM, Marković S, Dragišić Maksimović J, Nedović VA, Bugarski BM, Ilic VL. Maltose-mediated, long-term stabilization of freeze- and spray-dried forms of bovine and porcine hemoglobin. in Journal of the Serbian Chemical Society. 2019;84(10):1105-1117.
doi:10.2298/JSC190513067D .

Drvenica, Ivana T., Stancic, Ana Z., Kalusević, Ana M., Marković, Smilja, Dragišić Maksimović, Jelena, Nedović, Viktor A., Bugarski, Branko M., Ilic, Vesna Lj, "Maltose-mediated, long-term stabilization of freeze- and spray-dried forms of bovine and porcine hemoglobin" in Journal of the Serbian Chemical Society, 84, no. 10 (2019):1105-1117,
https://doi.org/10.2298/JSC190513067D . .

TY  - JOUR
AU  - Spasojević, Ljiljana
AU  - Katona, Jaroslav
AU  - Bucko, Sandra
AU  - Savić, Slavica M.
AU  - Petrović, Lidija
AU  - Milinkovic-Budinicic, Jelena
AU  - Tasić, Nikola
AU  - Aidarova, Saule
AU  - Sharipova, Altynay
PY  - 2019
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1233
AB  - Zein, a corn protein, is often used for preparing edible films and coatings. Since zein is insoluble in water, zein films and coatings are usually prepared by spraying or casting its aqueous ethanol solutions to a contact surface (Z(sol) films). However, the use of organic solvents in many food applications is unwanted. In this work, aqueous dispersions of zein nanoparticles were prepared by antisolvent precipitation from 90% v/v aqueous ethanol zein solutions. Zein films were then prepared by casting the dispersions in silicone molds and air-drying at 50 degrees C (Z(dis) films), The obtained films were characterized for morphology, FTIR analysis, mechanical, water barrier and optical properties, and were benchmarked against Z(sol) films. It was found that continuous zein films can be prepared out of aqueous dispersions of zein nanoparticles. Z(dis) films proved to have grainy morphology and higher surface roughness when compared to Z(sol). Surface roughness of Z(dis) films was decreased when plasticizer was added. Water barrier properties of Z(dis) films were found to be comparable to Z(sol) films. No differences in mechanical properties were found between Z(sol) and Z(dis) film. Size of zein particles influenced morphology and optical properties of zein dispersion films.
PB  - Elsevier Science Bv, Amsterdam
T2  - LWT-Food Science and Technology
T1  - Edible water barrier films prepared from aqueous dispersions of zein nanoparticles
EP  - 358
SP  - 350
VL  - 109
DO  - 10.1016/j.lwt.2019.04.038
ER  - 

@article{
author = "Spasojević, Ljiljana and Katona, Jaroslav and Bucko, Sandra and Savić, Slavica M. and Petrović, Lidija and Milinkovic-Budinicic, Jelena and Tasić, Nikola and Aidarova, Saule and Sharipova, Altynay",
year = "2019",
abstract = "Zein, a corn protein, is often used for preparing edible films and coatings. Since zein is insoluble in water, zein films and coatings are usually prepared by spraying or casting its aqueous ethanol solutions to a contact surface (Z(sol) films). However, the use of organic solvents in many food applications is unwanted. In this work, aqueous dispersions of zein nanoparticles were prepared by antisolvent precipitation from 90% v/v aqueous ethanol zein solutions. Zein films were then prepared by casting the dispersions in silicone molds and air-drying at 50 degrees C (Z(dis) films), The obtained films were characterized for morphology, FTIR analysis, mechanical, water barrier and optical properties, and were benchmarked against Z(sol) films. It was found that continuous zein films can be prepared out of aqueous dispersions of zein nanoparticles. Z(dis) films proved to have grainy morphology and higher surface roughness when compared to Z(sol). Surface roughness of Z(dis) films was decreased when plasticizer was added. Water barrier properties of Z(dis) films were found to be comparable to Z(sol) films. No differences in mechanical properties were found between Z(sol) and Z(dis) film. Size of zein particles influenced morphology and optical properties of zein dispersion films.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "LWT-Food Science and Technology",
title = "Edible water barrier films prepared from aqueous dispersions of zein nanoparticles",
pages = "358-350",
volume = "109",
doi = "10.1016/j.lwt.2019.04.038"
}

Spasojević, L., Katona, J., Bucko, S., Savić, S. M., Petrović, L., Milinkovic-Budinicic, J., Tasić, N., Aidarova, S.,& Sharipova, A.. (2019). Edible water barrier films prepared from aqueous dispersions of zein nanoparticles. in LWT-Food Science and Technology
Elsevier Science Bv, Amsterdam., 109, 350-358.
https://doi.org/10.1016/j.lwt.2019.04.038

Spasojević L, Katona J, Bucko S, Savić SM, Petrović L, Milinkovic-Budinicic J, Tasić N, Aidarova S, Sharipova A. Edible water barrier films prepared from aqueous dispersions of zein nanoparticles. in LWT-Food Science and Technology. 2019;109:350-358.
doi:10.1016/j.lwt.2019.04.038 .

Spasojević, Ljiljana, Katona, Jaroslav, Bucko, Sandra, Savić, Slavica M., Petrović, Lidija, Milinkovic-Budinicic, Jelena, Tasić, Nikola, Aidarova, Saule, Sharipova, Altynay, "Edible water barrier films prepared from aqueous dispersions of zein nanoparticles" in LWT-Food Science and Technology, 109 (2019):350-358,
https://doi.org/10.1016/j.lwt.2019.04.038 . .