TY  - JOUR
AU  - Mijin, Nemanja
AU  - Milošević, Jelica
AU  - Stevanović, Sanja
AU  - Petrović, Predrag
AU  - Lolić, Aleksandar
AU  - Urbic, Tomaz
AU  - Polović, Natalija
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5987
AB  - The aggregation of proteins into fibrillar, amyloid-like aggregates generally results in an improved, positive effect on various techno-functional properties within food products, such as gelation, emulsification, and foam stabilization. These highly stable structures, characterized by their repetitive, β-sheet rich motifs, may develop as the result of the thermal treatment of protein-rich food products. Heavy metal ions can influence amyloid-like aggregation of food proteins. Lead(II) and cadmium(II) represent some of the most abundant and common environmental water and food pollutants. In this work, the influence of heavy metal ions, lead and cadmium on amyloid-like aggregation of ovalbumin at high temperatures (90 °C) and under acidic conditions (pH 2.0) was investigated. Ovalbumin is used as a general model for how heavy metals can affect amyloid-like aggregation of a food protein. Structural changes were monitored via Thioflavin T and 8-Anilino-1-naphthalenesulfonic acid fluorescence, Fourier-Transform infrared spectroscopy, atomic force microscopy, dynamic light scattering, as well as computational analyses. The obtained results indicate that the added heavy metal ions bind to different sites within ovalbumin prior to thermal treatment. Lead binding sites are closer to the hydrophobic regions of an protein, while cadmium ion binding sites are more exposed. This specific binding of metal ions affects the morphologies of amyloid-like aggregates, resulting in lead-induced branching of amyloid-like fibrils, or cadmium-induced tangling of fibrils into dense amyloid clusters. This additive effect of heavy metal ions is most evident in ovalbumin samples which contain a mixture of both heavy metal ions.
PB  - Elsevier B.V.
T2  - Food Hydrocolloids
T1  - Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin
VL  - 136
SP  - 108292
DO  - 10.1016/j.foodhyd.2022.108292
ER  - 

@article{
author = "Mijin, Nemanja and Milošević, Jelica and Stevanović, Sanja and Petrović, Predrag and Lolić, Aleksandar and Urbic, Tomaz and Polović, Natalija",
year = "2023",
abstract = "The aggregation of proteins into fibrillar, amyloid-like aggregates generally results in an improved, positive effect on various techno-functional properties within food products, such as gelation, emulsification, and foam stabilization. These highly stable structures, characterized by their repetitive, β-sheet rich motifs, may develop as the result of the thermal treatment of protein-rich food products. Heavy metal ions can influence amyloid-like aggregation of food proteins. Lead(II) and cadmium(II) represent some of the most abundant and common environmental water and food pollutants. In this work, the influence of heavy metal ions, lead and cadmium on amyloid-like aggregation of ovalbumin at high temperatures (90 °C) and under acidic conditions (pH 2.0) was investigated. Ovalbumin is used as a general model for how heavy metals can affect amyloid-like aggregation of a food protein. Structural changes were monitored via Thioflavin T and 8-Anilino-1-naphthalenesulfonic acid fluorescence, Fourier-Transform infrared spectroscopy, atomic force microscopy, dynamic light scattering, as well as computational analyses. The obtained results indicate that the added heavy metal ions bind to different sites within ovalbumin prior to thermal treatment. Lead binding sites are closer to the hydrophobic regions of an protein, while cadmium ion binding sites are more exposed. This specific binding of metal ions affects the morphologies of amyloid-like aggregates, resulting in lead-induced branching of amyloid-like fibrils, or cadmium-induced tangling of fibrils into dense amyloid clusters. This additive effect of heavy metal ions is most evident in ovalbumin samples which contain a mixture of both heavy metal ions.",
publisher = "Elsevier B.V.",
journal = "Food Hydrocolloids",
title = "Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin",
volume = "136",
pages = "108292",
doi = "10.1016/j.foodhyd.2022.108292"
}

Mijin, N., Milošević, J., Stevanović, S., Petrović, P., Lolić, A., Urbic, T.,& Polović, N.. (2023). Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin. in Food Hydrocolloids
Elsevier B.V.., 136, 108292.
https://doi.org/10.1016/j.foodhyd.2022.108292

Mijin N, Milošević J, Stevanović S, Petrović P, Lolić A, Urbic T, Polović N. Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin. in Food Hydrocolloids. 2023;136:108292.
doi:10.1016/j.foodhyd.2022.108292 .

Mijin, Nemanja, Milošević, Jelica, Stevanović, Sanja, Petrović, Predrag, Lolić, Aleksandar, Urbic, Tomaz, Polović, Natalija, "Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin" in Food Hydrocolloids, 136 (2023):108292,
https://doi.org/10.1016/j.foodhyd.2022.108292 . .

TY  - JOUR
AU  - Marković, Srdjan
AU  - Andrejević, Natalija S.
AU  - Milošević, Jelica
AU  - Polović, Natalija
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6289
AB  - The significant role of papain-like cysteine proteases, including papain, cathepsin L and SARS-CoV-2 PLpro, in biomedicine and biotechnology makes them interesting model systems for sensor development. These enzymes have a free thiol group that is suitable for many sensor designs including strong binding to gold nanoparticles or low-molecular-weight inhibitors. Focusing on the importance of the preservation of native protein structure for inhibitor-binding and molecular-imprinting, which has been applied in some efficient examples of sensor development, the aim of this work was to examine the effects of the free-thiol-group’s reversible blocking on papain denaturation that is the basis of its activity loss and aggregation. To utilize biophysical methods common in protein structural transitions characterization, such as fluorimetry and high-resolution infrared spectroscopy, low-molecular-weight electrophilic thiol blocking reagent S-Methyl methanethiosulfonate (MMTS) was used in solution. MMTS binding led to a two-fold increase in 8-Anilinonaphthalene-1-sulfonic acid fluorescence, indicating increased hydrophobic residue exposure. A more in-depth analysis showed significant transitions on the secondary structure level upon MMTS binding, mostly characterized by the lowered content of α-helices and unordered structures (either for approximately one third), and the increase in aggregation-specific β-sheets (from 25 to 52%) in a dose-dependant manner. The recovery of this inhibited protein showed that reversibility of inhibition is accompanied by reversibility of protein denaturation. Nevertheless, a 100-fold molar excess of the inhibitor led to the incomplete recovery of proteolytic activity, which can be explained by irreversible denaturation. The structural stability of the C-terminal β-sheet rich domain of the papain-like cysteine protease family opens up an interesting possibility to use its foldamers as a strategy for sensor development and other multiple potential applications that rely on the great commercial value of papain-like cysteine proteases.
PB  - MDPI
T2  - Biomimetics
T1  - Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development
VL  - 8
IS  - 3
SP  - 281
DO  - 10.3390/biomimetics8030281
ER  - 

@article{
author = "Marković, Srdjan and Andrejević, Natalija S. and Milošević, Jelica and Polović, Natalija",
year = "2023",
abstract = "The significant role of papain-like cysteine proteases, including papain, cathepsin L and SARS-CoV-2 PLpro, in biomedicine and biotechnology makes them interesting model systems for sensor development. These enzymes have a free thiol group that is suitable for many sensor designs including strong binding to gold nanoparticles or low-molecular-weight inhibitors. Focusing on the importance of the preservation of native protein structure for inhibitor-binding and molecular-imprinting, which has been applied in some efficient examples of sensor development, the aim of this work was to examine the effects of the free-thiol-group’s reversible blocking on papain denaturation that is the basis of its activity loss and aggregation. To utilize biophysical methods common in protein structural transitions characterization, such as fluorimetry and high-resolution infrared spectroscopy, low-molecular-weight electrophilic thiol blocking reagent S-Methyl methanethiosulfonate (MMTS) was used in solution. MMTS binding led to a two-fold increase in 8-Anilinonaphthalene-1-sulfonic acid fluorescence, indicating increased hydrophobic residue exposure. A more in-depth analysis showed significant transitions on the secondary structure level upon MMTS binding, mostly characterized by the lowered content of α-helices and unordered structures (either for approximately one third), and the increase in aggregation-specific β-sheets (from 25 to 52%) in a dose-dependant manner. The recovery of this inhibited protein showed that reversibility of inhibition is accompanied by reversibility of protein denaturation. Nevertheless, a 100-fold molar excess of the inhibitor led to the incomplete recovery of proteolytic activity, which can be explained by irreversible denaturation. The structural stability of the C-terminal β-sheet rich domain of the papain-like cysteine protease family opens up an interesting possibility to use its foldamers as a strategy for sensor development and other multiple potential applications that rely on the great commercial value of papain-like cysteine proteases.",
publisher = "MDPI",
journal = "Biomimetics",
title = "Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development",
volume = "8",
number = "3",
pages = "281",
doi = "10.3390/biomimetics8030281"
}

Marković, S., Andrejević, N. S., Milošević, J.,& Polović, N.. (2023). Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development. in Biomimetics
MDPI., 8(3), 281.
https://doi.org/10.3390/biomimetics8030281

Marković S, Andrejević NS, Milošević J, Polović N. Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development. in Biomimetics. 2023;8(3):281.
doi:10.3390/biomimetics8030281 .

Marković, Srdjan, Andrejević, Natalija S., Milošević, Jelica, Polović, Natalija, "Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development" in Biomimetics, 8, no. 3 (2023):281,
https://doi.org/10.3390/biomimetics8030281 . .

TY  - JOUR
AU  - Mijin, Nemanja D.
AU  - Milošević, Jelica
AU  - Filipović, Nenad R.
AU  - Mitić, Dragana
AU  - Anđelković, Katarina K.
AU  - Polović, Natalija
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5686
AB  - Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancer
cell lines were investigated. However, the results of the cytotoxic activity did
not correlate with the hydrophobic character of the complexes. To gain further
insight into the structure–activity relationship, essential for the design of novel
potential drugs, other factors, such as non-specific interactions with cellular
proteins, have to be taken into account. To explore the potential non-specific
influence of the complexes on protein structures, ovalbumin (OVA) was
chosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold.
Contrary, the effect of complex 5 on OVA secondary structures was concentration-dependent. While the lower concentration of complex 5 had no effect
on OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water may
be related to a potential crosslinking that leads to OVA aggregation.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure
VL  - 87
IS  - 10
SP  - 1143
SP  - 1156
DO  - 10.2298/JSC220518050M
ER  - 

@article{
author = "Mijin, Nemanja D. and Milošević, Jelica and Filipović, Nenad R. and Mitić, Dragana and Anđelković, Katarina K. and Polović, Natalija and Todorović, Tamara",
year = "2022",
abstract = "Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancer
cell lines were investigated. However, the results of the cytotoxic activity did
not correlate with the hydrophobic character of the complexes. To gain further
insight into the structure–activity relationship, essential for the design of novel
potential drugs, other factors, such as non-specific interactions with cellular
proteins, have to be taken into account. To explore the potential non-specific
influence of the complexes on protein structures, ovalbumin (OVA) was
chosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold.
Contrary, the effect of complex 5 on OVA secondary structures was concentration-dependent. While the lower concentration of complex 5 had no effect
on OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water may
be related to a potential crosslinking that leads to OVA aggregation.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure",
volume = "87",
number = "10",
pages = "1143-1156",
doi = "10.2298/JSC220518050M"
}

Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K. K., Polović, N.,& Todorović, T.. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 87(10), 1143.
https://doi.org/10.2298/JSC220518050M

Mijin ND, Milošević J, Filipović NR, Mitić D, Anđelković KK, Polović N, Todorović T. The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. in Journal of the Serbian Chemical Society. 2022;87(10):1143.
doi:10.2298/JSC220518050M .

Mijin, Nemanja D., Milošević, Jelica, Filipović, Nenad R., Mitić, Dragana, Anđelković, Katarina K., Polović, Natalija, Todorović, Tamara, "The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure" in Journal of the Serbian Chemical Society, 87, no. 10 (2022):1143,
https://doi.org/10.2298/JSC220518050M . .

TY  - DATA
AU  - Mijin, Nemanja D.
AU  - Milošević, Jelica
AU  - Filipović, Nenad R.
AU  - Mitić, Dragana
AU  - Anđelković, Katarina K.
AU  - Polović, Natalija
AU  - Todorović, Tamara
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5707
AB  - Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancercell lines were investigated. However, the results of the cytotoxic activity didnot correlate with the hydrophobic character of the complexes. To gain furtherinsight into the structure–activity relationship, essential for the design of novelpotential drugs, other factors, such as non-specific interactions with cellularproteins, have to be taken into account. To explore the potential non-specificinfluence of the complexes on protein structures, ovalbumin (OVA) waschosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold.Contrary, the effect of complex 5 on OVA secondary structures was concentration-dependent. While the lower concentration of complex 5 had no effecton OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water maybe related to a potential crosslinking that leads to OVA aggregation.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Supplementary material for: Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K., Polović, N. Đ., & Todorović, T. R. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. Journal of the Serbian Chemical Society, 87(10), 1143. https://doi.org/10.2298/JSC220518050M
VL  - 87
IS  - 10
SP  - 1143
SP  - 1156
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5707
ER  - 

@misc{
author = "Mijin, Nemanja D. and Milošević, Jelica and Filipović, Nenad R. and Mitić, Dragana and Anđelković, Katarina K. and Polović, Natalija and Todorović, Tamara",
year = "2022",
abstract = "Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancercell lines were investigated. However, the results of the cytotoxic activity didnot correlate with the hydrophobic character of the complexes. To gain furtherinsight into the structure–activity relationship, essential for the design of novelpotential drugs, other factors, such as non-specific interactions with cellularproteins, have to be taken into account. To explore the potential non-specificinfluence of the complexes on protein structures, ovalbumin (OVA) waschosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold.Contrary, the effect of complex 5 on OVA secondary structures was concentration-dependent. While the lower concentration of complex 5 had no effecton OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water maybe related to a potential crosslinking that leads to OVA aggregation.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Supplementary material for: Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K., Polović, N. Đ., & Todorović, T. R. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. Journal of the Serbian Chemical Society, 87(10), 1143. https://doi.org/10.2298/JSC220518050M",
volume = "87",
number = "10",
pages = "1143-1156",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5707"
}

Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K. K., Polović, N.,& Todorović, T.. (2022). Supplementary material for: Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K., Polović, N. Đ., & Todorović, T. R. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. Journal of the Serbian Chemical Society, 87(10), 1143. https://doi.org/10.2298/JSC220518050M. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 87(10), 1143.
https://hdl.handle.net/21.15107/rcub_cherry_5707

Mijin ND, Milošević J, Filipović NR, Mitić D, Anđelković KK, Polović N, Todorović T. Supplementary material for: Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K., Polović, N. Đ., & Todorović, T. R. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. Journal of the Serbian Chemical Society, 87(10), 1143. https://doi.org/10.2298/JSC220518050M. in Journal of the Serbian Chemical Society. 2022;87(10):1143.
https://hdl.handle.net/21.15107/rcub_cherry_5707 .

Mijin, Nemanja D., Milošević, Jelica, Filipović, Nenad R., Mitić, Dragana, Anđelković, Katarina K., Polović, Natalija, Todorović, Tamara, "Supplementary material for: Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K., Polović, N. Đ., & Todorović, T. R. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. Journal of the Serbian Chemical Society, 87(10), 1143. https://doi.org/10.2298/JSC220518050M" in Journal of the Serbian Chemical Society, 87, no. 10 (2022):1143,
https://hdl.handle.net/21.15107/rcub_cherry_5707 .

TY  - JOUR
AU  - Vrhovac, Lidija
AU  - Šelemetjev, Sonja A.
AU  - Vatić, Saša
AU  - Mitrović, Aleksandar
AU  - Milošević, Jelica
AU  - Lolić, Aleksandar
AU  - Beletić, Anđelo D.
AU  - Polović, Natalija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4295
AB  - Measurement of antithyroglobulin antibodies (TgAb) is an inevitable laboratory tool in the management of thyroid gland diseases. Currently available immunoassays still have limitations underlying the necessity of the introduction of fast, sensitive, and label-free technologies. Our aim was to develop a method for TgAb measurement in human serum based on the quartz crystal microbalance (QCM) technology. We immobilized thyroglobulin on the surface of Attana LNB Carboxyl sensor chip®, prepared standard curve covering the range of 1–50000 kIU/L, and established optimal measurement conditions. The validation included determination of the detection limit (LOD), functional sensitivity, linearity, precision, as well as the comparison with the results of the radioimmunoassay (RIA). The LOD and functional sensitivity were 4.2 kIU/L and 4.7 kIU/L, respectively. The method was linear in the range of 20–10000 kIU/L. The regression equation for comparison with RIA was CQCM = 1.0056 • CRIA – 24.2778, whereby no significant proportional or systematic difference was present. There was a good agreement with RIA in the classification of patients according to the clinical significance of the results. The developed method has advantages over currently available assays in terms of better LOQ, a higher upper limit of linearity, and precision. The characteristics of the developed method unambiguously show that the application of the QCM biosensors offers a highly reliable novel approach for the measurement of TgAb in human serum.
PB  - Elsevier
T2  - Talanta
T1  - Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors
VL  - 223
SP  - 121588
DO  - 10.1016/j.talanta.2020.121588
ER  - 

@article{
author = "Vrhovac, Lidija and Šelemetjev, Sonja A. and Vatić, Saša and Mitrović, Aleksandar and Milošević, Jelica and Lolić, Aleksandar and Beletić, Anđelo D. and Polović, Natalija",
year = "2021",
abstract = "Measurement of antithyroglobulin antibodies (TgAb) is an inevitable laboratory tool in the management of thyroid gland diseases. Currently available immunoassays still have limitations underlying the necessity of the introduction of fast, sensitive, and label-free technologies. Our aim was to develop a method for TgAb measurement in human serum based on the quartz crystal microbalance (QCM) technology. We immobilized thyroglobulin on the surface of Attana LNB Carboxyl sensor chip®, prepared standard curve covering the range of 1–50000 kIU/L, and established optimal measurement conditions. The validation included determination of the detection limit (LOD), functional sensitivity, linearity, precision, as well as the comparison with the results of the radioimmunoassay (RIA). The LOD and functional sensitivity were 4.2 kIU/L and 4.7 kIU/L, respectively. The method was linear in the range of 20–10000 kIU/L. The regression equation for comparison with RIA was CQCM = 1.0056 • CRIA – 24.2778, whereby no significant proportional or systematic difference was present. There was a good agreement with RIA in the classification of patients according to the clinical significance of the results. The developed method has advantages over currently available assays in terms of better LOQ, a higher upper limit of linearity, and precision. The characteristics of the developed method unambiguously show that the application of the QCM biosensors offers a highly reliable novel approach for the measurement of TgAb in human serum.",
publisher = "Elsevier",
journal = "Talanta",
title = "Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors",
volume = "223",
pages = "121588",
doi = "10.1016/j.talanta.2020.121588"
}

Vrhovac, L., Šelemetjev, S. A., Vatić, S., Mitrović, A., Milošević, J., Lolić, A., Beletić, A. D.,& Polović, N.. (2021). Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors. in Talanta
Elsevier., 223, 121588.
https://doi.org/10.1016/j.talanta.2020.121588

Vrhovac L, Šelemetjev SA, Vatić S, Mitrović A, Milošević J, Lolić A, Beletić AD, Polović N. Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors. in Talanta. 2021;223:121588.
doi:10.1016/j.talanta.2020.121588 .

Vrhovac, Lidija, Šelemetjev, Sonja A., Vatić, Saša, Mitrović, Aleksandar, Milošević, Jelica, Lolić, Aleksandar, Beletić, Anđelo D., Polović, Natalija, "Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors" in Talanta, 223 (2021):121588,
https://doi.org/10.1016/j.talanta.2020.121588 . .

TY  - JOUR
AU  - Marković, Srđan
AU  - Milošević, Jelica
AU  - Đurić, Milica
AU  - Lolić, Aleksandar
AU  - Polović, Natalija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4479
AB  - Papain is a proteolytic enzyme of great commercial value. It is a cysteine protease highly expressed in Carica papaya fruit latex, but also present in papaya leaves. Purification procedures mostly deal with the latex and include a combination of precipitation and/or chromatographic techniques. Due to its solubility, structure and activity characteristics, the pH and salt content play significant roles in handling papain extracts. Here we report a simple, rapid and easily scalable procedure for papain purification from papaya leaves, which contain different contaminants as compared to papaya latex. Sodium chloride precipitation of contaminants at pH 5 followed by ammonium sulphate precipitation resulted in the removal of other leaf proteins and protein fragments from papain solution and about a 3-fold purification. The procedure also benefits from the suppression of autoproteolysis and preservation of the native structure, as confirmed by FTIR analysis, and the high recovery of activity of over 80%.
T2  - Archives of Biological Sciences
T1  - One-step purification and freeze stability of papain at acidic pH values
VL  - 73
IS  - 1
SP  - 57
EP  - 64
DO  - 10.2298/ABS201217001M
ER  - 

@article{
author = "Marković, Srđan and Milošević, Jelica and Đurić, Milica and Lolić, Aleksandar and Polović, Natalija",
year = "2021",
abstract = "Papain is a proteolytic enzyme of great commercial value. It is a cysteine protease highly expressed in Carica papaya fruit latex, but also present in papaya leaves. Purification procedures mostly deal with the latex and include a combination of precipitation and/or chromatographic techniques. Due to its solubility, structure and activity characteristics, the pH and salt content play significant roles in handling papain extracts. Here we report a simple, rapid and easily scalable procedure for papain purification from papaya leaves, which contain different contaminants as compared to papaya latex. Sodium chloride precipitation of contaminants at pH 5 followed by ammonium sulphate precipitation resulted in the removal of other leaf proteins and protein fragments from papain solution and about a 3-fold purification. The procedure also benefits from the suppression of autoproteolysis and preservation of the native structure, as confirmed by FTIR analysis, and the high recovery of activity of over 80%.",
journal = "Archives of Biological Sciences",
title = "One-step purification and freeze stability of papain at acidic pH values",
volume = "73",
number = "1",
pages = "57-64",
doi = "10.2298/ABS201217001M"
}

Marković, S., Milošević, J., Đurić, M., Lolić, A.,& Polović, N.. (2021). One-step purification and freeze stability of papain at acidic pH values. in Archives of Biological Sciences, 73(1), 57-64.
https://doi.org/10.2298/ABS201217001M

Marković S, Milošević J, Đurić M, Lolić A, Polović N. One-step purification and freeze stability of papain at acidic pH values. in Archives of Biological Sciences. 2021;73(1):57-64.
doi:10.2298/ABS201217001M .

Marković, Srđan, Milošević, Jelica, Đurić, Milica, Lolić, Aleksandar, Polović, Natalija, "One-step purification and freeze stability of papain at acidic pH values" in Archives of Biological Sciences, 73, no. 1 (2021):57-64,
https://doi.org/10.2298/ABS201217001M . .

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1389172320303996
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4779
AB  - Trypsin is a serine protease with important applications such as protein sequencing and tissue dissociation. Preserving protein structure and its activity during freeze-thawing and prolonging its shelf life is one of the most interesting tasks in biochemistry. In the present study, trypsin cryoprotection was achieved by altering buffer composition. Sodium phosphate buffer at pH 8.0 led to pH shift-induced destabilization of trypsin and formation of a molten globule, followed by significant activity loss (about 70%). Potassium phosphate and ammonium bicarbonate buffers at pH 8.0 were used with up to 90% activity recovery rate after 7 freeze-thaw cycles. The addition of non-ionic surfactants Tween 20 and Tween 80 led to up to 99% activity recovery rate. Amide I region changes, corresponding to specific secondary structures in the Fourier transform infrared (FTIR) spectrum, were modest in the case of Tween 20 and Tween 80. On the other hand, the addition of Triton X-100 led to the destabilization of α-helicoidal segments of trypsin structure after 7 freeze-thaw cycles but also increased protein substrate availability.
PB  - Elsevier
T2  - Journal of Bioscience and Bioengineering
T1  - Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants
VL  - 131
IS  - 3
SP  - 234
EP  - 240
DO  - 10.1016/j.jbiosc.2020.10.010
ER  - 

@article{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2021",
abstract = "Trypsin is a serine protease with important applications such as protein sequencing and tissue dissociation. Preserving protein structure and its activity during freeze-thawing and prolonging its shelf life is one of the most interesting tasks in biochemistry. In the present study, trypsin cryoprotection was achieved by altering buffer composition. Sodium phosphate buffer at pH 8.0 led to pH shift-induced destabilization of trypsin and formation of a molten globule, followed by significant activity loss (about 70%). Potassium phosphate and ammonium bicarbonate buffers at pH 8.0 were used with up to 90% activity recovery rate after 7 freeze-thaw cycles. The addition of non-ionic surfactants Tween 20 and Tween 80 led to up to 99% activity recovery rate. Amide I region changes, corresponding to specific secondary structures in the Fourier transform infrared (FTIR) spectrum, were modest in the case of Tween 20 and Tween 80. On the other hand, the addition of Triton X-100 led to the destabilization of α-helicoidal segments of trypsin structure after 7 freeze-thaw cycles but also increased protein substrate availability.",
publisher = "Elsevier",
journal = "Journal of Bioscience and Bioengineering",
title = "Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants",
volume = "131",
number = "3",
pages = "234-240",
doi = "10.1016/j.jbiosc.2020.10.010"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2021). Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants. in Journal of Bioscience and Bioengineering
Elsevier., 131(3), 234-240.
https://doi.org/10.1016/j.jbiosc.2020.10.010

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants. in Journal of Bioscience and Bioengineering. 2021;131(3):234-240.
doi:10.1016/j.jbiosc.2020.10.010 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants" in Journal of Bioscience and Bioengineering, 131, no. 3 (2021):234-240,
https://doi.org/10.1016/j.jbiosc.2020.10.010 . .

TY  - JOUR
AU  - Milošević, Jelica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4388
UR  - https://www.mdpi.com/1420-3049/26/4/970
AB  - Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis— Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.
PB  - MDPI
T2  - Molecules
T1  - On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy
VL  - 26
IS  - 4
SP  - 970
DO  - 10.3390/molecules26040970
ER  - 

@article{
author = "Milošević, Jelica and Prodanović, Radivoje and Polović, Natalija",
year = "2021",
abstract = "Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis— Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.",
publisher = "MDPI",
journal = "Molecules",
title = "On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy",
volume = "26",
number = "4",
pages = "970",
doi = "10.3390/molecules26040970"
}

Milošević, J., Prodanović, R.,& Polović, N.. (2021). On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. in Molecules
MDPI., 26(4), 970.
https://doi.org/10.3390/molecules26040970

Milošević J, Prodanović R, Polović N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. in Molecules. 2021;26(4):970.
doi:10.3390/molecules26040970 .

Milošević, Jelica, Prodanović, Radivoje, Polović, Natalija, "On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy" in Molecules, 26, no. 4 (2021):970,
https://doi.org/10.3390/molecules26040970 . .

TY  - DATA
AU  - Milošević, Jelica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4391
PB  - MDPI
T2  - Molecules
T1  - Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970
VL  - 26
IS  - 4
SP  - 970
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4391
ER  - 

@misc{
author = "Milošević, Jelica and Prodanović, Radivoje and Polović, Natalija",
year = "2021",
publisher = "MDPI",
journal = "Molecules",
title = "Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970",
volume = "26",
number = "4",
pages = "970",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4391"
}

Milošević, J., Prodanović, R.,& Polović, N.. (2021). Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970. in Molecules
MDPI., 26(4), 970.
https://hdl.handle.net/21.15107/rcub_cherry_4391

Milošević J, Prodanović R, Polović N. Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970. in Molecules. 2021;26(4):970.
https://hdl.handle.net/21.15107/rcub_cherry_4391 .

Milošević, Jelica, Prodanović, Radivoje, Polović, Natalija, "Supplementary data for the article: Milošević, J.; Prodanović, R.; Polović, N. On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy. Molecules, 2021, 26, 4, 970-. https://doi.org/10.3390/molecules26040970" in Molecules, 26, no. 4 (2021):970,
https://hdl.handle.net/21.15107/rcub_cherry_4391 .

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4090
AB  - Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.
PB  - Elsevier
T2  - International Journal of Food Microbiology
T1  - Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes
VL  - 334
SP  - 108851
DO  - 10.1016/j.ijfoodmicro.2020.108851
ER  - 

@article{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2020",
abstract = "Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.",
publisher = "Elsevier",
journal = "International Journal of Food Microbiology",
title = "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes",
volume = "334",
pages = "108851",
doi = "10.1016/j.ijfoodmicro.2020.108851"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2020). Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology
Elsevier., 334, 108851.
https://doi.org/10.1016/j.ijfoodmicro.2020.108851

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology. 2020;334:108851.
doi:10.1016/j.ijfoodmicro.2020.108851 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes" in International Journal of Food Microbiology, 334 (2020):108851,
https://doi.org/10.1016/j.ijfoodmicro.2020.108851 . .

TY  - DATA
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4091
PB  - Elsevier
T2  - International Journal of Food Microbiology
T1  - Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4091
ER  - 

@misc{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2020",
publisher = "Elsevier",
journal = "International Journal of Food Microbiology",
title = "Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4091"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2020). Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851. in International Journal of Food Microbiology
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4091

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851. in International Journal of Food Microbiology. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_4091 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851" in International Journal of Food Microbiology (2020),
https://hdl.handle.net/21.15107/rcub_cherry_4091 .

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip T.
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4265
AB  - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Isolation, identification, and stability of Ficin 1c isoform from fig latex
VL  - 44
IS  - 36
SP  - 15716
EP  - 15723
DO  - 10.1039/D0NJ02938F
ER  - 

@article{
author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex",
volume = "44",
number = "36",
pages = "15716-15723",
doi = "10.1039/D0NJ02938F"
}

Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry
Royal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F

Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .

Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip T.
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4264
AB  - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Isolation, identification, and stability of Ficin 1c isoform from fig latex
VL  - 44
IS  - 36
SP  - 15716
EP  - 15723
DO  - 10.1039/D0NJ02938F
ER  - 

@article{
author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex",
volume = "44",
number = "36",
pages = "15716-15723",
doi = "10.1039/D0NJ02938F"
}

Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry
Royal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F

Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .

Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .

TY  - JOUR
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3884
AB  - Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation
VL  - 229
DO  - 10.1016/j.saa.2019.117882
ER  - 

@article{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
abstract = "Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation",
volume = "229",
doi = "10.1016/j.saa.2019.117882"
}

Milošević, J., Petrić, J., Jovčić, B., Janković, B.,& Polović, N.. (2020). Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Elsevier., 229.
https://doi.org/10.1016/j.saa.2019.117882

Milošević J, Petrić J, Jovčić B, Janković B, Polović N. Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;229.
doi:10.1016/j.saa.2019.117882 .

Milošević, Jelica, Petrić, Jovan, Jovčić, Branko, Janković, Brankica, Polović, Natalija, "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation" in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 229 (2020),
https://doi.org/10.1016/j.saa.2019.117882 . .

TY  - DATA
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3894
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3894
ER  - 

@misc{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3894"
}

Milošević, J., Petrić, J., Jovčić, B., Janković, B.,& Polović, N.. (2020). Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_3894

Milošević J, Petrić J, Jovčić B, Janković B, Polović N. Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_3894 .

Milošević, Jelica, Petrić, Jovan, Jovčić, Branko, Janković, Brankica, Polović, Natalija, "Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882" in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy (2020),
https://hdl.handle.net/21.15107/rcub_cherry_3894 .

TY  - JOUR
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3895
AB  - Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation
VL  - 229
DO  - 10.1016/j.saa.2019.117882
ER  - 

@article{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
abstract = "Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation",
volume = "229",
doi = "10.1016/j.saa.2019.117882"
}

Milošević, J., Petrić, J., Jovčić, B., Janković, B.,& Polović, N.. (2020). Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Elsevier., 229.
https://doi.org/10.1016/j.saa.2019.117882

Milošević J, Petrić J, Jovčić B, Janković B, Polović N. Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;229.
doi:10.1016/j.saa.2019.117882 .

Milošević, Jelica, Petrić, Jovan, Jovčić, Branko, Janković, Brankica, Polović, Natalija, "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation" in Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 229 (2020),
https://doi.org/10.1016/j.saa.2019.117882 . .

TY  - JOUR
AU  - Milošević, Jelica
AU  - Janković, Brankica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3932
AB  - Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.
PB  - Springer
T2  - Amino Acids
T1  - Comparative stability of ficin and papain in acidic conditions and the presence of ethanol
VL  - 51
IS  - 5
SP  - 829
EP  - 838
DO  - 10.1007/s00726-019-02724-3
ER  - 

@article{
author = "Milošević, Jelica and Janković, Brankica and Prodanović, Radivoje and Polović, Natalija",
year = "2019",
abstract = "Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.",
publisher = "Springer",
journal = "Amino Acids",
title = "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol",
volume = "51",
number = "5",
pages = "829-838",
doi = "10.1007/s00726-019-02724-3"
}

Milošević, J., Janković, B., Prodanović, R.,& Polović, N.. (2019). Comparative stability of ficin and papain in acidic conditions and the presence of ethanol. in Amino Acids
Springer., 51(5), 829-838.
https://doi.org/10.1007/s00726-019-02724-3

Milošević J, Janković B, Prodanović R, Polović N. Comparative stability of ficin and papain in acidic conditions and the presence of ethanol. in Amino Acids. 2019;51(5):829-838.
doi:10.1007/s00726-019-02724-3 .

Milošević, Jelica, Janković, Brankica, Prodanović, Radivoje, Polović, Natalija, "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol" in Amino Acids, 51, no. 5 (2019):829-838,
https://doi.org/10.1007/s00726-019-02724-3 . .

TY  - DATA
AU  - Milošević, Jelica
AU  - Janković, Brankica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3933
PB  - Springer
T2  - Amino Acids
T1  - Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3933
ER  - 

@misc{
author = "Milošević, Jelica and Janković, Brankica and Prodanović, Radivoje and Polović, Natalija",
year = "2019",
publisher = "Springer",
journal = "Amino Acids",
title = "Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3933"
}

Milošević, J., Janković, B., Prodanović, R.,& Polović, N.. (2019). Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3. in Amino Acids
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_3933

Milošević J, Janković B, Prodanović R, Polović N. Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3. in Amino Acids. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3933 .

Milošević, Jelica, Janković, Brankica, Prodanović, Radivoje, Polović, Natalija, "Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3" in Amino Acids (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3933 .