Janković, Brankica

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  • Janković, Brankica (7)
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Author's Bibliography

Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation

Milošević, Jelica; Petrić, Jovan; Jovčić, Branko; Janković, Brankica; Polović, Natalija

(Elsevier, 2020)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3884",
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.
Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyElsevier., 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. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;229
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" 229 (2020),
https://doi.org/10.1016/j.saa.2019.117882 .
3
3
2

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

Milošević, Jelica; Petrić, Jovan; Jovčić, Branko; Janković, Brankica; Polović, Natalija

(Elsevier, 2020)

TY  - BOOK
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - http://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
ER  - 
@book{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3894",
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"
}
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.
Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyElsevier..
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. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;
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" (2020)

Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation

Milošević, Jelica; Petrić, Jovan; Jovčić, Branko; Janković, Brankica; Polović, Natalija

(Elsevier, 2020)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3895",
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.
Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyElsevier., 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. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;229
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" 229 (2020),
https://doi.org/10.1016/j.saa.2019.117882 .
3
3
2

Isolation, identification, and stability of Ficin 1c isoform from fig latex

Milošević, Jelica; Vrhovac, Lidija; Đurković, Filip; Janković, Brankica; Malkov, Saša; Lah, Jurij; Polović, Natalija

(Royal Society of Chemistry, 2020)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - http://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 and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4264",
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., Janković, B., Malkov, S., Lah, J.,& Polović, N. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex.
New Journal of ChemistryRoyal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković F, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. New Journal of Chemistry. 2020;44(36):15716-15723
Milošević Jelica, Vrhovac Lidija, Đurković Filip, Janković Brankica, Malkov Saša, Lah Jurij, Polović Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F .
2
1
2

Isolation, identification, and stability of Ficin 1c isoform from fig latex

Milošević, Jelica; Vrhovac, Lidija; Đurković, Filip; Janković, Brankica; Malkov, Saša; Lah, Jurij; Polović, Natalija

(Royal Society of Chemistry, 2020)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - http://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 and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4265",
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., Janković, B., Malkov, S., Lah, J.,& Polović, N. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex.
New Journal of ChemistryRoyal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković F, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. New Journal of Chemistry. 2020;44(36):15716-15723
Milošević Jelica, Vrhovac Lidija, Đurković Filip, Janković Brankica, Malkov Saša, Lah Jurij, Polović Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F .
2
1
2

Comparative stability of ficin and papain in acidic conditions and the presence of ethanol

Milošević, Jelica; Janković, Brankica; Prodanović, Radivoje; Polović, Natalija

(Springer, 2019)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Janković, Brankica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2019
UR  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3932",
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.
Amino AcidsSpringer., 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. Amino Acids. 2019;51(5):829-838
Milošević Jelica, Janković Brankica, Prodanović Radivoje, Polović Natalija, "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol" 51, no. 5 (2019):829-838,
https://doi.org/10.1007/s00726-019-02724-3 .
6
4
7

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

Milošević, Jelica; Janković, Brankica; Prodanović, Radivoje; Polović, Natalija

(Springer, 2019)

TY  - BOOK
AU  - Milošević, Jelica
AU  - Janković, Brankica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2019
UR  - http://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
ER  - 
@book{
author = "Milošević, Jelica and Janković, Brankica and Prodanović, Radivoje and Polović, Natalija",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3933",
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"
}
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.
Amino AcidsSpringer..
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. Amino Acids. 2019;
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" (2019)