TY  - DATA
AU  - Rašković, Brankica
AU  - Vatić, Saša
AU  - Anđelković, Boban D.
AU  - Blagojević, Vladimir A.
AU  - Polović, Natalija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3586
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3586
ER  - 

@misc{
author = "Rašković, Brankica and Vatić, Saša and Anđelković, Boban D. and Blagojević, Vladimir A. and Polović, Natalija",
year = "2016",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3586"
}

Rašković, B., Vatić, S., Anđelković, B. D., Blagojević, V. A.,& Polović, N.. (2016). Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018. in Biochemical Engineering Journal
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3586

Rašković B, Vatić S, Anđelković BD, Blagojević VA, Polović N. Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018. in Biochemical Engineering Journal. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3586 .

Rašković, Brankica, Vatić, Saša, Anđelković, Boban D., Blagojević, Vladimir A., Polović, Natalija, "Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018" in Biochemical Engineering Journal (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3586 .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Vatić, Saša
AU  - Anđelković, Boban D.
AU  - Blagojević, Vladimir A.
AU  - Polović, Natalija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2024
AB  - Trypsin is a serine protease with widespread applications, including protein sequencing and typsin mass fingerprinting. In the present study, the storage of trypsin in acidic conditions significantly affected the recovery of activity (40%) after 7 freeze-thaw cycles. Further, trypsin lost parts of its native secondary structure elements, which resulted in a 10% increase in beta-sheet content (band maximum detected at a frequency of 1634 cm in the Fourier transform infrared (FT-IR) spectrum) indicative of freezing-induced denaturation of the protein. The cold storage of trypsin in ammonium bicarbonate (pH 8.2) with the addition of ayoprotectants, such as glycerol or lysine, led to protein stabilization (complete secondary structure content preservation was detected by FT-IR), higher activity recovery ( gt 90%) and modest autolysis ( lt 10%). High activity recovery ( gt 90%) was also detected with the addition of propylene glycol and polyethylene glycol, saccharides and arginine. Nevertheless, trypsin stored at pH 8.2 with the addition of glycerol or lysine was as efficient as untreated trypsin in the trypsin mass fingerprinting analysis of BSA, suggesting that the cold storage of trypsin in slightly alkaline conditions with the addition of cryoprotectants could prolong its shelf life. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life
VL  - 105
SP  - 168
EP  - 176
DO  - 10.1016/j.bej.2015.09.018
ER  - 

@article{
author = "Rašković, Brankica and Vatić, Saša and Anđelković, Boban D. and Blagojević, Vladimir A. and Polović, Natalija",
year = "2016",
abstract = "Trypsin is a serine protease with widespread applications, including protein sequencing and typsin mass fingerprinting. In the present study, the storage of trypsin in acidic conditions significantly affected the recovery of activity (40%) after 7 freeze-thaw cycles. Further, trypsin lost parts of its native secondary structure elements, which resulted in a 10% increase in beta-sheet content (band maximum detected at a frequency of 1634 cm in the Fourier transform infrared (FT-IR) spectrum) indicative of freezing-induced denaturation of the protein. The cold storage of trypsin in ammonium bicarbonate (pH 8.2) with the addition of ayoprotectants, such as glycerol or lysine, led to protein stabilization (complete secondary structure content preservation was detected by FT-IR), higher activity recovery ( gt 90%) and modest autolysis ( lt 10%). High activity recovery ( gt 90%) was also detected with the addition of propylene glycol and polyethylene glycol, saccharides and arginine. Nevertheless, trypsin stored at pH 8.2 with the addition of glycerol or lysine was as efficient as untreated trypsin in the trypsin mass fingerprinting analysis of BSA, suggesting that the cold storage of trypsin in slightly alkaline conditions with the addition of cryoprotectants could prolong its shelf life. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life",
volume = "105",
pages = "168-176",
doi = "10.1016/j.bej.2015.09.018"
}

Rašković, B., Vatić, S., Anđelković, B. D., Blagojević, V. A.,& Polović, N.. (2016). Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life. in Biochemical Engineering Journal
Elsevier Science Bv, Amsterdam., 105, 168-176.
https://doi.org/10.1016/j.bej.2015.09.018

Rašković B, Vatić S, Anđelković BD, Blagojević VA, Polović N. Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life. in Biochemical Engineering Journal. 2016;105:168-176.
doi:10.1016/j.bej.2015.09.018 .

Rašković, Brankica, Vatić, Saša, Anđelković, Boban D., Blagojević, Vladimir A., Polović, Natalija, "Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life" in Biochemical Engineering Journal, 105 (2016):168-176,
https://doi.org/10.1016/j.bej.2015.09.018 . .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Lazić, Jelena O.
AU  - Polović, Natalija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2017
AB  - The physiological role of fig latex is to protect the plant from pathogens. Latex is a rich source of proteases, predominantly ficin. Fig latex also contains collagenolytic protease and chitinolytic enzymes. Our aim was to investigate changes in protein composition, enzyme and antifungal activities of fig latex during fruit ripening. RESULTSComparison of latex samples in different time periods showed a uniform increase of protein concentration in chronological order. The content of collagenolytic protease did not differ significantly in the latex samples, while the content of ficin decreased. Ficin-specific activity towards casein was the highest at the beginning of fruit development (about 80 U mg(-1)). Specific milk clotting activity increased as well as the abundance of casein band in the clots. Specific chitinolytic activity at the beginning of flowering was 6.5 times higher than the activity in the period when fruits are ripe. Antifungal activity is the most extensive in spring. CONCLUSIONFicin forms with different casein specificities are present in different proportions during fruit ripening, which is of importance for applications in the dairy industry. The protection mechanism against insects and fungi, which relies on chitinolytic activity, is the most important in the early phases of flowering and is replaced with other strategies over time. (c) 2015 Society of Chemical Industry
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening
VL  - 96
IS  - 2
SP  - 576
EP  - 582
DO  - 10.1002/jsfa.7126
ER  - 

@article{
author = "Rašković, Brankica and Lazić, Jelena O. and Polović, Natalija",
year = "2016",
abstract = "The physiological role of fig latex is to protect the plant from pathogens. Latex is a rich source of proteases, predominantly ficin. Fig latex also contains collagenolytic protease and chitinolytic enzymes. Our aim was to investigate changes in protein composition, enzyme and antifungal activities of fig latex during fruit ripening. RESULTSComparison of latex samples in different time periods showed a uniform increase of protein concentration in chronological order. The content of collagenolytic protease did not differ significantly in the latex samples, while the content of ficin decreased. Ficin-specific activity towards casein was the highest at the beginning of fruit development (about 80 U mg(-1)). Specific milk clotting activity increased as well as the abundance of casein band in the clots. Specific chitinolytic activity at the beginning of flowering was 6.5 times higher than the activity in the period when fruits are ripe. Antifungal activity is the most extensive in spring. CONCLUSIONFicin forms with different casein specificities are present in different proportions during fruit ripening, which is of importance for applications in the dairy industry. The protection mechanism against insects and fungi, which relies on chitinolytic activity, is the most important in the early phases of flowering and is replaced with other strategies over time. (c) 2015 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening",
volume = "96",
number = "2",
pages = "576-582",
doi = "10.1002/jsfa.7126"
}

Rašković, B., Lazić, J. O.,& Polović, N.. (2016). Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Hoboken., 96(2), 576-582.
https://doi.org/10.1002/jsfa.7126

Rašković B, Lazić JO, Polović N. Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening. in Journal of the Science of Food and Agriculture. 2016;96(2):576-582.
doi:10.1002/jsfa.7126 .

Rašković, Brankica, Lazić, Jelena O., Polović, Natalija, "Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening" in Journal of the Science of Food and Agriculture, 96, no. 2 (2016):576-582,
https://doi.org/10.1002/jsfa.7126 . .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Polović, Natalija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3413
AB  - Ficus carica, the common fig has been widely used for centuries for medicine as well as food. Fig latex is used for the treatments of cancer, inflammatory diseases, bacterial and gastrointestinal nematode infections, warts and skin diseases. The aim of the study was to investigate if some of the fig latex applications could be attributed to collagenase activity. The usage of figs in the Western Balkans indicated that the latex of unripe fruits is often used for treatments that could involve remodeling of connective tissue. Collagenase activity in fig latices collected in spring was twice as high as the one detected in summer. Collagenase improved diffusion of low-molecular-weight model molecule through the gelatin hydrogel. Fig latex collagenase was stable during boiling and in the simulated gastric conditions for up to 1 h. The presence of fig latex collagenase in traditional medicine preparations could increase treatment efficacy by hydrolyzing collagen present in extracellular matrix and facilitating the penetration of active molecules through the connective tissue. (C) 2016 Elsevier GmbH. All rights reserved.
PB  - Elsevier Gmbh, Urban & Fischer Verlag, Jena
T2  - Journal of Herbal Medicine
T1  - Collegenase activity in fig latex could contribute to its efficacy in ethnomedicinal preparations
VL  - 6
IS  - 2
SP  - 73
EP  - 78
DO  - 10.1016/j.hermed.2016.03.002
ER  - 

@article{
author = "Rašković, Brankica and Polović, Natalija",
year = "2016",
abstract = "Ficus carica, the common fig has been widely used for centuries for medicine as well as food. Fig latex is used for the treatments of cancer, inflammatory diseases, bacterial and gastrointestinal nematode infections, warts and skin diseases. The aim of the study was to investigate if some of the fig latex applications could be attributed to collagenase activity. The usage of figs in the Western Balkans indicated that the latex of unripe fruits is often used for treatments that could involve remodeling of connective tissue. Collagenase activity in fig latices collected in spring was twice as high as the one detected in summer. Collagenase improved diffusion of low-molecular-weight model molecule through the gelatin hydrogel. Fig latex collagenase was stable during boiling and in the simulated gastric conditions for up to 1 h. The presence of fig latex collagenase in traditional medicine preparations could increase treatment efficacy by hydrolyzing collagen present in extracellular matrix and facilitating the penetration of active molecules through the connective tissue. (C) 2016 Elsevier GmbH. All rights reserved.",
publisher = "Elsevier Gmbh, Urban & Fischer Verlag, Jena",
journal = "Journal of Herbal Medicine",
title = "Collegenase activity in fig latex could contribute to its efficacy in ethnomedicinal preparations",
volume = "6",
number = "2",
pages = "73-78",
doi = "10.1016/j.hermed.2016.03.002"
}

Rašković, B.,& Polović, N.. (2016). Collegenase activity in fig latex could contribute to its efficacy in ethnomedicinal preparations. in Journal of Herbal Medicine
Elsevier Gmbh, Urban & Fischer Verlag, Jena., 6(2), 73-78.
https://doi.org/10.1016/j.hermed.2016.03.002

Rašković B, Polović N. Collegenase activity in fig latex could contribute to its efficacy in ethnomedicinal preparations. in Journal of Herbal Medicine. 2016;6(2):73-78.
doi:10.1016/j.hermed.2016.03.002 .

Rašković, Brankica, Polović, Natalija, "Collegenase activity in fig latex could contribute to its efficacy in ethnomedicinal preparations" in Journal of Herbal Medicine, 6, no. 2 (2016):73-78,
https://doi.org/10.1016/j.hermed.2016.03.002 . .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Popović, Milica M.
AU  - Ostojić, Sanja B.
AU  - Anđelković, Boban D.
AU  - Tešević, Vele
AU  - Polović, Natalija
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3367
AB  - Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
T1  - Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage
VL  - 150
SP  - 238
EP  - 246
DO  - 10.1016/j.saa.2015.05.061
ER  - 

@article{
author = "Rašković, Brankica and Popović, Milica M. and Ostojić, Sanja B. and Anđelković, Boban D. and Tešević, Vele and Polović, Natalija",
year = "2015",
abstract = "Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy",
title = "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage",
volume = "150",
pages = "238-246",
doi = "10.1016/j.saa.2015.05.061"
}

Rašković, B., Popović, M. M., Ostojić, S. B., Anđelković, B. D., Tešević, V.,& Polović, N.. (2015). Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage. in Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
Pergamon-Elsevier Science Ltd, Oxford., 150, 238-246.
https://doi.org/10.1016/j.saa.2015.05.061

Rašković B, Popović MM, Ostojić SB, Anđelković BD, Tešević V, Polović N. Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage. in Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy. 2015;150:238-246.
doi:10.1016/j.saa.2015.05.061 .

Rašković, Brankica, Popović, Milica M., Ostojić, Sanja B., Anđelković, Boban D., Tešević, Vele, Polović, Natalija, "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage" in Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy, 150 (2015):238-246,
https://doi.org/10.1016/j.saa.2015.05.061 . .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Popović, Milica M.
AU  - Ostojić, Sanja B.
AU  - Anđelković, Boban D.
AU  - Tešević, Vele
AU  - Polović, Natalija
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1970
AB  - Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
T1  - Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage
VL  - 150
SP  - 238
EP  - 246
DO  - 10.1016/j.saa.2015.05.061
ER  - 

@article{
author = "Rašković, Brankica and Popović, Milica M. and Ostojić, Sanja B. and Anđelković, Boban D. and Tešević, Vele and Polović, Natalija",
year = "2015",
abstract = "Papain is a cysteine protease with wide substrate specificity and many applications. Despite its widespread applications, cold stability of papain has never been studied. Here, we used differential spectroscopy to monitor thermal denaturation process. Papain was the most stabile from 45 degrees C to 60 degrees C with Delta G degrees(321) of 13.9 +/- 0.3 kJ/mol and T-m value of 84 +/- 1 degrees C. After cold storage, papain lost parts of its native secondary structures elements which gave an increase of 40% of intermolecular beta-sheet content (band maximum detected at frequency of 1621 cm(-1) in Fourier transform infrared (FT-IR) spectrum) indicating the presence of secondary structures necessary for aggregation. The presence of protein aggregates after cold storage was also proven by analytical size exclusion chromatography. After six freeze-thaw cycles around 75% of starting enzyme activity of papain was lost due to cold denaturation and aggregation of unfolded protein. Autoproteolysis of papain did not cause significant loss of the protein activity. Upon the cold storage, papain underwent structural rearrangements and aggregation that correspond to other cold denatured proteins, rather than autoproteolysis which could have the commercial importance for the growing polypeptide based industry.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy",
title = "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage",
volume = "150",
pages = "238-246",
doi = "10.1016/j.saa.2015.05.061"
}

Rašković, B., Popović, M. M., Ostojić, S. B., Anđelković, B. D., Tešević, V.,& Polović, N.. (2015). Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage. in Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy
Pergamon-Elsevier Science Ltd, Oxford., 150, 238-246.
https://doi.org/10.1016/j.saa.2015.05.061

Rašković B, Popović MM, Ostojić SB, Anđelković BD, Tešević V, Polović N. Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage. in Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy. 2015;150:238-246.
doi:10.1016/j.saa.2015.05.061 .

Rašković, Brankica, Popović, Milica M., Ostojić, Sanja B., Anđelković, Boban D., Tešević, Vele, Polović, Natalija, "Fourier transform infrared spectroscopy provides an evidence of papain denaturation and aggregation during cold storage" in Spectrochimica Acta. Part A: Molecular and Biomolecular Spectroscopy, 150 (2015):238-246,
https://doi.org/10.1016/j.saa.2015.05.061 . .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Babic, Nikolina
AU  - Korać, Jelena
AU  - Polović, Natalija
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1953
AB  - Papain is a protease that consists of alpha-helical and beta-sheet domains that unfold almost independently. Both, considerable thermal stability and sodium dodecyl sulfate (SDS) resistance of papain have been shown. However, the ability of each domain to unfold upon thermal and SDS denaturation has never been studied. This work shows that fruit papain has slightly higher resistance to thermal inactivation when compared to that of stem papain with a rather high activation energy (E-a) of 223 +/- 16 kJ mol(-1) and a T(m)50 value of 79 +/- 2 degrees C. The SDS resistance of fruit papain was estimated by SDS-PAGE analysis and activity staining. It was noted that, in the presence of SDS the protein remained active, unless heat energy was applied in order to unfold papain. Furthermore, it was proven via Fourier transform infrared spectroscopy (FT-IR) that an alpha-helical domain of fruit papain is more prone to unfolding at elevated temperatures and in the presence of SDS then a beta-sheet rich domain. Thermal denaturation of papain without detergent present led to accelerated formation of aggregation specific intermolecular beta-sheets as compared to native protein. The presented results are of both fundamental and practical importance.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Evidence of beta-sheet structure induced kinetic stability of papain upon thermal and sodium dodecyl sulfate denaturation
VL  - 80
IS  - 5
SP  - 613
EP  - 625
DO  - 10.2298/JSC140901007R
ER  - 

@article{
author = "Rašković, Brankica and Babic, Nikolina and Korać, Jelena and Polović, Natalija",
year = "2015",
abstract = "Papain is a protease that consists of alpha-helical and beta-sheet domains that unfold almost independently. Both, considerable thermal stability and sodium dodecyl sulfate (SDS) resistance of papain have been shown. However, the ability of each domain to unfold upon thermal and SDS denaturation has never been studied. This work shows that fruit papain has slightly higher resistance to thermal inactivation when compared to that of stem papain with a rather high activation energy (E-a) of 223 +/- 16 kJ mol(-1) and a T(m)50 value of 79 +/- 2 degrees C. The SDS resistance of fruit papain was estimated by SDS-PAGE analysis and activity staining. It was noted that, in the presence of SDS the protein remained active, unless heat energy was applied in order to unfold papain. Furthermore, it was proven via Fourier transform infrared spectroscopy (FT-IR) that an alpha-helical domain of fruit papain is more prone to unfolding at elevated temperatures and in the presence of SDS then a beta-sheet rich domain. Thermal denaturation of papain without detergent present led to accelerated formation of aggregation specific intermolecular beta-sheets as compared to native protein. The presented results are of both fundamental and practical importance.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Evidence of beta-sheet structure induced kinetic stability of papain upon thermal and sodium dodecyl sulfate denaturation",
volume = "80",
number = "5",
pages = "613-625",
doi = "10.2298/JSC140901007R"
}

Rašković, B., Babic, N., Korać, J.,& Polović, N.. (2015). Evidence of beta-sheet structure induced kinetic stability of papain upon thermal and sodium dodecyl sulfate denaturation. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 80(5), 613-625.
https://doi.org/10.2298/JSC140901007R

Rašković B, Babic N, Korać J, Polović N. Evidence of beta-sheet structure induced kinetic stability of papain upon thermal and sodium dodecyl sulfate denaturation. in Journal of the Serbian Chemical Society. 2015;80(5):613-625.
doi:10.2298/JSC140901007R .

Rašković, Brankica, Babic, Nikolina, Korać, Jelena, Polović, Natalija, "Evidence of beta-sheet structure induced kinetic stability of papain upon thermal and sodium dodecyl sulfate denaturation" in Journal of the Serbian Chemical Society, 80, no. 5 (2015):613-625,
https://doi.org/10.2298/JSC140901007R . .

TY  - JOUR
AU  - Filipović, Nenad R.
AU  - Polović, Natalija
AU  - Rašković, Brankica
AU  - Misirlić-Denčić, Sonja
AU  - Dulović, Marija
AU  - Savić, Milena
AU  - Nikšić, Miomir
AU  - Mitić, Dragana
AU  - Anđelković, Katarina K.
AU  - Todorović, Tamara
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1787
AB  - New square-planar Pd(II) and Pt(II) complexes with 8-quinolinecarboxaldehyde selenosemicarbazone have been synthesized and characterized by use of elemental analysis, molar conductivity measurements, and IR and NMR spectroscopy. The cytotoxic activity of the ligand, new Pt(II) and Pd(II) compounds, and previously synthesized Pd(II), Pt(II), Cd(II), and Ni(II) complexes with the analogous ligand, 2-quinolinecarboxaldehyde selenosemicarbazone, was tested against two human cancer cell lines: lung carcinoma (H460) and glioma (U251). The potential of these compounds to induce perturbations of the H460 cell cycle was also evaluated. These substances had an excellent radical-scavenging effect against ABTS radical cations. The best antimicrobial activity, among two yeasts and eight bacterial strains tested, was against Bacillus cereus.
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Biological activity of two isomeric N-heteroaromatic selenosemicarbazones and their metal complexes
VL  - 145
IS  - 7
SP  - 1089
EP  - 1099
DO  - 10.1007/s00706-014-1197-6
ER  - 

@article{
author = "Filipović, Nenad R. and Polović, Natalija and Rašković, Brankica and Misirlić-Denčić, Sonja and Dulović, Marija and Savić, Milena and Nikšić, Miomir and Mitić, Dragana and Anđelković, Katarina K. and Todorović, Tamara",
year = "2014",
abstract = "New square-planar Pd(II) and Pt(II) complexes with 8-quinolinecarboxaldehyde selenosemicarbazone have been synthesized and characterized by use of elemental analysis, molar conductivity measurements, and IR and NMR spectroscopy. The cytotoxic activity of the ligand, new Pt(II) and Pd(II) compounds, and previously synthesized Pd(II), Pt(II), Cd(II), and Ni(II) complexes with the analogous ligand, 2-quinolinecarboxaldehyde selenosemicarbazone, was tested against two human cancer cell lines: lung carcinoma (H460) and glioma (U251). The potential of these compounds to induce perturbations of the H460 cell cycle was also evaluated. These substances had an excellent radical-scavenging effect against ABTS radical cations. The best antimicrobial activity, among two yeasts and eight bacterial strains tested, was against Bacillus cereus.",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Biological activity of two isomeric N-heteroaromatic selenosemicarbazones and their metal complexes",
volume = "145",
number = "7",
pages = "1089-1099",
doi = "10.1007/s00706-014-1197-6"
}

Filipović, N. R., Polović, N., Rašković, B., Misirlić-Denčić, S., Dulović, M., Savić, M., Nikšić, M., Mitić, D., Anđelković, K. K.,& Todorović, T.. (2014). Biological activity of two isomeric N-heteroaromatic selenosemicarbazones and their metal complexes. in Monatshefte Fur Chemie
Springer Wien, Wien., 145(7), 1089-1099.
https://doi.org/10.1007/s00706-014-1197-6

Filipović NR, Polović N, Rašković B, Misirlić-Denčić S, Dulović M, Savić M, Nikšić M, Mitić D, Anđelković KK, Todorović T. Biological activity of two isomeric N-heteroaromatic selenosemicarbazones and their metal complexes. in Monatshefte Fur Chemie. 2014;145(7):1089-1099.
doi:10.1007/s00706-014-1197-6 .

Filipović, Nenad R., Polović, Natalija, Rašković, Brankica, Misirlić-Denčić, Sonja, Dulović, Marija, Savić, Milena, Nikšić, Miomir, Mitić, Dragana, Anđelković, Katarina K., Todorović, Tamara, "Biological activity of two isomeric N-heteroaromatic selenosemicarbazones and their metal complexes" in Monatshefte Fur Chemie, 145, no. 7 (2014):1089-1099,
https://doi.org/10.1007/s00706-014-1197-6 . .

TY  - DATA
AU  - Filipović, Nenad R.
AU  - Polović, Natalija
AU  - Rašković, Brankica
AU  - Misirlić-Denčić, Sonja
AU  - Dulović, Marija
AU  - Savić, Milena
AU  - Nikšić, Miomir
AU  - Mitić, Dragana
AU  - Anđelković, Katarina K.
AU  - Todorović, Tamara
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3683
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Supplementary data for the article: Filipović, N.; Polović, N.; Rašković, B.; Misirlić-Denčić, S.; Dulović, M.; Savić, M.; Nikšić, M.; Mitić, D.; Ancrossed D Signelković, K.; Todorović, T. Biological Activity of Two Isomeric N-Heteroaromatic Selenosemicarbazones and Their Metal Complexes. Monatshefte fur Chemie 2014, 145 (7), 1089–1099. https://doi.org/10.1007/s00706-014-1197-6
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3683
ER  - 

@misc{
author = "Filipović, Nenad R. and Polović, Natalija and Rašković, Brankica and Misirlić-Denčić, Sonja and Dulović, Marija and Savić, Milena and Nikšić, Miomir and Mitić, Dragana and Anđelković, Katarina K. and Todorović, Tamara",
year = "2014",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Supplementary data for the article: Filipović, N.; Polović, N.; Rašković, B.; Misirlić-Denčić, S.; Dulović, M.; Savić, M.; Nikšić, M.; Mitić, D.; Ancrossed D Signelković, K.; Todorović, T. Biological Activity of Two Isomeric N-Heteroaromatic Selenosemicarbazones and Their Metal Complexes. Monatshefte fur Chemie 2014, 145 (7), 1089–1099. https://doi.org/10.1007/s00706-014-1197-6",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3683"
}

Filipović, N. R., Polović, N., Rašković, B., Misirlić-Denčić, S., Dulović, M., Savić, M., Nikšić, M., Mitić, D., Anđelković, K. K.,& Todorović, T.. (2014). Supplementary data for the article: Filipović, N.; Polović, N.; Rašković, B.; Misirlić-Denčić, S.; Dulović, M.; Savić, M.; Nikšić, M.; Mitić, D.; Ancrossed D Signelković, K.; Todorović, T. Biological Activity of Two Isomeric N-Heteroaromatic Selenosemicarbazones and Their Metal Complexes. Monatshefte fur Chemie 2014, 145 (7), 1089–1099. https://doi.org/10.1007/s00706-014-1197-6. in Monatshefte Fur Chemie
Springer Wien, Wien..
https://hdl.handle.net/21.15107/rcub_cherry_3683

Filipović NR, Polović N, Rašković B, Misirlić-Denčić S, Dulović M, Savić M, Nikšić M, Mitić D, Anđelković KK, Todorović T. Supplementary data for the article: Filipović, N.; Polović, N.; Rašković, B.; Misirlić-Denčić, S.; Dulović, M.; Savić, M.; Nikšić, M.; Mitić, D.; Ancrossed D Signelković, K.; Todorović, T. Biological Activity of Two Isomeric N-Heteroaromatic Selenosemicarbazones and Their Metal Complexes. Monatshefte fur Chemie 2014, 145 (7), 1089–1099. https://doi.org/10.1007/s00706-014-1197-6. in Monatshefte Fur Chemie. 2014;.
https://hdl.handle.net/21.15107/rcub_cherry_3683 .

Filipović, Nenad R., Polović, Natalija, Rašković, Brankica, Misirlić-Denčić, Sonja, Dulović, Marija, Savić, Milena, Nikšić, Miomir, Mitić, Dragana, Anđelković, Katarina K., Todorović, Tamara, "Supplementary data for the article: Filipović, N.; Polović, N.; Rašković, B.; Misirlić-Denčić, S.; Dulović, M.; Savić, M.; Nikšić, M.; Mitić, D.; Ancrossed D Signelković, K.; Todorović, T. Biological Activity of Two Isomeric N-Heteroaromatic Selenosemicarbazones and Their Metal Complexes. Monatshefte fur Chemie 2014, 145 (7), 1089–1099. https://doi.org/10.1007/s00706-014-1197-6" in Monatshefte Fur Chemie (2014),
https://hdl.handle.net/21.15107/rcub_cherry_3683 .

TY  - JOUR
AU  - Prokopovic, Vladimir
AU  - Popović, Milica M.
AU  - Anđelković, Uroš
AU  - Marsavelski, Aleksandra
AU  - Rašković, Brankica
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1520
AB  - Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Archives of Oral Biology
T1  - Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein
VL  - 59
IS  - 3
SP  - 302
EP  - 309
DO  - 10.1016/j.archoralbio.2013.12.005
ER  - 

@article{
author = "Prokopovic, Vladimir and Popović, Milica M. and Anđelković, Uroš and Marsavelski, Aleksandra and Rašković, Brankica and Gavrović-Jankulović, Marija and Polović, Natalija",
year = "2014",
abstract = "Objective: Human BPIFA2 (parotid secretory protein) is a ubiquitous soluble salivary protein, which belongs to the PLUNC family of proteins. Having sequence similarity to bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein, PLUNC proteins are probably involved in local antibacterial response at mucosal sites, such as oral cavity. The aim of the study was to isolate and characterize human BPIFA2. Design: In this paper, we report one-step affinity chromatography method for BPIFA2 purification from whole human saliva. The isolated BPIFA2 was identified by trypsin mass fingerprinting and characterized by electrophoretic methods. Antibacterial activity of BPIFA2 against model microorganism Pseudomonas aeruginosa was shown in minimum inhibitory concentration and time kill study assays. Results: The protein showed microheterogeneity, both in molecular weight and pI value. BPIFA2 inhibited the growth of P. aeruginosa in microgram concentration range determined by minimum inhibitory concentration assay. In the time kill study, 32 mu g/mL BPIFA2 showed clear bactericidal activity and did not cause any aggregation of bacteria. Conclusion: Affinity chromatography is well suited for isolation of functional BPIFA2 with a potent bactericidal activity against P. aeruginosa. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Archives of Oral Biology",
title = "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein",
volume = "59",
number = "3",
pages = "302-309",
doi = "10.1016/j.archoralbio.2013.12.005"
}

Prokopovic, V., Popović, M. M., Anđelković, U., Marsavelski, A., Rašković, B., Gavrović-Jankulović, M.,& Polović, N.. (2014). Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology
Pergamon-Elsevier Science Ltd, Oxford., 59(3), 302-309.
https://doi.org/10.1016/j.archoralbio.2013.12.005

Prokopovic V, Popović MM, Anđelković U, Marsavelski A, Rašković B, Gavrović-Jankulović M, Polović N. Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein. in Archives of Oral Biology. 2014;59(3):302-309.
doi:10.1016/j.archoralbio.2013.12.005 .

Prokopovic, Vladimir, Popović, Milica M., Anđelković, Uroš, Marsavelski, Aleksandra, Rašković, Brankica, Gavrović-Jankulović, Marija, Polović, Natalija, "Isolation, biochemical characterization and anti-bacterial activity of BPIFA2 protein" in Archives of Oral Biology, 59, no. 3 (2014):302-309,
https://doi.org/10.1016/j.archoralbio.2013.12.005 . .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Bozovic, Olga
AU  - Prodanović, Radivoje
AU  - Niketić, Vesna
AU  - Polović, Natalija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1902
AB  - A novel collagenolytic serine protease was identified and then purified (along with ficin) to apparent homogeneity from the latex of fig (Ficus carica, var. Brown Turkey) by two step chromatographic procedure using gel and covalent chromatography. The enzyme is a monomeric protein of molecular mass of 41 +/- 9 kDa as estimated by analytical gel filtration chromatography. It is an acidic protein with a pI value of approximately 5 and optimal activity at pH 8.0-8.5 and temperature 60 degrees C. The enzymatic activity was strongly inhibited by PMSF and Pefabloc SC, indicating that the enzyme is a serine protease. The enzyme showed specificity towards gelatin and collagen (215 GDU/mg and 24.8 CDU/mg, respectively) and non-specific protease activity (0.18 U/mg against casein). The enzyme was stable and retained full activity over a broad range of pH and temperature. The fig latex collagenolytic protease is potentially useful as a non-microbial enzyme with collagenolytic activity for various applications in the fields of biochemistry, biotechnology and medicine. (C) 2014, The Society for Biotechnology, Japan. All rights reserved.
PB  - Soc Bioscience Bioengineering Japan, Osaka
T2  - Journal of Bioscience and Bioengineering
T1  - Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex
VL  - 118
IS  - 6
SP  - 622
EP  - 627
DO  - 10.1016/j.jbiosc.2014.05.020
ER  - 

@article{
author = "Rašković, Brankica and Bozovic, Olga and Prodanović, Radivoje and Niketić, Vesna and Polović, Natalija",
year = "2014",
abstract = "A novel collagenolytic serine protease was identified and then purified (along with ficin) to apparent homogeneity from the latex of fig (Ficus carica, var. Brown Turkey) by two step chromatographic procedure using gel and covalent chromatography. The enzyme is a monomeric protein of molecular mass of 41 +/- 9 kDa as estimated by analytical gel filtration chromatography. It is an acidic protein with a pI value of approximately 5 and optimal activity at pH 8.0-8.5 and temperature 60 degrees C. The enzymatic activity was strongly inhibited by PMSF and Pefabloc SC, indicating that the enzyme is a serine protease. The enzyme showed specificity towards gelatin and collagen (215 GDU/mg and 24.8 CDU/mg, respectively) and non-specific protease activity (0.18 U/mg against casein). The enzyme was stable and retained full activity over a broad range of pH and temperature. The fig latex collagenolytic protease is potentially useful as a non-microbial enzyme with collagenolytic activity for various applications in the fields of biochemistry, biotechnology and medicine. (C) 2014, The Society for Biotechnology, Japan. All rights reserved.",
publisher = "Soc Bioscience Bioengineering Japan, Osaka",
journal = "Journal of Bioscience and Bioengineering",
title = "Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex",
volume = "118",
number = "6",
pages = "622-627",
doi = "10.1016/j.jbiosc.2014.05.020"
}

Rašković, B., Bozovic, O., Prodanović, R., Niketić, V.,& Polović, N.. (2014). Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex. in Journal of Bioscience and Bioengineering
Soc Bioscience Bioengineering Japan, Osaka., 118(6), 622-627.
https://doi.org/10.1016/j.jbiosc.2014.05.020

Rašković B, Bozovic O, Prodanović R, Niketić V, Polović N. Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex. in Journal of Bioscience and Bioengineering. 2014;118(6):622-627.
doi:10.1016/j.jbiosc.2014.05.020 .

Rašković, Brankica, Bozovic, Olga, Prodanović, Radivoje, Niketić, Vesna, Polović, Natalija, "Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex" in Journal of Bioscience and Bioengineering, 118, no. 6 (2014):622-627,
https://doi.org/10.1016/j.jbiosc.2014.05.020 . .