Polović, Natalija

Link to this page

Authority KeyName Variants
orcid::0000-0002-9127-2014
  • Polović, Natalija (66)
Projects
Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
Genes and molecular mechanisms promoting probiotic activity of lactic acid bacteria from Western Balkan Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima
Interactions of natural products, their derivatives and coordination compounds with proteins and nucleic acids Modulation of intracellular energy balance-controlling signalling pathways in therapy of cancer and neuro-immuno-endocrine disorders
Study of structure-function relationships in the plant cell wall and modifications of the wall structure by enzyme engineering Bernard Osher Initiative for Research on Severe Asthma at Karolinska Institutet
Center for Inflammatory Diseases Centre for Allergy Research
CMST COST Action [CM1106] EAACI
Hesselman Foundation Directed synthesis, structure and properties of multifunctional materials
Molecular characterization of bacteria from genera Bacillus and Pseudomonas as potential agents for biological control Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200053 (University of Belgrade, Institute for Multidisciplinary Research)
Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness Razvoj i primena proizvoda na bazi mineralnih sirovina u proizvodnji bezbedne hrane
Karolinska Institutet King Gustaf V 80th Birthday Foundation
Konsul Th C Bergh Foundation Stockholm County Council
Swedish Asthma and Allergy Associations Research Foundation Swedish Cancer and Allergy Foundation
Swedish Heart-Lung Foundation Swedish Research Council
COST [928] Federation of European Microbiological Societies (FEMS)
Development of new and improvement of existing electrochemical, spectroscopic and flow injection (FIA) methods on environmental quality monitoring Molecular characterization of thyroid gland tumors:biological and clinical aspects

Author's Bibliography

Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization

Popović, Nikolina; Stanišić, Marija; Ilić Đurđić, Karla; Prodanović, Olivera; Polović, Natalija; Prodanović, Radivoje

(Elsevier, 2021)

TY  - JOUR
AU  - Popović, Nikolina
AU  - Stanišić, Marija
AU  - Ilić Đurđić, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S235218642100047X
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4493
AB  - Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV–Vis,FTIR, and 1H NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.
PB  - Elsevier
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization
VL  - 22
SP  - 101399
DO  - 10.1016/j.eti.2021.101399
ER  - 
@article{
author = "Popović, Nikolina and Stanišić, Marija and Ilić Đurđić, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
abstract = "Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV–Vis,FTIR, and 1H NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.",
publisher = "Elsevier",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization",
volume = "22",
pages = "101399",
doi = "10.1016/j.eti.2021.101399"
}
Popović, N., Stanišić, M., Ilić Đurđić, K., Prodanović, O., Polović, N.,& Prodanović, R.. (2021). Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. in Environmental Technology & Innovation
Elsevier., 22, 101399.
https://doi.org/10.1016/j.eti.2021.101399
Popović N, Stanišić M, Ilić Đurđić K, Prodanović O, Polović N, Prodanović R. Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization. in Environmental Technology & Innovation. 2021;22:101399.
doi:10.1016/j.eti.2021.101399 .
Popović, Nikolina, Stanišić, Marija, Ilić Đurđić, Karla, Prodanović, Olivera, Polović, Natalija, Prodanović, Radivoje, "Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization" in Environmental Technology & Innovation, 22 (2021):101399,
https://doi.org/10.1016/j.eti.2021.101399 . .
1
1
1

One-step purification and freeze stability of papain at acidic pH values

Marković, Srđan; Milošević, Jelica; Đurić, Milica; Lolić, Aleksandar; Polović, Natalija

(2021)

TY  - JOUR
AU  - Marković, Srđan
AU  - Milošević, Jelica
AU  - Đurić, Milica
AU  - Lolić, Aleksandar
AU  - Polović, Natalija
PY  - 2021
UR  - http://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 . .

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

Milošević, Jelica; Prodanović, Radivoje; Polović, Natalija

(MDPI, 2021)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2021
UR  - http://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
ER  - 
@article{
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"
}
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.
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..
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.

On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy

Milošević, Jelica; Prodanović, Radivoje; Polović, Natalija

(MDPI, 2021)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2021
UR  - http://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 . .
2
2

Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.

Popović, Nikolina; Stanišić, Marija; Ilić Đurđić, Karla; Prodanović, Olivera; Polović, Natalija; Prodanović, Radivoje

(Elsevier, 2021)

TY  - DATA
AU  - Popović, Nikolina
AU  - Stanišić, Marija
AU  - Ilić Đurđić, Karla
AU  - Prodanović, Olivera
AU  - Polović, Natalija
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4493
PB  - Elsevier
T2  - Environmental Technology & Innovation
T2  - Environmental Technology & InnovationEnvironmental Technology & Innovation
T1  - Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.
ER  - 
@misc{
author = "Popović, Nikolina and Stanišić, Marija and Ilić Đurđić, Karla and Prodanović, Olivera and Polović, Natalija and Prodanović, Radivoje",
year = "2021",
publisher = "Elsevier",
journal = "Environmental Technology & Innovation, Environmental Technology & InnovationEnvironmental Technology & Innovation",
title = "Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399."
}
Popović, N., Stanišić, M., Ilić Đurđić, K., Prodanović, O., Polović, N.,& Prodanović, R.. (2021). Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.. in Environmental Technology & Innovation
Elsevier..
Popović N, Stanišić M, Ilić Đurđić K, Prodanović O, Polović N, Prodanović R. Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399.. in Environmental Technology & Innovation. 2021;..
Popović, Nikolina, Stanišić, Marija, Ilić Đurđić, Karla, Prodanović, Olivera, Polović, Natalija, Prodanović, Radivoje, "Supplementary data for the article: Popović, N.; Stanišić, M.; Ilić Đurđić, K.; Prodanović, O.; Polović, N.; Prodanović, R. Dopamine-Modified Pectin for a Streptomyces Cyaneus Laccase Induced Microbeads Formation, Immobilization, and Textile Dyes Decolorization. Environmental Technology & Innovation 2021, 22, 101399. https://doi.org/10.1016/j.eti.2021.101399." in Environmental Technology & Innovation (2021).

Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors

Vrhovac, Lidija; Šelemetjev, Sonja A.; Vatić, Saša; Mitrović, Aleksandar; Milošević, Jelica; Lolić, Aleksandar; Beletić, Anđelo D.; Polović, Natalija

(Elsevier, 2021)

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  - http://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 . .
1
1

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",
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 . .
4
3

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  - DATA
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  - 
@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"
}
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..
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;..
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).

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",
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 . .
4
3

Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes

Vatić, Saša; Mirković, Nemanja; Milošević, Jelica; Jovčić, Branko; Polović, Natalija

(Elsevier, 2020)

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - http://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 . .
3
1
1
2

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

Vatić, Saša; Mirković, Nemanja; Milošević, Jelica; Jovčić, Branko; Polović, Natalija

(Elsevier, 2020)

TY  - DATA
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - http://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
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"
}
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..
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;..
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).

Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity

Malešević, Milka; Stanisavljević, Nemanja S.; Novović, Katarina; Polović, Natalija; Vasiljević, Zorica; Kojić, Milan O.; Jovčić, Branko

(Elsevier, 2020)

TY  - JOUR
AU  - Malešević, Milka
AU  - Stanisavljević, Nemanja S.
AU  - Novović, Katarina
AU  - Polović, Natalija
AU  - Vasiljević, Zorica
AU  - Kojić, Milan O.
AU  - Jovčić, Branko
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4257
AB  - Burkholderia cepacia is well known as the causative agent of infections in humans where often shares niche with other pathogens, like Pseudomonas aeruginosa. Clinical isolate Burkholderia sp. BCC4135 was selected due to its strong quorum quenching (QQ) activity. Whole genome sequencing unveiled this isolate as B. cepacia with unique sequence type ST1485 and a myriad of genes belonging to resistome and virulome. Two QQ lactonases YtnP and Y2-aiiA originated from B. cepacia BCC4135 were cloned, expressed, and functionally characterized. They were active against a broad substrate spectrum of the N-acyl-homoserine lactones (AHLs). The YtnP lactonase was inactive, while Y2-aiiA was active against N-tetradecanoyl-dl-homoserine lactone (C14-HSL) which could imply the difference in their biological roles from the aspect of its quorum sensing (QS) autoregulation and interference with the QS systems of bacteria residing within the same niche. Both YtnP and Y2-aiiA were able to attenuate virulence potential of P. aeruginosa MMA83 clinical isolate declining its biofilm formation and virulence factors production. B. cepacia BCC4135 lactonases interfered with the las, rhl, and even pqs QS circuit of P. aeruginosa MMA83 transcription and the effect of combined enzymes was even more prominent. B. cepacia BCC4135 also employs the CepI/R QS system for governing its own virulence traits and possibly self-regulates the QQ/QS network through the different expression and activity of YtnP and/or Y2-aiiA. Our findings pointed out that BCC4135 lactonases could be exploited as an effective antivirulence drugs against P. aeruginosa and gave us a new insight into B. cepacia QQ/QS machinery.
PB  - Elsevier
T2  - Microbial Pathogenesis
T1  - Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity
VL  - 149
DO  - 10.1016/j.micpath.2020.104561
ER  - 
@article{
author = "Malešević, Milka and Stanisavljević, Nemanja S. and Novović, Katarina and Polović, Natalija and Vasiljević, Zorica and Kojić, Milan O. and Jovčić, Branko",
year = "2020",
abstract = "Burkholderia cepacia is well known as the causative agent of infections in humans where often shares niche with other pathogens, like Pseudomonas aeruginosa. Clinical isolate Burkholderia sp. BCC4135 was selected due to its strong quorum quenching (QQ) activity. Whole genome sequencing unveiled this isolate as B. cepacia with unique sequence type ST1485 and a myriad of genes belonging to resistome and virulome. Two QQ lactonases YtnP and Y2-aiiA originated from B. cepacia BCC4135 were cloned, expressed, and functionally characterized. They were active against a broad substrate spectrum of the N-acyl-homoserine lactones (AHLs). The YtnP lactonase was inactive, while Y2-aiiA was active against N-tetradecanoyl-dl-homoserine lactone (C14-HSL) which could imply the difference in their biological roles from the aspect of its quorum sensing (QS) autoregulation and interference with the QS systems of bacteria residing within the same niche. Both YtnP and Y2-aiiA were able to attenuate virulence potential of P. aeruginosa MMA83 clinical isolate declining its biofilm formation and virulence factors production. B. cepacia BCC4135 lactonases interfered with the las, rhl, and even pqs QS circuit of P. aeruginosa MMA83 transcription and the effect of combined enzymes was even more prominent. B. cepacia BCC4135 also employs the CepI/R QS system for governing its own virulence traits and possibly self-regulates the QQ/QS network through the different expression and activity of YtnP and/or Y2-aiiA. Our findings pointed out that BCC4135 lactonases could be exploited as an effective antivirulence drugs against P. aeruginosa and gave us a new insight into B. cepacia QQ/QS machinery.",
publisher = "Elsevier",
journal = "Microbial Pathogenesis",
title = "Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity",
volume = "149",
doi = "10.1016/j.micpath.2020.104561"
}
Malešević, M., Stanisavljević, N. S., Novović, K., Polović, N., Vasiljević, Z., Kojić, M. O.,& Jovčić, B.. (2020). Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis
Elsevier., 149.
https://doi.org/10.1016/j.micpath.2020.104561
Malešević M, Stanisavljević NS, Novović K, Polović N, Vasiljević Z, Kojić MO, Jovčić B. Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis. 2020;149.
doi:10.1016/j.micpath.2020.104561 .
Malešević, Milka, Stanisavljević, Nemanja S., Novović, Katarina, Polović, Natalija, Vasiljević, Zorica, Kojić, Milan O., Jovčić, Branko, "Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity" in Microbial Pathogenesis, 149 (2020),
https://doi.org/10.1016/j.micpath.2020.104561 . .
1
2
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",
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. in New Journal of Chemistry
Royal 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. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .
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" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .
2
2
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",
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. in New Journal of Chemistry
Royal 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. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .
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" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .
2
2
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",
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 . .
7
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  - DATA
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  - 
@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"
}
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..
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;..
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).

Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation

Spasojević, Dragica; Prokopijević, Miloš; Prodanović, Olivera; Zelenović, Nevena D.; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(The Polymer Society of Korea, 2019)

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Zelenović, Nevena D.
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3732
AB  - Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.
PB  - The Polymer Society of Korea
T2  - Macromolecular Research
T1  - Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation
VL  - 27
IS  - 8
SP  - 764
EP  - 771
DO  - 10.1007/s13233-019-7111-7
ER  - 
@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Zelenović, Nevena D. and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2019",
abstract = "Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.",
publisher = "The Polymer Society of Korea",
journal = "Macromolecular Research",
title = "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation",
volume = "27",
number = "8",
pages = "764-771",
doi = "10.1007/s13233-019-7111-7"
}
Spasojević, D., Prokopijević, M., Prodanović, O., Zelenović, N. D., Polović, N., Radotić, K.,& Prodanović, R.. (2019). Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research
The Polymer Society of Korea., 27(8), 764-771.
https://doi.org/10.1007/s13233-019-7111-7
Spasojević D, Prokopijević M, Prodanović O, Zelenović ND, Polović N, Radotić K, Prodanović R. Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research. 2019;27(8):764-771.
doi:10.1007/s13233-019-7111-7 .
Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Zelenović, Nevena D., Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation" in Macromolecular Research, 27, no. 8 (2019):764-771,
https://doi.org/10.1007/s13233-019-7111-7 . .
3
3

Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501

Vukotić, Goran; Polović, Natalija; Mirković, Nemanja; Jovčić, Branko; Stanisavljević, Nemanja S.; Fira, Đorđe; Kojić, Milan O.

(Frontiers in Microbiology, 2019)

TY  - JOUR
AU  - Vukotić, Goran
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja S.
AU  - Fira, Đorđe
AU  - Kojić, Milan O.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3298
AB  - In our previous study we demonstrated that proteinase PrtP is able to impair bacteriocin LcnB activity, despite being produced by the same organism and encoded by the same plasmid. However, precise mechanism of this action, i.e., the exact cleavage site within LcnB bacteriocin, as well as its effect on antimicrobial activity of the resulting peptide remained vague. Here we further explored the interplay between these two proteins and defined, using mass spectrometry, that this unusual hydrolysis indeed occurs in vivo, between the sixth and seventh amino acid on the N terminus of LcnB. To address whether the cleaved form of LcnB retains any level of activity, both recombinant and chemically synthesized variant of truncated LcnB were engineered and produced, but demonstrated no antimicrobial activity. When LcnB was recombinantly overexpressed and subjected to PrtP digestion, the change in its antimicrobial activity was monitored and the degradation products analyzed with reverse-phase high-pressure liquid chromatography. The results confirmed the inactivity of the truncated LcnB and additionally corroborated the PrtP cleavage site in LcnB bacteriocin. In addition, it was demonstrated that, once truncated, LcnB is not able to bind its receptor and is susceptible to additional hydrolysis. This is the first report on proteolytic inactivation of bacteriocins inside the same bacterial host.
PB  - Frontiers in Microbiology
T2  - Frontiers in Microbiology
T1  - Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501
VL  - 10
IS  - APR
DO  - 10.3389/fmicb.2019.00874
ER  - 
@article{
author = "Vukotić, Goran and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja S. and Fira, Đorđe and Kojić, Milan O.",
year = "2019",
abstract = "In our previous study we demonstrated that proteinase PrtP is able to impair bacteriocin LcnB activity, despite being produced by the same organism and encoded by the same plasmid. However, precise mechanism of this action, i.e., the exact cleavage site within LcnB bacteriocin, as well as its effect on antimicrobial activity of the resulting peptide remained vague. Here we further explored the interplay between these two proteins and defined, using mass spectrometry, that this unusual hydrolysis indeed occurs in vivo, between the sixth and seventh amino acid on the N terminus of LcnB. To address whether the cleaved form of LcnB retains any level of activity, both recombinant and chemically synthesized variant of truncated LcnB were engineered and produced, but demonstrated no antimicrobial activity. When LcnB was recombinantly overexpressed and subjected to PrtP digestion, the change in its antimicrobial activity was monitored and the degradation products analyzed with reverse-phase high-pressure liquid chromatography. The results confirmed the inactivity of the truncated LcnB and additionally corroborated the PrtP cleavage site in LcnB bacteriocin. In addition, it was demonstrated that, once truncated, LcnB is not able to bind its receptor and is susceptible to additional hydrolysis. This is the first report on proteolytic inactivation of bacteriocins inside the same bacterial host.",
publisher = "Frontiers in Microbiology",
journal = "Frontiers in Microbiology",
title = "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501",
volume = "10",
number = "APR",
doi = "10.3389/fmicb.2019.00874"
}
Vukotić, G., Polović, N., Mirković, N., Jovčić, B., Stanisavljević, N. S., Fira, Đ.,& Kojić, M. O.. (2019). Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501. in Frontiers in Microbiology
Frontiers in Microbiology., 10(APR).
https://doi.org/10.3389/fmicb.2019.00874
Vukotić G, Polović N, Mirković N, Jovčić B, Stanisavljević NS, Fira Đ, Kojić MO. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501. in Frontiers in Microbiology. 2019;10(APR).
doi:10.3389/fmicb.2019.00874 .
Vukotić, Goran, Polović, Natalija, Mirković, Nemanja, Jovčić, Branko, Stanisavljević, Nemanja S., Fira, Đorđe, Kojić, Milan O., "Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus lactis subsp. Lactis BGMN1-501" in Frontiers in Microbiology, 10, no. APR (2019),
https://doi.org/10.3389/fmicb.2019.00874 . .
2
2

Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874

Vukotić, Goran; Polović, Natalija; Mirković, Nemanja; Jovčić, Branko; Stanisavljević, Nemanja S.; Fira, Đorđe; Kojić, Milan O.

(Frontiers in Microbiology, 2019)

TY  - DATA
AU  - Vukotić, Goran
AU  - Polović, Natalija
AU  - Mirković, Nemanja
AU  - Jovčić, Branko
AU  - Stanisavljević, Nemanja S.
AU  - Fira, Đorđe
AU  - Kojić, Milan O.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3299
PB  - Frontiers in Microbiology
T2  - Frontiers in Microbiology
T1  - Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874
ER  - 
@misc{
author = "Vukotić, Goran and Polović, Natalija and Mirković, Nemanja and Jovčić, Branko and Stanisavljević, Nemanja S. and Fira, Đorđe and Kojić, Milan O.",
year = "2019",
publisher = "Frontiers in Microbiology",
journal = "Frontiers in Microbiology",
title = "Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874"
}
Vukotić, G., Polović, N., Mirković, N., Jovčić, B., Stanisavljević, N. S., Fira, Đ.,& Kojić, M. O.. (2019). Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874. in Frontiers in Microbiology
Frontiers in Microbiology..
Vukotić G, Polović N, Mirković N, Jovčić B, Stanisavljević NS, Fira Đ, Kojić MO. Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874. in Frontiers in Microbiology. 2019;..
Vukotić, Goran, Polović, Natalija, Mirković, Nemanja, Jovčić, Branko, Stanisavljević, Nemanja S., Fira, Đorđe, Kojić, Milan O., "Supplementary material for the article: Vukotic, G.; Polovic, N.; Mirkovic, N.; Jovcic, B.; Stanisavljevic, N.; Fira, D.; Kojic, M. Lactococcin B Is Inactivated by Intrinsic Proteinase PrtP Digestion in Lactococcus Lactis Subsp. Lactis BGMN1-501. Frontiers in Microbiology 2019, 10 (APR). https://doi.org/10.3389/fmicb.2019.00874" in Frontiers in Microbiology (2019).

Supplementary data for article : Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17

Lozo, Jelena; Mirković, Nemanja; O'Connor, Paula M.; Malešević, Milka; Miljković, Marija; Polović, Natalija; Jovčić, Branko; Cotter, Paul D.; Kojić, Milan O.

(Amer Soc Microbiology, Washington, 2017)

TY  - DATA
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2999
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17
ER  - 
@misc{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17"
}
Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington..
Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17. in Applied and Environmental Microbiology. 2017;..
Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Supplementary data for article :  Lozo, J.; Mirkovic, N.; O’Connor, P. M.; Malesevic, M.; Miljkovic, M.; Polović, N.; Jovcic, B.; Cotter, P. D.; Kojić, M. O. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus Lactis Subsp Lactis Bv. Diacetylactis BGBU1-4. Applied and Environmental Microbiology 2017, 83 (21). https://doi.org/10.1128/AEM.01519-17" in Applied and Environmental Microbiology (2017).

Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x

Prokopijević, Miloš; Prodanović, Olivera; Spasojević, Dragica; Kovačević, Gordana; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(Springer, New York, 2017)

TY  - DATA
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Kovačević, Gordana
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3053
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x
ER  - 
@misc{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Kovačević, Gordana and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2017",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x"
}
Prokopijević, M., Prodanović, O., Spasojević, D., Kovačević, G., Polović, N., Radotić, K.,& Prodanović, R.. (2017). Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x. in Applied Microbiology and Biotechnology
Springer, New York..
Prokopijević M, Prodanović O, Spasojević D, Kovačević G, Polović N, Radotić K, Prodanović R. Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x. in Applied Microbiology and Biotechnology. 2017;..
Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Kovačević, Gordana, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Supplementary data for article: Prokopijevic, M.; Prodanovic, O.; Spasojevic, D.; Kovacevic, G.; Polovic, N.; Radotic, K.; Prodanovic, R. Tyramine-Modified Pectins via Periodate Oxidation for Soybean Hull Peroxidase Induced Hydrogel Formation and Immobilization. Applied Microbiology and Biotechnology 2017, 101 (6), 2281–2290. https://doi.org/10.1007/s00253-016-8002-x" in Applied Microbiology and Biotechnology (2017).

Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4

Lozo, Jelena; Mirković, Nemanja; O'Connor, Paula M.; Malešević, Milka; Miljković, Marija; Polović, Natalija; Jovčić, Branko; Cotter, Paul D.; Kojić, Milan O.

(Amer Soc Microbiology, Washington, 2017)

TY  - JOUR
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2998
AB  - Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4
VL  - 83
IS  - 21
DO  - 10.1128/AEM.01519-17
ER  - 
@article{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
abstract = "Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4",
volume = "83",
number = "21",
doi = "10.1128/AEM.01519-17"
}
Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 83(21).
https://doi.org/10.1128/AEM.01519-17
Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology. 2017;83(21).
doi:10.1128/AEM.01519-17 .
Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4" in Applied and Environmental Microbiology, 83, no. 21 (2017),
https://doi.org/10.1128/AEM.01519-17 . .
10
13
15

Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4

Lozo, Jelena; Mirković, Nemanja; O'Connor, Paula M.; Malešević, Milka; Miljković, Marija; Polović, Natalija; Jovčić, Branko; Cotter, Paul D.; Kojić, Milan O.

(Amer Soc Microbiology, Washington, 2017)

TY  - JOUR
AU  - Lozo, Jelena
AU  - Mirković, Nemanja
AU  - O'Connor, Paula M.
AU  - Malešević, Milka
AU  - Miljković, Marija
AU  - Polović, Natalija
AU  - Jovčić, Branko
AU  - Cotter, Paul D.
AU  - Kojić, Milan O.
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2541
AB  - Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.
PB  - Amer Soc Microbiology, Washington
T2  - Applied and Environmental Microbiology
T1  - Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4
VL  - 83
IS  - 21
DO  - 10.1128/AEM.01519-17
UR  - Kon_3357
ER  - 
@article{
author = "Lozo, Jelena and Mirković, Nemanja and O'Connor, Paula M. and Malešević, Milka and Miljković, Marija and Polović, Natalija and Jovčić, Branko and Cotter, Paul D. and Kojić, Milan O.",
year = "2017",
abstract = "Lactococcus lactis subsp. lactis bv. diacetylactis BGBU1-4 produces a novel bacteriocin, lactolisterin BU, with strong antimicrobial activity against many species of Gram-positive bacteria, including important food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU was extracted from the cell surface of BGBU1-4 by 2-propanol and purified to homogeneity by C18 solid-phase extraction and reversed-phase high-performance liquid chromatography. The molecular mass of the purified lactolisterin BU was 5,160.94 Da, and an internal fragment, AVSWAWQH, as determined by N-terminal sequencing, showed low-level similarity to existing antimicrobial peptides. Curing and transformation experiments revealed the presence of a corresponding bacteriocin operon on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4. Analysis of the bacteriocin operon revealed a leaderless bacteriocin of 43 amino acids that exhibited similarity to bacteriocin BHT-B (63%) from Streptococcus ratti, a bacteriocin with analogy to aureocin A. IMPORTANCE Lactolisterin BU, a broad-spectrum leaderless bacteriocin produced by L. lactis subsp. lactis bv. diacetylactis BGBU1-4, expresses strong antimicrobial activity against food spoilage and foodborne pathogens, such as Listeria monocytogenes, Staphylococcus aureus, Bacillus spp., and streptococci. Lactolisterin BU showed the highest similarity to aureocin-like bacteriocins produced by different bacteria. The operon for synthesis is located on the smallest plasmid, pBU6 (6.2 kb), of strain BGBU1-4, indicating possible horizontal transfer among producers.",
publisher = "Amer Soc Microbiology, Washington",
journal = "Applied and Environmental Microbiology",
title = "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4",
volume = "83",
number = "21",
doi = "10.1128/AEM.01519-17",
url = "Kon_3357"
}
Lozo, J., Mirković, N., O'Connor, P. M., Malešević, M., Miljković, M., Polović, N., Jovčić, B., Cotter, P. D.,& Kojić, M. O.. (2017). Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology
Amer Soc Microbiology, Washington., 83(21).
https://doi.org/10.1128/AEM.01519-17
Kon_3357
Lozo J, Mirković N, O'Connor PM, Malešević M, Miljković M, Polović N, Jovčić B, Cotter PD, Kojić MO. Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4. in Applied and Environmental Microbiology. 2017;83(21).
doi:10.1128/AEM.01519-17
Kon_3357 .
Lozo, Jelena, Mirković, Nemanja, O'Connor, Paula M., Malešević, Milka, Miljković, Marija, Polović, Natalija, Jovčić, Branko, Cotter, Paul D., Kojić, Milan O., "Lactolisterin BU, a Novel Class II Broad-Spectrum Bacteriocin from Lactococcus lactis subsp lactis bv. diacetylactis BGBU1-4" in Applied and Environmental Microbiology, 83, no. 21 (2017),
https://doi.org/10.1128/AEM.01519-17 .,
Kon_3357 .
10
13
15

Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization

Prokopijević, Miloš; Prodanović, Olivera; Spasojević, Dragica; Kovačević, Gordana; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(Springer, New York, 2017)

TY  - JOUR
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Spasojević, Dragica
AU  - Kovačević, Gordana
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2421
AB  - Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 mu mol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K (m) value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization
VL  - 101
IS  - 6
SP  - 2281
EP  - 2290
DO  - 10.1007/s00253-016-8002-x
UR  - Kon_3237
ER  - 
@article{
author = "Prokopijević, Miloš and Prodanović, Olivera and Spasojević, Dragica and Kovačević, Gordana and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2017",
abstract = "Pectin was modified by oxidation with sodium periodate at molar ratios of 2.5, 5, 10, 15 and 20 mol% and reductive amination with tyramine and sodium cyanoborohydride afterwards. Concentration of tyramine groups within modified pectin ranged from 54.5 to 538 mu mol/g of dry pectin while concentration of ionizable groups ranged from 3.0 to 4.0 mmol/g of dry polymer compared to 1.5 mmol/g before modification due to the introduction of amino group. All tyramine-pectins showed exceptional gelling properties and could form hydrogel both by cross-linking of carboxyl groups with calcium or by cross-linking phenol groups with peroxidase in the presence of hydrogen peroxide. These hydrogels were tested as carriers for soybean hull peroxidase (SHP) immobilization within microbeads formed in an emulsion based enzymatic polymerization reaction. SHP immobilized within tyramine-pectin microbeads had an increased thermal and organic solvent stability compared to the soluble enzyme. Immobilized SHP was more active in acidic pH region and had slightly decreased K (m) value of 2.61 mM compared to the soluble enzyme. After 7 cycles of repeated use in batch reactor for pyrogallol oxidation microbeads, immobilized SHP retained half of the initial activity.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization",
volume = "101",
number = "6",
pages = "2281-2290",
doi = "10.1007/s00253-016-8002-x",
url = "Kon_3237"
}
Prokopijević, M., Prodanović, O., Spasojević, D., Kovačević, G., Polović, N., Radotić, K.,& Prodanović, R.. (2017). Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization. in Applied Microbiology and Biotechnology
Springer, New York., 101(6), 2281-2290.
https://doi.org/10.1007/s00253-016-8002-x
Kon_3237
Prokopijević M, Prodanović O, Spasojević D, Kovačević G, Polović N, Radotić K, Prodanović R. Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization. in Applied Microbiology and Biotechnology. 2017;101(6):2281-2290.
doi:10.1007/s00253-016-8002-x
Kon_3237 .
Prokopijević, Miloš, Prodanović, Olivera, Spasojević, Dragica, Kovačević, Gordana, Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Tyramine-modified pectins via periodate oxidation for soybean hull peroxidase induced hydrogel formation and immobilization" in Applied Microbiology and Biotechnology, 101, no. 6 (2017):2281-2290,
https://doi.org/10.1007/s00253-016-8002-x .,
Kon_3237 .
8
7

Characterization of novel collagenolytic proteases

Mucić, G.; Rašković, B.; Polović, Natalija

(Springer Science+Business Media LLC, 2017)

TY  - CHAP
AU  - Mucić, G.
AU  - Rašković, B.
AU  - Polović, Natalija
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/313
AB  - Collagenolytic proteases have many potential applications in different areas of science, industry, and medicine. The determination of the activity of such proteins is paramount to their application. Here, we describe methods which can be applied to determine the activity and some basic characteristics of potential collagenases. © 2017, Springer Science+Business Media LLC.
PB  - Springer Science+Business Media LLC
T2  - Methods in Molecular Biology
T1  - Characterization of novel collagenolytic proteases
VL  - 1626
SP  - 71
EP  - 78
DO  - 10.1007/978-1-4939-7111-4_7
UR  - Kon_1280
ER  - 
@inbook{
author = "Mucić, G. and Rašković, B. and Polović, Natalija",
year = "2017",
abstract = "Collagenolytic proteases have many potential applications in different areas of science, industry, and medicine. The determination of the activity of such proteins is paramount to their application. Here, we describe methods which can be applied to determine the activity and some basic characteristics of potential collagenases. © 2017, Springer Science+Business Media LLC.",
publisher = "Springer Science+Business Media LLC",
journal = "Methods in Molecular Biology",
booktitle = "Characterization of novel collagenolytic proteases",
volume = "1626",
pages = "71-78",
doi = "10.1007/978-1-4939-7111-4_7",
url = "Kon_1280"
}
Mucić, G., Rašković, B.,& Polović, N.. (2017). Characterization of novel collagenolytic proteases. in Methods in Molecular Biology
Springer Science+Business Media LLC., 1626, 71-78.
https://doi.org/10.1007/978-1-4939-7111-4_7
Kon_1280
Mucić G, Rašković B, Polović N. Characterization of novel collagenolytic proteases. in Methods in Molecular Biology. 2017;1626:71-78.
doi:10.1007/978-1-4939-7111-4_7
Kon_1280 .
Mucić, G., Rašković, B., Polović, Natalija, "Characterization of novel collagenolytic proteases" in Methods in Molecular Biology, 1626 (2017):71-78,
https://doi.org/10.1007/978-1-4939-7111-4_7 .,
Kon_1280 .