TY  - CONF
AU  - Izrael Živković, Lidija
AU  - Živković, Ljiljana S.
AU  - Beškoski, Vladimir
AU  - Gopčević, Kristina
AU  - Radosavljević, Dragoslav
AU  - Karadžić, Ivanka
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11195
AB  - Kinetic measurements can be used to predict the optimum kinetic behaviour of a particular biocatalyst. Based on those predictions, optimisation of biocatalytic reactions, as well as process design to improve productivity and reduce the cost of various processes can be performed.
PB  - RAD Centre, Niš, Serbia
C3  - RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro
T1  - Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent
SP  - 76
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11195
ER  - 

@conference{
author = "Izrael Živković, Lidija and Živković, Ljiljana S. and Beškoski, Vladimir and Gopčević, Kristina and Radosavljević, Dragoslav and Karadžić, Ivanka",
year = "2017",
abstract = "Kinetic measurements can be used to predict the optimum kinetic behaviour of a particular biocatalyst. Based on those predictions, optimisation of biocatalytic reactions, as well as process design to improve productivity and reduce the cost of various processes can be performed.",
publisher = "RAD Centre, Niš, Serbia",
journal = "RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro",
title = "Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent",
pages = "76",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11195"
}

Izrael Živković, L., Živković, L. S., Beškoski, V., Gopčević, K., Radosavljević, D.,& Karadžić, I.. (2017). Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro
RAD Centre, Niš, Serbia., 76.
https://hdl.handle.net/21.15107/rcub_vinar_11195

Izrael Živković L, Živković LS, Beškoski V, Gopčević K, Radosavljević D, Karadžić I. Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent. in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro. 2017;:76.
https://hdl.handle.net/21.15107/rcub_vinar_11195 .

Izrael Živković, Lidija, Živković, Ljiljana S., Beškoski, Vladimir, Gopčević, Kristina, Radosavljević, Dragoslav, Karadžić, Ivanka, "Candida rugosa lipase immobilized onto titania as nanobiocatalyst  in organic solvent" in RAD 2017 : 5th International Conference on Radiation in Various Fields of Research : book of abstracts; June 12-16, 2017; Budva, Montenegro (2017):76,
https://hdl.handle.net/21.15107/rcub_vinar_11195 .

TY  - JOUR
AU  - Rastegari, Ali Asghar
AU  - Buzari, Behnaz
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Petković, Marijana
AU  - Bordbar, Abdol-Khalegh
PY  - 2013
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5664
AB  - The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (C) 2013 Elsevier B.V. All rights reserved.
T2  - Thermochimica Acta
T1  - Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques
VL  - 568
SP  - 165
EP  - 170
DO  - 10.1016/j.tca.2013.06.030
ER  - 

@article{
author = "Rastegari, Ali Asghar and Buzari, Behnaz and Pavelkić, Vesna M. and Gopčević, Kristina and Petković, Marijana and Bordbar, Abdol-Khalegh",
year = "2013",
abstract = "The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (C) 2013 Elsevier B.V. All rights reserved.",
journal = "Thermochimica Acta",
title = "Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques",
volume = "568",
pages = "165-170",
doi = "10.1016/j.tca.2013.06.030"
}

Rastegari, A. A., Buzari, B., Pavelkić, V. M., Gopčević, K., Petković, M.,& Bordbar, A.. (2013). Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques. in Thermochimica Acta, 568, 165-170.
https://doi.org/10.1016/j.tca.2013.06.030

Rastegari AA, Buzari B, Pavelkić VM, Gopčević K, Petković M, Bordbar A. Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques. in Thermochimica Acta. 2013;568:165-170.
doi:10.1016/j.tca.2013.06.030 .

Rastegari, Ali Asghar, Buzari, Behnaz, Pavelkić, Vesna M., Gopčević, Kristina, Petković, Marijana, Bordbar, Abdol-Khalegh, "Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques" in Thermochimica Acta, 568 (2013):165-170,
https://doi.org/10.1016/j.tca.2013.06.030 . .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Antić, K.
AU  - Babić, M.
AU  - Gopčević, Kristina
AU  - Petković, Marijana
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9301
AB  - To obtain detailed information about properties of pepsin in thermal denaturing
conditions, polyacrylamide gel electrophoresis (PAGE) and matrix-assisted laser
desorption-ionization time-of-flight mass spectrometry (MALDI-TOF MS)
experimental data were analyzed. These methods were used to analyze the changes
in the structural properties of pepsin molecule subjected to broad-range
temperature variations, from 25 ºC to 70 ºC, and pH range from 1 to 4.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry
T1  - Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data
VL  - 1
SP  - 397
EP  - 399
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9301
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Antić, K. and Babić, M. and Gopčević, Kristina and Petković, Marijana",
year = "2012",
abstract = "To obtain detailed information about properties of pepsin in thermal denaturing
conditions, polyacrylamide gel electrophoresis (PAGE) and matrix-assisted laser
desorption-ionization time-of-flight mass spectrometry (MALDI-TOF MS)
experimental data were analyzed. These methods were used to analyze the changes
in the structural properties of pepsin molecule subjected to broad-range
temperature variations, from 25 ºC to 70 ºC, and pH range from 1 to 4.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry",
title = "Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data",
volume = "1",
pages = "397-399",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9301"
}

Pavelkić, V. M., Antić, K., Babić, M., Gopčević, K.,& Petković, M.. (2012). Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data. in Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 397-399.
https://hdl.handle.net/21.15107/rcub_vinar_9301

Pavelkić VM, Antić K, Babić M, Gopčević K, Petković M. Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data. in Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry. 2012;1:397-399.
https://hdl.handle.net/21.15107/rcub_vinar_9301 .

Pavelkić, Vesna M., Antić, K., Babić, M., Gopčević, Kristina, Petković, Marijana, "Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data" in Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry, 1 (2012):397-399,
https://hdl.handle.net/21.15107/rcub_vinar_9301 .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Krstić, Danijela Z.
AU  - Ilić, Milan
AU  - Pavelkić, M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9371
AB  - The in vitro effect of Al3+ ions on pepsin activity at pH 2, via kinetic parameters was evaluated. Kinetic study showed that Al3+ ions increase the maximal velocity (Vmax) rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Non-essential activation of pepsin by Al3+ “in vitro”
VL  - 1
SP  - 393
EP  - 395
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9371
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Gopčević, Kristina and Krstić, Danijela Z. and Ilić, Milan and Pavelkić, M.",
year = "2008",
abstract = "The in vitro effect of Al3+ ions on pepsin activity at pH 2, via kinetic parameters was evaluated. Kinetic study showed that Al3+ ions increase the maximal velocity (Vmax) rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Non-essential activation of pepsin by Al3+ “in vitro”",
volume = "1",
pages = "393-395",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9371"
}

Pavelkić, V. M., Gopčević, K., Krstić, D. Z., Ilić, M.,& Pavelkić, M.. (2008). Non-essential activation of pepsin by Al3+ “in vitro”. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 393-395.
https://hdl.handle.net/21.15107/rcub_vinar_9371

Pavelkić VM, Gopčević K, Krstić DZ, Ilić M, Pavelkić M. Non-essential activation of pepsin by Al3+ “in vitro”. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:393-395.
https://hdl.handle.net/21.15107/rcub_vinar_9371 .

Pavelkić, Vesna M., Gopčević, Kristina, Krstić, Danijela Z., Ilić, Milan, Pavelkić, M., "Non-essential activation of pepsin by Al3+ “in vitro”" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):393-395,
https://hdl.handle.net/21.15107/rcub_vinar_9371 .

TY  - JOUR
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Krstić, Danijela Z.
AU  - Ilić Marija A. 
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3566
AB  - The in vitro effect of Al3+ ions in the concentration range 1.710-6M-8.710-3M on pepsin activity at pH 2, via kinetic parameters and its electrophoretic mobility was evaluated. Kinetic study demonstrated the existence of an activation effect of Al3+ at pH 2 on pepsin molecule. Kinetic analysis with respect to concentrations of haemoglobin showed that Al3+ ions increase the maximal velocity (Vmax) and kcat values rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type. The values of the equilibrium constants KS and KmA for dissociation of corresponding complexes were evaluated as 0.9040.083mM and 8.560.51M, respectively. Dissociation constant KA, of activator from enzyme-activator complex calculated via kinetic and direct measurement of Al3+ binding data, as well as activation constant A50, the activator concentration that gives a rate equal to half at a saturating concentration of activator, were found to be 8.820.90M, 8.390.76M, and 8.050.48M respectively. Native PAGE electrophoresis shows the decrease in electrophoretic mobility of pepsin and confirms modification of the electric charge and conformational changes of pepsin caused by bound Al3+ on the pepsin molecule. Al3+ induced conformational changes of pepsin were verified by UV-VIS and IR spectra. Moreover, the absence of conformational changes in the haemoglobin molecule in the presence of Al3+ ions confirms that the obtained activation is a consequence of conformational changes caused only in the pepsin molecule.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - The influence of Al3+ion on porcine pepsin activity in vitro
VL  - 23
IS  - 6
SP  - 1002
EP  - 1010
DO  - 10.1080/14756360701841095
ER  - 

@article{
author = "Pavelkić, Vesna M. and Gopčević, Kristina and Krstić, Danijela Z. and Ilić Marija A. ",
year = "2008",
abstract = "The in vitro effect of Al3+ ions in the concentration range 1.710-6M-8.710-3M on pepsin activity at pH 2, via kinetic parameters and its electrophoretic mobility was evaluated. Kinetic study demonstrated the existence of an activation effect of Al3+ at pH 2 on pepsin molecule. Kinetic analysis with respect to concentrations of haemoglobin showed that Al3+ ions increase the maximal velocity (Vmax) and kcat values rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type. The values of the equilibrium constants KS and KmA for dissociation of corresponding complexes were evaluated as 0.9040.083mM and 8.560.51M, respectively. Dissociation constant KA, of activator from enzyme-activator complex calculated via kinetic and direct measurement of Al3+ binding data, as well as activation constant A50, the activator concentration that gives a rate equal to half at a saturating concentration of activator, were found to be 8.820.90M, 8.390.76M, and 8.050.48M respectively. Native PAGE electrophoresis shows the decrease in electrophoretic mobility of pepsin and confirms modification of the electric charge and conformational changes of pepsin caused by bound Al3+ on the pepsin molecule. Al3+ induced conformational changes of pepsin were verified by UV-VIS and IR spectra. Moreover, the absence of conformational changes in the haemoglobin molecule in the presence of Al3+ ions confirms that the obtained activation is a consequence of conformational changes caused only in the pepsin molecule.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "The influence of Al3+ion on porcine pepsin activity in vitro",
volume = "23",
number = "6",
pages = "1002-1010",
doi = "10.1080/14756360701841095"
}

Pavelkić, V. M., Gopčević, K., Krstić, D. Z.,& Ilić Marija A. . (2008). The influence of Al3+ion on porcine pepsin activity in vitro. in Journal of Enzyme Inhibition and Medicinal Chemistry, 23(6), 1002-1010.
https://doi.org/10.1080/14756360701841095

Pavelkić VM, Gopčević K, Krstić DZ, Ilić Marija A. . The influence of Al3+ion on porcine pepsin activity in vitro. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2008;23(6):1002-1010.
doi:10.1080/14756360701841095 .

Pavelkić, Vesna M., Gopčević, Kristina, Krstić, Danijela Z., Ilić Marija A. , "The influence of Al3+ion on porcine pepsin activity in vitro" in Journal of Enzyme Inhibition and Medicinal Chemistry, 23, no. 6 (2008):1002-1010,
https://doi.org/10.1080/14756360701841095 . .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Stanisavljev, Dragomir R.
AU  - Gopčević, Kristina
AU  - Beljanski, Vladimir
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9358
AB  - Microwave (MW) irradiated bovine serum albumin (BSA) and bromphenol blue (BPB) complex was used as substrate for the assay of pepsin by kinetic method. Decreased reaction velocity under absorbed MW energy and constant temperature was observed.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Effects of microwave treated substrate on pepsin reaction kinetics
VL  - 1
SP  - 166
EP  - 168
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9358
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Stanisavljev, Dragomir R. and Gopčević, Kristina and Beljanski, Vladimir",
year = "2008",
abstract = "Microwave (MW) irradiated bovine serum albumin (BSA) and bromphenol blue (BPB) complex was used as substrate for the assay of pepsin by kinetic method. Decreased reaction velocity under absorbed MW energy and constant temperature was observed.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Effects of microwave treated substrate on pepsin reaction kinetics",
volume = "1",
pages = "166-168",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9358"
}

Pavelkić, V. M., Stanisavljev, D. R., Gopčević, K.,& Beljanski, V.. (2008). Effects of microwave treated substrate on pepsin reaction kinetics. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 166-168.
https://hdl.handle.net/21.15107/rcub_vinar_9358

Pavelkić VM, Stanisavljev DR, Gopčević K, Beljanski V. Effects of microwave treated substrate on pepsin reaction kinetics. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:166-168.
https://hdl.handle.net/21.15107/rcub_vinar_9358 .

Pavelkić, Vesna M., Stanisavljev, Dragomir R., Gopčević, Kristina, Beljanski, Vladimir, "Effects of microwave treated substrate on pepsin reaction kinetics" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):166-168,
https://hdl.handle.net/21.15107/rcub_vinar_9358 .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Krstić, Danijela Z.
AU  - Ilić, Milan
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9426
AB  - The influence of temperature and different concentrations of Al3+ on pepsin electrophoretic mobility was investigated. The increase of Al3+ concentrations causes the decrease the electrophoretic mobility of enzyme. Also the increase of temperature induced the same effect. The influence of both temperature and Al3+ ion concentrations is additive.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
T1  - Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin
SP  - 374
EP  - 376
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9426
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Gopčević, Kristina and Krstić, Danijela Z. and Ilić, Milan",
year = "2006",
abstract = "The influence of temperature and different concentrations of Al3+ on pepsin electrophoretic mobility was investigated. The increase of Al3+ concentrations causes the decrease the electrophoretic mobility of enzyme. Also the increase of temperature induced the same effect. The influence of both temperature and Al3+ ion concentrations is additive.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry",
title = "Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin",
pages = "374-376",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9426"
}

Pavelkić, V. M., Gopčević, K., Krstić, D. Z.,& Ilić, M.. (2006). Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 374-376.
https://hdl.handle.net/21.15107/rcub_vinar_9426

Pavelkić VM, Gopčević K, Krstić DZ, Ilić M. Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry. 2006;:374-376.
https://hdl.handle.net/21.15107/rcub_vinar_9426 .

Pavelkić, Vesna M., Gopčević, Kristina, Krstić, Danijela Z., Ilić, Milan, "Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin" in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry (2006):374-376,
https://hdl.handle.net/21.15107/rcub_vinar_9426 .