TY  - JOUR
AU  - Pavelkić, Vesna M.
AU  - Brdarić, Tanja
AU  - Petrović, Marija P.
AU  - Šekularac, Gavrilo M.
AU  - Košević, Milica G.
AU  - Pezo, Lato
AU  - Ilić Marija A. 
PY  - 2015
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/944
AB  - The applicability of Peleg model was investigated for predicting mass transfer kinetics during the osmotic dehydration (OD) process of pears, at different concentrations (40, 60 and 70%, w/w) and temperatures (20, 35 and 50 degrees C) of sucrose solution. Increase in sucrose solution concentration resulted in higher water loss (WL) and solid gain (SG) values through the osmotic treatment period. After 360 min of osmotic treatment of pears, WL ranged from 23.71 to 31.68% at 20 degrees C, from 24.80 to 40.38% at 35 degrees C and from 33.30 to 52.07% at 50 degrees C of initial weight of pears. The increase of dry mass of the samples, SG, after 360 min of osmotic treatment ranged from 3.02 to 6.68% at 20 degrees C, from 4.15 to 7.71% at 35 degrees C and from 5.00 to 8.92% at 50 degrees C. Pelegs rate constants, k(1)(WL) and k(1)(SG), decreased with increasing temperature, as well as decreased with increasing concentration of osmotic solution at constant temperature. Both capacity constants k(2)(WL) and k(2)(SG) also exhibited the inverse relationship between capacity constant and temperature, as well as concentration of the osmotic solution. Pelegs rate constants for WL and SG at all temperatures followed an Arrhenius type relationship. The predicted equilibrium values were very close to experimental ones, which was confirmed with high coefficients of determination and by the residual analysis.
T2  - Chemical Industry and Chemical Engineering Quarterly / CICEQ
T1  - Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution
VL  - 21
IS  - 4
SP  - 485
EP  - 492
DO  - 10.2298/CICEQ141014004P
ER  - 

@article{
author = "Pavelkić, Vesna M. and Brdarić, Tanja and Petrović, Marija P. and Šekularac, Gavrilo M. and Košević, Milica G. and Pezo, Lato and Ilić Marija A. ",
year = "2015",
abstract = "The applicability of Peleg model was investigated for predicting mass transfer kinetics during the osmotic dehydration (OD) process of pears, at different concentrations (40, 60 and 70%, w/w) and temperatures (20, 35 and 50 degrees C) of sucrose solution. Increase in sucrose solution concentration resulted in higher water loss (WL) and solid gain (SG) values through the osmotic treatment period. After 360 min of osmotic treatment of pears, WL ranged from 23.71 to 31.68% at 20 degrees C, from 24.80 to 40.38% at 35 degrees C and from 33.30 to 52.07% at 50 degrees C of initial weight of pears. The increase of dry mass of the samples, SG, after 360 min of osmotic treatment ranged from 3.02 to 6.68% at 20 degrees C, from 4.15 to 7.71% at 35 degrees C and from 5.00 to 8.92% at 50 degrees C. Pelegs rate constants, k(1)(WL) and k(1)(SG), decreased with increasing temperature, as well as decreased with increasing concentration of osmotic solution at constant temperature. Both capacity constants k(2)(WL) and k(2)(SG) also exhibited the inverse relationship between capacity constant and temperature, as well as concentration of the osmotic solution. Pelegs rate constants for WL and SG at all temperatures followed an Arrhenius type relationship. The predicted equilibrium values were very close to experimental ones, which was confirmed with high coefficients of determination and by the residual analysis.",
journal = "Chemical Industry and Chemical Engineering Quarterly / CICEQ",
title = "Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution",
volume = "21",
number = "4",
pages = "485-492",
doi = "10.2298/CICEQ141014004P"
}

Pavelkić, V. M., Brdarić, T., Petrović, M. P., Šekularac, G. M., Košević, M. G., Pezo, L.,& Ilić Marija A. . (2015). Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution. in Chemical Industry and Chemical Engineering Quarterly / CICEQ, 21(4), 485-492.
https://doi.org/10.2298/CICEQ141014004P

Pavelkić VM, Brdarić T, Petrović MP, Šekularac GM, Košević MG, Pezo L, Ilić Marija A. . Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution. in Chemical Industry and Chemical Engineering Quarterly / CICEQ. 2015;21(4):485-492.
doi:10.2298/CICEQ141014004P .

Pavelkić, Vesna M., Brdarić, Tanja, Petrović, Marija P., Šekularac, Gavrilo M., Košević, Milica G., Pezo, Lato, Ilić Marija A. , "Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution" in Chemical Industry and Chemical Engineering Quarterly / CICEQ, 21, no. 4 (2015):485-492,
https://doi.org/10.2298/CICEQ141014004P . .

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 . .