TY  - JOUR
AU  - Stefanović, Andrea
AU  - Jovanović, Jelena
AU  - Balanč, Bojana
AU  - Šekuljica, Nataša
AU  - Jakovetić Tanasković, Sonja
AU  - Dojčinović, Marina
AU  - Knežević-Jugović, Zorica
PY  - 2018
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3997
AB  - The objective of this study was to discover the relationship between the ultrasound probe treatment (UPT) on egg white proteins (EWPs) before EWPs hydrolysis by different proteases, and the functional properties of the obtained hydrolysates. To fulfill this goal, the protein solubility, foaming, and emulsifying properties were studied as a function of the UPT time and then related to the surface characteristics and structural properties. The changes in the hydrolysates microstructures and macromolecular conformation, induced by the UPT, were followed using scanning electron microscope analyzis (SEM) and Fourier transforms infrared spectroscopy (FTIR). The results showed that UPT influenced (P  lt  0.05) the proteolysis of egg white proteins for all examined treatment times. Alcalase hydrolysates (AHs) and papain hydrolysates (PHs) were found to have a higher solubility, as a consequence of their relatively higher foaming, and emulsifying properties compared to the untreated hydrolysates. The changes in surface hydrophobicity, sulfhydryl content and surface charge of AHs and PHs indicated unfolding of EWPs affected by ultrasound. SEM analyzis showed that UPT destroyed the microstructures of AHs and PHs, while FTIR spectra indicated remarkable changes in the macromolecular conformation of AHs and PHs after UPT. This study revealed that by combining ultrasound pre-hydrolysis treatment under controlled conditions with thoughtful proteases selection, hydrolysates with improved functional properties could be produced, enhancing utilization of EWPs in food products.
PB  - Oxford Univ Press, Oxford
T2  - Poultry Science
T1  - Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates
EP  - 2229
IS  - 6
SP  - 2218
VL  - 97
DO  - 10.3382/ps/pey055
ER  - 

@article{
author = "Stefanović, Andrea and Jovanović, Jelena and Balanč, Bojana and Šekuljica, Nataša and Jakovetić Tanasković, Sonja and Dojčinović, Marina and Knežević-Jugović, Zorica",
year = "2018",
abstract = "The objective of this study was to discover the relationship between the ultrasound probe treatment (UPT) on egg white proteins (EWPs) before EWPs hydrolysis by different proteases, and the functional properties of the obtained hydrolysates. To fulfill this goal, the protein solubility, foaming, and emulsifying properties were studied as a function of the UPT time and then related to the surface characteristics and structural properties. The changes in the hydrolysates microstructures and macromolecular conformation, induced by the UPT, were followed using scanning electron microscope analyzis (SEM) and Fourier transforms infrared spectroscopy (FTIR). The results showed that UPT influenced (P  lt  0.05) the proteolysis of egg white proteins for all examined treatment times. Alcalase hydrolysates (AHs) and papain hydrolysates (PHs) were found to have a higher solubility, as a consequence of their relatively higher foaming, and emulsifying properties compared to the untreated hydrolysates. The changes in surface hydrophobicity, sulfhydryl content and surface charge of AHs and PHs indicated unfolding of EWPs affected by ultrasound. SEM analyzis showed that UPT destroyed the microstructures of AHs and PHs, while FTIR spectra indicated remarkable changes in the macromolecular conformation of AHs and PHs after UPT. This study revealed that by combining ultrasound pre-hydrolysis treatment under controlled conditions with thoughtful proteases selection, hydrolysates with improved functional properties could be produced, enhancing utilization of EWPs in food products.",
publisher = "Oxford Univ Press, Oxford",
journal = "Poultry Science",
title = "Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates",
pages = "2229-2218",
number = "6",
volume = "97",
doi = "10.3382/ps/pey055"
}

Stefanović, A., Jovanović, J., Balanč, B., Šekuljica, N., Jakovetić Tanasković, S., Dojčinović, M.,& Knežević-Jugović, Z.. (2018). Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates. in Poultry Science
Oxford Univ Press, Oxford., 97(6), 2218-2229.
https://doi.org/10.3382/ps/pey055

Stefanović A, Jovanović J, Balanč B, Šekuljica N, Jakovetić Tanasković S, Dojčinović M, Knežević-Jugović Z. Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates. in Poultry Science. 2018;97(6):2218-2229.
doi:10.3382/ps/pey055 .

Stefanović, Andrea, Jovanović, Jelena, Balanč, Bojana, Šekuljica, Nataša, Jakovetić Tanasković, Sonja, Dojčinović, Marina, Knežević-Jugović, Zorica, "Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates" in Poultry Science, 97, no. 6 (2018):2218-2229,
https://doi.org/10.3382/ps/pey055 . .

TY  - JOUR
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Šekuljica, Nataša
AU  - Jakovetić Tanasković, Sonja
AU  - Dojčinović, Marina
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3309
AB  - The impact of ultrasound waves generated by probe-type sonicator and ultrasound cleaning bath on egg white protein susceptibility to hydrolysis by alcalase compared to both thermal pretreatment and conventional enzymatic hydrolysis was quantitatively investigated. A series of hydrolytic reactions was carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations, and temperatures using untreated, and pretreated egg white proteins (EWPs). The kinetic model based on substrate inhibition and second-order enzyme deactivation successfully predicts the experimental behavior providing an effective tool for comparison and optimization. The ultrasound pretreatments appear to greatly improve the enzymatic hydrolysis of EWPs under different conditions when compare to other methods. The apparent reaction rate constants for proteolysis (k(2)) are 0.009, 0.011, 0.053, and 0.045 min(-1) for untreated EWPs, and those pretreated with heat, probe-type sonicator, and ultrasound cleaning bath technologies, respectively. The ultrasound pretreatment also decreases hydrolysis activation (E-a) and enzyme deactivation (E-d) energy, enthalpy (Delta H), and entropy (Delta S) of activation and for the probe-type sonication this decrease is 61.7%, 61.6%, 63.6%, and 32.2%, respectively, but ultrasound has little change in Gibbs free energy value in the temperature range of 318 to 338 K. The content of sulfhydryl groups and zeta potential show a significant increase (P  lt  0.05) for both applied ultrasound pretreatments and the reduction of particle size distribution are achieved, providing some evidence that the ultrasound causes EWP structural changes affecting the proteolysis rate.
PB  - Wiley, Hoboken
T2  - Journal of Food Science
T1  - Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics
EP  - C2675
IS  - 11
SP  - C2664
VL  - 81
DO  - 10.1111/1750-3841.13503
ER  - 

@article{
author = "Jovanović, Jelena and Stefanović, Andrea and Šekuljica, Nataša and Jakovetić Tanasković, Sonja and Dojčinović, Marina and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2016",
abstract = "The impact of ultrasound waves generated by probe-type sonicator and ultrasound cleaning bath on egg white protein susceptibility to hydrolysis by alcalase compared to both thermal pretreatment and conventional enzymatic hydrolysis was quantitatively investigated. A series of hydrolytic reactions was carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations, and temperatures using untreated, and pretreated egg white proteins (EWPs). The kinetic model based on substrate inhibition and second-order enzyme deactivation successfully predicts the experimental behavior providing an effective tool for comparison and optimization. The ultrasound pretreatments appear to greatly improve the enzymatic hydrolysis of EWPs under different conditions when compare to other methods. The apparent reaction rate constants for proteolysis (k(2)) are 0.009, 0.011, 0.053, and 0.045 min(-1) for untreated EWPs, and those pretreated with heat, probe-type sonicator, and ultrasound cleaning bath technologies, respectively. The ultrasound pretreatment also decreases hydrolysis activation (E-a) and enzyme deactivation (E-d) energy, enthalpy (Delta H), and entropy (Delta S) of activation and for the probe-type sonication this decrease is 61.7%, 61.6%, 63.6%, and 32.2%, respectively, but ultrasound has little change in Gibbs free energy value in the temperature range of 318 to 338 K. The content of sulfhydryl groups and zeta potential show a significant increase (P  lt  0.05) for both applied ultrasound pretreatments and the reduction of particle size distribution are achieved, providing some evidence that the ultrasound causes EWP structural changes affecting the proteolysis rate.",
publisher = "Wiley, Hoboken",
journal = "Journal of Food Science",
title = "Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics",
pages = "C2675-C2664",
number = "11",
volume = "81",
doi = "10.1111/1750-3841.13503"
}

Jovanović, J., Stefanović, A., Šekuljica, N., Jakovetić Tanasković, S., Dojčinović, M., Bugarski, B.,& Knežević-Jugović, Z.. (2016). Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics. in Journal of Food Science
Wiley, Hoboken., 81(11), C2664-C2675.
https://doi.org/10.1111/1750-3841.13503

Jovanović J, Stefanović A, Šekuljica N, Jakovetić Tanasković S, Dojčinović M, Bugarski B, Knežević-Jugović Z. Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics. in Journal of Food Science. 2016;81(11):C2664-C2675.
doi:10.1111/1750-3841.13503 .

Jovanović, Jelena, Stefanović, Andrea, Šekuljica, Nataša, Jakovetić Tanasković, Sonja, Dojčinović, Marina, Bugarski, Branko, Knežević-Jugović, Zorica, "Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics" in Journal of Food Science, 81, no. 11 (2016):C2664-C2675,
https://doi.org/10.1111/1750-3841.13503 . .

TY  - JOUR
AU  - Jakovetić, Sonja
AU  - Luković, Nevena
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Grbavčić, Sanja
AU  - Jovanović, Jelena
AU  - Knežević-Jugović, Zorica
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3008
AB  - The objective of this research was to design an efficient continuously operated membrane reactor with a separation unit for egg white protein (EWP) hydrolysis and production of hydrolysates with improved antioxidant properties. For this purpose, a mechanically stirred tank reactor coupled with the polyethersulfone ultrafiltration module with a molecular weight cutoff of 10 kDa was employed. Several proteolytic enzymes have been tested in order to obtain the best quality of peptide-based formulations intended for human consumption. Among protease from Bacillus licheniformis (Alcalase), protease from Bacillus amyloliquefaciens (Neutrase), and protease from papaya latex (papain), the highest degree of hydrolysis (DH), as well as the best antioxidant properties of obtained hydrolysates, was achieved with Alcalase. The effects of operating variables such as enzyme/substrate ([E]/[S]) ratio, impeller speed, and permeate flow rate were further studied using response surface methodology (RSM) and Box-Behnken experimental design. Results obtained in RSM analysis confirmed that over the studied range [E]/[S] ratio, impeller speed and permeate flow rate had the significant effect on the DH and reactor capacity. The effects of different impeller geometries were also studied and four-bladed propeller stirrer enabled the highest DH. Antioxidant properties were analyzed by the 2,2-diphenyl-1-picrylhydrazyl (DPPH), by the 2,2'-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, and by the linear voltammetry methods. Results show that the use of Alcalase in the membrane reactor system is of potential interest for the EWP hydrolysis and obtaining value-added egg products.
PB  - Springer, New York
T2  - Food and Bioprocess Technology
T1  - Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit
EP  - 300
IS  - 2
SP  - 287
VL  - 8
DO  - 10.1007/s11947-014-1402-y
ER  - 

@article{
author = "Jakovetić, Sonja and Luković, Nevena and Jugović, Branimir and Gvozdenović, Milica and Grbavčić, Sanja and Jovanović, Jelena and Knežević-Jugović, Zorica",
year = "2015",
abstract = "The objective of this research was to design an efficient continuously operated membrane reactor with a separation unit for egg white protein (EWP) hydrolysis and production of hydrolysates with improved antioxidant properties. For this purpose, a mechanically stirred tank reactor coupled with the polyethersulfone ultrafiltration module with a molecular weight cutoff of 10 kDa was employed. Several proteolytic enzymes have been tested in order to obtain the best quality of peptide-based formulations intended for human consumption. Among protease from Bacillus licheniformis (Alcalase), protease from Bacillus amyloliquefaciens (Neutrase), and protease from papaya latex (papain), the highest degree of hydrolysis (DH), as well as the best antioxidant properties of obtained hydrolysates, was achieved with Alcalase. The effects of operating variables such as enzyme/substrate ([E]/[S]) ratio, impeller speed, and permeate flow rate were further studied using response surface methodology (RSM) and Box-Behnken experimental design. Results obtained in RSM analysis confirmed that over the studied range [E]/[S] ratio, impeller speed and permeate flow rate had the significant effect on the DH and reactor capacity. The effects of different impeller geometries were also studied and four-bladed propeller stirrer enabled the highest DH. Antioxidant properties were analyzed by the 2,2-diphenyl-1-picrylhydrazyl (DPPH), by the 2,2'-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, and by the linear voltammetry methods. Results show that the use of Alcalase in the membrane reactor system is of potential interest for the EWP hydrolysis and obtaining value-added egg products.",
publisher = "Springer, New York",
journal = "Food and Bioprocess Technology",
title = "Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit",
pages = "300-287",
number = "2",
volume = "8",
doi = "10.1007/s11947-014-1402-y"
}

Jakovetić, S., Luković, N., Jugović, B., Gvozdenović, M., Grbavčić, S., Jovanović, J.,& Knežević-Jugović, Z.. (2015). Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit. in Food and Bioprocess Technology
Springer, New York., 8(2), 287-300.
https://doi.org/10.1007/s11947-014-1402-y

Jakovetić S, Luković N, Jugović B, Gvozdenović M, Grbavčić S, Jovanović J, Knežević-Jugović Z. Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit. in Food and Bioprocess Technology. 2015;8(2):287-300.
doi:10.1007/s11947-014-1402-y .

Jakovetić, Sonja, Luković, Nevena, Jugović, Branimir, Gvozdenović, Milica, Grbavčić, Sanja, Jovanović, Jelena, Knežević-Jugović, Zorica, "Production of Antioxidant Egg White Hydrolysates in a Continuous Stirred Tank Enzyme Reactor Coupled with Membrane Separation Unit" in Food and Bioprocess Technology, 8, no. 2 (2015):287-300,
https://doi.org/10.1007/s11947-014-1402-y . .

TY  - JOUR
AU  - Jakovetić, Sonja
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Bezbradica, Dejan
AU  - Antov, Mirjana
AU  - Mijin, Dušan
AU  - Knežević-Jugović, Zorica
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2420
AB  - Immobilized lipase from Candida antarctica (Novozyme 435) was tested for the synthesis of various phenolic acid esters (ethyl and n-butyl cinnamate, ethyl p-coumarate and n-butyl p-methoxycinnamate). The second-order kinetic model was used to mathematically describe the reaction kinetics and to compare present processes quantitatively. It was found that the model agreed well with the experimental data. Further, the effect of alcohol type on the esterification of cinnamic acid was investigated. The immobilized lipase showed more ability to catalyze the synthesis of butyl cinnamate. Therefore, the process was optimized for the synthesis of butyl cinnamate as a function of solvent polarity (logP) and amount of biocatalyst. The highest ester yield of 60.7 % was obtained for the highest enzyme concentration tested (3 % w/w), but the productivity was for 34 % lower than the corresponding value obtained for the enzyme concentration of 1 % (w/w). The synthesized esters were purified, identified, and screened for antioxidant activities. Both DPPH assay and cyclic voltammetry measurement have shown that cinnamic acid esters have better antioxidant properties than cinnamic acid itself.
PB  - Springer, New York
T2  - Applied Biochemistry and Biotechnology
T1  - Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica
EP  - 1573
IS  - 7
SP  - 1560
VL  - 170
DO  - 10.1007/s12010-013-0294-z
ER  - 

@article{
author = "Jakovetić, Sonja and Jugović, Branimir and Gvozdenović, Milica and Bezbradica, Dejan and Antov, Mirjana and Mijin, Dušan and Knežević-Jugović, Zorica",
year = "2013",
abstract = "Immobilized lipase from Candida antarctica (Novozyme 435) was tested for the synthesis of various phenolic acid esters (ethyl and n-butyl cinnamate, ethyl p-coumarate and n-butyl p-methoxycinnamate). The second-order kinetic model was used to mathematically describe the reaction kinetics and to compare present processes quantitatively. It was found that the model agreed well with the experimental data. Further, the effect of alcohol type on the esterification of cinnamic acid was investigated. The immobilized lipase showed more ability to catalyze the synthesis of butyl cinnamate. Therefore, the process was optimized for the synthesis of butyl cinnamate as a function of solvent polarity (logP) and amount of biocatalyst. The highest ester yield of 60.7 % was obtained for the highest enzyme concentration tested (3 % w/w), but the productivity was for 34 % lower than the corresponding value obtained for the enzyme concentration of 1 % (w/w). The synthesized esters were purified, identified, and screened for antioxidant activities. Both DPPH assay and cyclic voltammetry measurement have shown that cinnamic acid esters have better antioxidant properties than cinnamic acid itself.",
publisher = "Springer, New York",
journal = "Applied Biochemistry and Biotechnology",
title = "Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica",
pages = "1573-1560",
number = "7",
volume = "170",
doi = "10.1007/s12010-013-0294-z"
}

Jakovetić, S., Jugović, B., Gvozdenović, M., Bezbradica, D., Antov, M., Mijin, D.,& Knežević-Jugović, Z.. (2013). Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica. in Applied Biochemistry and Biotechnology
Springer, New York., 170(7), 1560-1573.
https://doi.org/10.1007/s12010-013-0294-z

Jakovetić S, Jugović B, Gvozdenović M, Bezbradica D, Antov M, Mijin D, Knežević-Jugović Z. Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica. in Applied Biochemistry and Biotechnology. 2013;170(7):1560-1573.
doi:10.1007/s12010-013-0294-z .

Jakovetić, Sonja, Jugović, Branimir, Gvozdenović, Milica, Bezbradica, Dejan, Antov, Mirjana, Mijin, Dušan, Knežević-Jugović, Zorica, "Synthesis of Aliphatic Esters of Cinnamic Acid as Potential Lipophilic Antioxidants Catalyzed by Lipase B from Candida antarctica" in Applied Biochemistry and Biotechnology, 170, no. 7 (2013):1560-1573,
https://doi.org/10.1007/s12010-013-0294-z . .

TY  - JOUR
AU  - Jakovetić, Sonja
AU  - Luković, Nevena
AU  - Bošković-Vragolović, Nevenka
AU  - Bezbradica, Dejan
AU  - Picazo-Espinosa, Rafael
AU  - Knežević-Jugović, Zorica
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2431
AB  - Ethyl cinnamate, an ester known as flavor and fragrance compound, has been synthesized using two immobilized bioreactor systems, batch and fluidized bed bioreactors. The enzyme used for this synthesis is a commercial lipase B preparation, Novozyme 435. Initial kinetic studies were conducted in both employed bioreactor configurations, and kinetic constants were obtained. Several models were tried for fitting of experimental data, but the best fit, for both bioreactors, was obtained when the ping-pong bi-bi mechanism was used. Interestingly enough, ethanol inhibition occurred in batch bioreactor, but it did not exist in the fluidized bed bioreactor. Solid-liquid mass transfer coefficients were calculated for both bioreactors to determine whether mass transfer limitations existed in either of these systems. The calculation of Damkohler numbers and Thiele modulus confirmed that mass transfer limitations had no effect on the overall reaction in both bioreactors.
PB  - Amer Chemical Soc, Washington
T2  - Industrial & Engineering Chemistry Research
T1  - Comparative Study of Batch and Fluidized Bed Bioreactors for Lipase-Catalyzed Ethyl Cinnamate Synthesis
EP  - 16697
IS  - 47
SP  - 16689
VL  - 52
DO  - 10.1021/ie402069c
ER  - 

@article{
author = "Jakovetić, Sonja and Luković, Nevena and Bošković-Vragolović, Nevenka and Bezbradica, Dejan and Picazo-Espinosa, Rafael and Knežević-Jugović, Zorica",
year = "2013",
abstract = "Ethyl cinnamate, an ester known as flavor and fragrance compound, has been synthesized using two immobilized bioreactor systems, batch and fluidized bed bioreactors. The enzyme used for this synthesis is a commercial lipase B preparation, Novozyme 435. Initial kinetic studies were conducted in both employed bioreactor configurations, and kinetic constants were obtained. Several models were tried for fitting of experimental data, but the best fit, for both bioreactors, was obtained when the ping-pong bi-bi mechanism was used. Interestingly enough, ethanol inhibition occurred in batch bioreactor, but it did not exist in the fluidized bed bioreactor. Solid-liquid mass transfer coefficients were calculated for both bioreactors to determine whether mass transfer limitations existed in either of these systems. The calculation of Damkohler numbers and Thiele modulus confirmed that mass transfer limitations had no effect on the overall reaction in both bioreactors.",
publisher = "Amer Chemical Soc, Washington",
journal = "Industrial & Engineering Chemistry Research",
title = "Comparative Study of Batch and Fluidized Bed Bioreactors for Lipase-Catalyzed Ethyl Cinnamate Synthesis",
pages = "16697-16689",
number = "47",
volume = "52",
doi = "10.1021/ie402069c"
}

Jakovetić, S., Luković, N., Bošković-Vragolović, N., Bezbradica, D., Picazo-Espinosa, R.,& Knežević-Jugović, Z.. (2013). Comparative Study of Batch and Fluidized Bed Bioreactors for Lipase-Catalyzed Ethyl Cinnamate Synthesis. in Industrial & Engineering Chemistry Research
Amer Chemical Soc, Washington., 52(47), 16689-16697.
https://doi.org/10.1021/ie402069c

Jakovetić S, Luković N, Bošković-Vragolović N, Bezbradica D, Picazo-Espinosa R, Knežević-Jugović Z. Comparative Study of Batch and Fluidized Bed Bioreactors for Lipase-Catalyzed Ethyl Cinnamate Synthesis. in Industrial & Engineering Chemistry Research. 2013;52(47):16689-16697.
doi:10.1021/ie402069c .

Jakovetić, Sonja, Luković, Nevena, Bošković-Vragolović, Nevenka, Bezbradica, Dejan, Picazo-Espinosa, Rafael, Knežević-Jugović, Zorica, "Comparative Study of Batch and Fluidized Bed Bioreactors for Lipase-Catalyzed Ethyl Cinnamate Synthesis" in Industrial & Engineering Chemistry Research, 52, no. 47 (2013):16689-16697,
https://doi.org/10.1021/ie402069c . .