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 . .

TY  - CONF
AU  - Jakovetić, Sonja
AU  - Picazo-Espinosa, Rafael
AU  - Manzanera, Maximino
AU  - Stojanović, Željko
AU  - Prodanović, Radivoje
AU  - Miladinović, Ružica
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6096
AB  - Immobilization of lipase B from Candida antarctica was carried out using three different
immobilization methods, and two epoxy activated supports, comercial Eupergit C and
synthesized macroporous copolymer of glycidyl methacrylate (GMA) and ethylene glycol
dimethacrylate (EGDMA). The synthesized polymer was proven to be better for CALB
immobilization at both ionic strenghts that wrere applied, 0.1M and 1.25M. Investigation of
the effect of immobilization pH on the activity of immobilized enzymes, showed that the
highest activities were obtained when immobilization process was conducted in acidic
enviorments. The highest immobilized enzyme activity, 30.5 IU/ g of dry support, was
achieved when periodate method was employed. Glutaraldehyde activation of support did
not improve activity of obtained immobilized enzymes.
T1  - Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment
SP  - 129
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6096
ER  - 

@conference{
author = "Jakovetić, Sonja and Picazo-Espinosa, Rafael and Manzanera, Maximino and Stojanović, Željko and Prodanović, Radivoje and Miladinović, Ružica and Knežević-Jugović, Zorica",
year = "2012",
abstract = "Immobilization of lipase B from Candida antarctica was carried out using three different
immobilization methods, and two epoxy activated supports, comercial Eupergit C and
synthesized macroporous copolymer of glycidyl methacrylate (GMA) and ethylene glycol
dimethacrylate (EGDMA). The synthesized polymer was proven to be better for CALB
immobilization at both ionic strenghts that wrere applied, 0.1M and 1.25M. Investigation of
the effect of immobilization pH on the activity of immobilized enzymes, showed that the
highest activities were obtained when immobilization process was conducted in acidic
enviorments. The highest immobilized enzyme activity, 30.5 IU/ g of dry support, was
achieved when periodate method was employed. Glutaraldehyde activation of support did
not improve activity of obtained immobilized enzymes.",
title = "Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment",
pages = "129",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6096"
}

Jakovetić, S., Picazo-Espinosa, R., Manzanera, M., Stojanović, Ž., Prodanović, R., Miladinović, R.,& Knežević-Jugović, Z.. (2012). Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment. , 129.
https://hdl.handle.net/21.15107/rcub_technorep_6096

Jakovetić S, Picazo-Espinosa R, Manzanera M, Stojanović Ž, Prodanović R, Miladinović R, Knežević-Jugović Z. Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment. 2012;:129.
https://hdl.handle.net/21.15107/rcub_technorep_6096 .

Jakovetić, Sonja, Picazo-Espinosa, Rafael, Manzanera, Maximino, Stojanović, Željko, Prodanović, Radivoje, Miladinović, Ružica, Knežević-Jugović, Zorica, "Immobilization of Candida antarctica lipase B on supports with epoxy groups via covalent attachment" (2012):129,
https://hdl.handle.net/21.15107/rcub_technorep_6096 .