Savanović, Jova K.

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  • Savanović, Jova K. (1)
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Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor

Damnjanović, Jasmina J.; Žuža, Milena; Savanović, Jova K.; Bezbradica, Dejan; Mijin, Dušan; Bošković-Vragolović, Nevenka; Knežević-Jugović, Zorica

(Elsevier, Amsterdam, 2012)

TY  - JOUR
AU  - Damnjanović, Jasmina J.
AU  - Žuža, Milena
AU  - Savanović, Jova K.
AU  - Bezbradica, Dejan
AU  - Mijin, Dušan
AU  - Bošković-Vragolović, Nevenka
AU  - Knežević-Jugović, Zorica
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2236
AB  - Three commercially available polymers (Sepabeads (R) EC-EP, Sepabeads (R) EC-HA and Purolite (R) A-109) were tested for potential application as supports for covalent immobilization of lipase from Candida rugosa by analyzing some critical properties of immobilized enzymes such as enzyme loading, activity and activity immobilization yield. Among them, lipase covalently immobilized on Sepabeads (R) EC-EP via epoxy groups appeared to show the best performance in a standard hydrolytic reaction. Therefore, it was selected and assayed in the esterification of butyric acid and geraniol to produce geranyl butyrate, first in a batch system followed by continuous geranyl butyrate synthesis in a fluidized bed reactor, as one being potentially applicable for large-scale production. Based on statistical analysis, optimal conditions for the production of geranyl butyrate by selected, immobilized lipase in the batch system are recommended as: temperature at 25-30 degrees C, water concentration at 3.6% (v/v) and acid/alcohol molar ratio at 2.5. A set of optimal conditions for the ester synthesis in a fluidized bed reactor system has also been determined, specifically, flow rate at 10 mL min(-1), temperature at 35 degrees C, water concentration at 2% (v/v), substrate concentration at 0.1 M and acid/alcohol ratio at 2.0. Implementation of the optimized parameters in a batch system and in a fluidized bed reactor enabled production of target ester with high molar conversion, at  gt  99.9% for 48 h in the batch process, and 78.9% for 10 h in fluidized bed reactor. Although when assayed at their optimal conditions, lower molar conversion was achieved in the fluidized bed reactor system compared to the batch system, the volumetric productivity in fluidized bed reactor was more than five fold higher than that obtained in the batch system.
PB  - Elsevier, Amsterdam
T2  - Journal of Molecular Catalysis B-Enzymatic
T1  - Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor
EP  - 59
SP  - 50
VL  - 75
DO  - 10.1016/j.molcatb.2011.11.009
ER  - 
@article{
author = "Damnjanović, Jasmina J. and Žuža, Milena and Savanović, Jova K. and Bezbradica, Dejan and Mijin, Dušan and Bošković-Vragolović, Nevenka and Knežević-Jugović, Zorica",
year = "2012",
abstract = "Three commercially available polymers (Sepabeads (R) EC-EP, Sepabeads (R) EC-HA and Purolite (R) A-109) were tested for potential application as supports for covalent immobilization of lipase from Candida rugosa by analyzing some critical properties of immobilized enzymes such as enzyme loading, activity and activity immobilization yield. Among them, lipase covalently immobilized on Sepabeads (R) EC-EP via epoxy groups appeared to show the best performance in a standard hydrolytic reaction. Therefore, it was selected and assayed in the esterification of butyric acid and geraniol to produce geranyl butyrate, first in a batch system followed by continuous geranyl butyrate synthesis in a fluidized bed reactor, as one being potentially applicable for large-scale production. Based on statistical analysis, optimal conditions for the production of geranyl butyrate by selected, immobilized lipase in the batch system are recommended as: temperature at 25-30 degrees C, water concentration at 3.6% (v/v) and acid/alcohol molar ratio at 2.5. A set of optimal conditions for the ester synthesis in a fluidized bed reactor system has also been determined, specifically, flow rate at 10 mL min(-1), temperature at 35 degrees C, water concentration at 2% (v/v), substrate concentration at 0.1 M and acid/alcohol ratio at 2.0. Implementation of the optimized parameters in a batch system and in a fluidized bed reactor enabled production of target ester with high molar conversion, at  gt  99.9% for 48 h in the batch process, and 78.9% for 10 h in fluidized bed reactor. Although when assayed at their optimal conditions, lower molar conversion was achieved in the fluidized bed reactor system compared to the batch system, the volumetric productivity in fluidized bed reactor was more than five fold higher than that obtained in the batch system.",
publisher = "Elsevier, Amsterdam",
journal = "Journal of Molecular Catalysis B-Enzymatic",
title = "Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor",
pages = "59-50",
volume = "75",
doi = "10.1016/j.molcatb.2011.11.009"
}
Damnjanović, J. J., Žuža, M., Savanović, J. K., Bezbradica, D., Mijin, D., Bošković-Vragolović, N.,& Knežević-Jugović, Z.. (2012). Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor. in Journal of Molecular Catalysis B-Enzymatic
Elsevier, Amsterdam., 75, 50-59.
https://doi.org/10.1016/j.molcatb.2011.11.009
Damnjanović JJ, Žuža M, Savanović JK, Bezbradica D, Mijin D, Bošković-Vragolović N, Knežević-Jugović Z. Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor. in Journal of Molecular Catalysis B-Enzymatic. 2012;75:50-59.
doi:10.1016/j.molcatb.2011.11.009 .
Damnjanović, Jasmina J., Žuža, Milena, Savanović, Jova K., Bezbradica, Dejan, Mijin, Dušan, Bošković-Vragolović, Nevenka, Knežević-Jugović, Zorica, "Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor" in Journal of Molecular Catalysis B-Enzymatic, 75 (2012):50-59,
https://doi.org/10.1016/j.molcatb.2011.11.009 . .
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