TY  - JOUR
AU  - Šaponjić, Svetlana V.
AU  - Knežević-Jugović, Zorica
AU  - Bezbradica, Dejan
AU  - Žuža, Milena
AU  - Saied, Omar Ali
AU  - Bošković-Vragolović, Nevenka
AU  - Mijin, Dušan
PY  - 2010
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1691
AB  - Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion ( gt  99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g(-1) dry support and in a relatively short time (24 hrs) at 37 degrees C, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.
PB  - University of Catolica De Valparaiso, Valparaiso
T2  - Electronic Journal of Biotechnology
T1  - Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
IS  - 6
VL  - 13
DO  - 10.2225/vol13-issue6-fulltext-8
ER  - 

@article{
author = "Šaponjić, Svetlana V. and Knežević-Jugović, Zorica and Bezbradica, Dejan and Žuža, Milena and Saied, Omar Ali and Bošković-Vragolović, Nevenka and Mijin, Dušan",
year = "2010",
abstract = "Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion ( gt  99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g(-1) dry support and in a relatively short time (24 hrs) at 37 degrees C, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.",
publisher = "University of Catolica De Valparaiso, Valparaiso",
journal = "Electronic Journal of Biotechnology",
title = "Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study",
number = "6",
volume = "13",
doi = "10.2225/vol13-issue6-fulltext-8"
}

Šaponjić, S. V., Knežević-Jugović, Z., Bezbradica, D., Žuža, M., Saied, O. A., Bošković-Vragolović, N.,& Mijin, D.. (2010). Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study. in Electronic Journal of Biotechnology
University of Catolica De Valparaiso, Valparaiso., 13(6).
https://doi.org/10.2225/vol13-issue6-fulltext-8

Šaponjić SV, Knežević-Jugović Z, Bezbradica D, Žuža M, Saied OA, Bošković-Vragolović N, Mijin D. Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study. in Electronic Journal of Biotechnology. 2010;13(6).
doi:10.2225/vol13-issue6-fulltext-8 .

Šaponjić, Svetlana V., Knežević-Jugović, Zorica, Bezbradica, Dejan, Žuža, Milena, Saied, Omar Ali, Bošković-Vragolović, Nevenka, Mijin, Dušan, "Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study" in Electronic Journal of Biotechnology, 13, no. 6 (2010),
https://doi.org/10.2225/vol13-issue6-fulltext-8 . .

TY  - JOUR
AU  - Ognjanović, Nevena
AU  - Šaponjić, Svetlana V.
AU  - Bezbradica, Dejan
AU  - Knežević, Zorica
PY  - 2008
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1279
AB  - Biodiesel is an alternative fuel for diesel engine that is environmentally acceptable. Conventionally, biodiesel is produced by transesterification of triglycerides and short alcohols in the presence of an acid or an alkaline catalyst. There are several problems associated with this kind of production that can be resolved by using lipase as the biocatalyst. The aim of the present work was to investigate novel acyl acceptors for biodiesel production. 2-Propanol and n-butanol have a less negative effect on lipase stability, and they also improve low temperature properties of the fuel. However, excess alcohol leads to inactivation of the enzyme, and glycerol, a major byproduct, can block the immobilized enzyme, resulting in low enzymatic activity. This problem was solved by using methyl acetate as acyl acceptor. Triacetylglycerol is produced instead of glycerol, and it has no negative effect on the activity of the lipase.
AB  - U ovom radu ispitana je mogućnost primene različitih acil akceptora kao polaznih reaktanata umesto metanola u sintezi biodizela u cilju smanjenja inhibicije enzima, povećanja njegove stabilnosti i mogućnosti značajnog pojednostavljivanja izvođenja procesa. Prvo je ispitana mogućnost korišćenja različitih alkohola: 2-propanol i n-butanol koji imaju manji uticaj na denaturaciju enzima. Osim toga, primenom ovih alkohola dobija se gorivo boljeg kvaliteta, pošto se sa povećanjem broja ugljenikovih atoma povećava oktanski broj, temperatura paljenja, kao i sadržaj toplote. Drugi deo istraživanja bio je orijentisan ka ispitivanju mogućnosti korišćenja metilacetata kao pogodnog nukleofila. Za razliku od alkohola, primenom ovog acil akceptora omogućen je jednostepeni postupak sinteze biodizela, što značajno smanjuje vreme trajanja reakcije, kao i kompleksnost iste. Takođe, primenom metilacetata povećava se stabilnost biokatalizatora, što omogućava višekratnu upotrebu. Naime, u reakciji sa metilacetatom kao nusprodukt se ne stvara glicerol već triacetilglicerol, koji nema negativan efekat na stabilnost lipaze.
PB  - Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Lipase-catalyzed biodiesel synthesis with different acyl acceptors
T1  - Primena novih acil akceptora u procesu enzimski katalizovane sinteze biodizela
EP  - 169
IS  - 39
SP  - 161
DO  - 10.2298/APT0839161O
ER  - 

@article{
author = "Ognjanović, Nevena and Šaponjić, Svetlana V. and Bezbradica, Dejan and Knežević, Zorica",
year = "2008",
abstract = "Biodiesel is an alternative fuel for diesel engine that is environmentally acceptable. Conventionally, biodiesel is produced by transesterification of triglycerides and short alcohols in the presence of an acid or an alkaline catalyst. There are several problems associated with this kind of production that can be resolved by using lipase as the biocatalyst. The aim of the present work was to investigate novel acyl acceptors for biodiesel production. 2-Propanol and n-butanol have a less negative effect on lipase stability, and they also improve low temperature properties of the fuel. However, excess alcohol leads to inactivation of the enzyme, and glycerol, a major byproduct, can block the immobilized enzyme, resulting in low enzymatic activity. This problem was solved by using methyl acetate as acyl acceptor. Triacetylglycerol is produced instead of glycerol, and it has no negative effect on the activity of the lipase., U ovom radu ispitana je mogućnost primene različitih acil akceptora kao polaznih reaktanata umesto metanola u sintezi biodizela u cilju smanjenja inhibicije enzima, povećanja njegove stabilnosti i mogućnosti značajnog pojednostavljivanja izvođenja procesa. Prvo je ispitana mogućnost korišćenja različitih alkohola: 2-propanol i n-butanol koji imaju manji uticaj na denaturaciju enzima. Osim toga, primenom ovih alkohola dobija se gorivo boljeg kvaliteta, pošto se sa povećanjem broja ugljenikovih atoma povećava oktanski broj, temperatura paljenja, kao i sadržaj toplote. Drugi deo istraživanja bio je orijentisan ka ispitivanju mogućnosti korišćenja metilacetata kao pogodnog nukleofila. Za razliku od alkohola, primenom ovog acil akceptora omogućen je jednostepeni postupak sinteze biodizela, što značajno smanjuje vreme trajanja reakcije, kao i kompleksnost iste. Takođe, primenom metilacetata povećava se stabilnost biokatalizatora, što omogućava višekratnu upotrebu. Naime, u reakciji sa metilacetatom kao nusprodukt se ne stvara glicerol već triacetilglicerol, koji nema negativan efekat na stabilnost lipaze.",
publisher = "Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Lipase-catalyzed biodiesel synthesis with different acyl acceptors, Primena novih acil akceptora u procesu enzimski katalizovane sinteze biodizela",
pages = "169-161",
number = "39",
doi = "10.2298/APT0839161O"
}

Ognjanović, N., Šaponjić, S. V., Bezbradica, D.,& Knežević, Z.. (2008). Lipase-catalyzed biodiesel synthesis with different acyl acceptors. in Acta periodica technologica
Faculty of Technology, Novi Sad.(39), 161-169.
https://doi.org/10.2298/APT0839161O

Ognjanović N, Šaponjić SV, Bezbradica D, Knežević Z. Lipase-catalyzed biodiesel synthesis with different acyl acceptors. in Acta periodica technologica. 2008;(39):161-169.
doi:10.2298/APT0839161O .

Ognjanović, Nevena, Šaponjić, Svetlana V., Bezbradica, Dejan, Knežević, Zorica, "Lipase-catalyzed biodiesel synthesis with different acyl acceptors" in Acta periodica technologica, no. 39 (2008):161-169,
https://doi.org/10.2298/APT0839161O . .

TY  - JOUR
AU  - Knežević-Jugović, Zorica
AU  - Šaponjić, Svetlana V.
AU  - Bezbradica, Dejan
AU  - Mijin, Dušan
PY  - 2008
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1280
AB  - The object of the study was to investigate the process conditions relevant for the pentyl octanoate production with the lipase from Candida rugosa immobilized on Sepabeads EC-EP carrier. This is an epoxide-containing commercial polymethacrylic carrier with suitable characteristics for enzyme immobilization. The immobilized lipase suitable for pentyl octanoate synthesis has been prepared by a direct lipase binding to polymers via their epoxide groups. The enzymatic activity was determined by both hydrolysis of olive oil in an aqueous system and esterification of n-pentanol with octanoic acid in a low aqueous system. The influence of several important reaction parameters such as temperature, initial water content, initial substrate molar ratio, enzyme loading and time of adding of molecular sieves in the system is carefully analyzed by means of an experimental design. Production of the ester was optimized and an ester production response equation was obtained, making it possible to predict ester yields from known values of the five main factors. Almost complete conversion ( gt 99%) of the substrate to ester could be realized, using lipase loading as low as 37 mg/g dry support and in a relatively short time (24 h) at 45ºC, when high initial substrate molar ratio of 2.2 is used.
AB  - U radu su ispitani uticaji procesnih parametara na sintezu pentil-oktanoata pomoću lipaze iz Candida rugosa imobilisane na komercijalni polimetakrilatni nosač (Sepabeads EC-EP). U radu je primenjena metoda imobilizacije enzima koja se zasniva na direktnom vezivanju enzima za nosač preko epoksidne grupe polimera. Aktivnost imobilisanog enzima ispitana je u vodenom sistemu na model reakciji hidrolize maslinovog ulja kao i u nevodenom sistemu na modelu sinteze pentil-oktanoata u izooktanu. Ispitani su uticaji pet procesnih faktora na enzimsku sintezu datog estra primenom metode planiranih eksperimenata i metodologije odzivnih površina i to sadržaja vode, temperature, mase vezanog enzima na nosaču, početnog molarnog odnosa reaktanata i trenutka dodavanja molekulskih sita u sistem. Sinteza estara je optimizovana, izvršena je ocena značajnosti parametara i utvrđen je adekvatan matematički model na osnovu koga se može predvideti ponašanje sistema (prinos estara) u funkciji navedenih faktora.
PB  - Faculty of Technology, Novi Sad
T2  - Acta periodica technologica
T1  - Immobilization of lipase on sepabeads and its application in pentyl octanoate synthesis in a low aqueous system
T1  - Imobilizacija lipaze na komercijalni epoksidni nosač za sintezu pentil-oktanoata u mikrovodenom sistemu
EP  - 152
IS  - 39
SP  - 139
DO  - 10.2298/APT0839139K
ER  - 

@article{
author = "Knežević-Jugović, Zorica and Šaponjić, Svetlana V. and Bezbradica, Dejan and Mijin, Dušan",
year = "2008",
abstract = "The object of the study was to investigate the process conditions relevant for the pentyl octanoate production with the lipase from Candida rugosa immobilized on Sepabeads EC-EP carrier. This is an epoxide-containing commercial polymethacrylic carrier with suitable characteristics for enzyme immobilization. The immobilized lipase suitable for pentyl octanoate synthesis has been prepared by a direct lipase binding to polymers via their epoxide groups. The enzymatic activity was determined by both hydrolysis of olive oil in an aqueous system and esterification of n-pentanol with octanoic acid in a low aqueous system. The influence of several important reaction parameters such as temperature, initial water content, initial substrate molar ratio, enzyme loading and time of adding of molecular sieves in the system is carefully analyzed by means of an experimental design. Production of the ester was optimized and an ester production response equation was obtained, making it possible to predict ester yields from known values of the five main factors. Almost complete conversion ( gt 99%) of the substrate to ester could be realized, using lipase loading as low as 37 mg/g dry support and in a relatively short time (24 h) at 45ºC, when high initial substrate molar ratio of 2.2 is used., U radu su ispitani uticaji procesnih parametara na sintezu pentil-oktanoata pomoću lipaze iz Candida rugosa imobilisane na komercijalni polimetakrilatni nosač (Sepabeads EC-EP). U radu je primenjena metoda imobilizacije enzima koja se zasniva na direktnom vezivanju enzima za nosač preko epoksidne grupe polimera. Aktivnost imobilisanog enzima ispitana je u vodenom sistemu na model reakciji hidrolize maslinovog ulja kao i u nevodenom sistemu na modelu sinteze pentil-oktanoata u izooktanu. Ispitani su uticaji pet procesnih faktora na enzimsku sintezu datog estra primenom metode planiranih eksperimenata i metodologije odzivnih površina i to sadržaja vode, temperature, mase vezanog enzima na nosaču, početnog molarnog odnosa reaktanata i trenutka dodavanja molekulskih sita u sistem. Sinteza estara je optimizovana, izvršena je ocena značajnosti parametara i utvrđen je adekvatan matematički model na osnovu koga se može predvideti ponašanje sistema (prinos estara) u funkciji navedenih faktora.",
publisher = "Faculty of Technology, Novi Sad",
journal = "Acta periodica technologica",
title = "Immobilization of lipase on sepabeads and its application in pentyl octanoate synthesis in a low aqueous system, Imobilizacija lipaze na komercijalni epoksidni nosač za sintezu pentil-oktanoata u mikrovodenom sistemu",
pages = "152-139",
number = "39",
doi = "10.2298/APT0839139K"
}

Knežević-Jugović, Z., Šaponjić, S. V., Bezbradica, D.,& Mijin, D.. (2008). Immobilization of lipase on sepabeads and its application in pentyl octanoate synthesis in a low aqueous system. in Acta periodica technologica
Faculty of Technology, Novi Sad.(39), 139-152.
https://doi.org/10.2298/APT0839139K

Knežević-Jugović Z, Šaponjić SV, Bezbradica D, Mijin D. Immobilization of lipase on sepabeads and its application in pentyl octanoate synthesis in a low aqueous system. in Acta periodica technologica. 2008;(39):139-152.
doi:10.2298/APT0839139K .

Knežević-Jugović, Zorica, Šaponjić, Svetlana V., Bezbradica, Dejan, Mijin, Dušan, "Immobilization of lipase on sepabeads and its application in pentyl octanoate synthesis in a low aqueous system" in Acta periodica technologica, no. 39 (2008):139-152,
https://doi.org/10.2298/APT0839139K . .