TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Milosavić, Nenad
AU  - Dimitrijević, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Kolarski, Dušan
AU  - Veličković, Dušan
PY  - 2017
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3659
AB  - A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases
EP  - 508
SP  - 505
VL  - 218
DO  - 10.1016/j.foodchem.2016.09.049
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Milosavić, Nenad and Dimitrijević, Aleksandra and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Kolarski, Dušan and Veličković, Dušan",
year = "2017",
abstract = "A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases",
pages = "508-505",
volume = "218",
doi = "10.1016/j.foodchem.2016.09.049"
}

Trbojević-Ivić, J., Milosavić, N., Dimitrijević, A., Gavrović-Jankulović, M., Bezbradica, D., Kolarski, D.,& Veličković, D.. (2017). Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. in Food Chemistry
Elsevier Sci Ltd, Oxford., 218, 505-508.
https://doi.org/10.1016/j.foodchem.2016.09.049

Trbojević-Ivić J, Milosavić N, Dimitrijević A, Gavrović-Jankulović M, Bezbradica D, Kolarski D, Veličković D. Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. in Food Chemistry. 2017;218:505-508.
doi:10.1016/j.foodchem.2016.09.049 .

Trbojević-Ivić, Jovana, Milosavić, Nenad, Dimitrijević, Aleksandra, Gavrović-Jankulović, Marija, Bezbradica, Dejan, Kolarski, Dušan, Veličković, Dušan, "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases" in Food Chemistry, 218 (2017):505-508,
https://doi.org/10.1016/j.foodchem.2016.09.049 . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Drakulić, Branko
AU  - Gavrović-Jankulović, Marija
AU  - Pavlović, Marija
AU  - Rogniaux, Helene
AU  - Veličković, Dušan
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3442
AB  - Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's -COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling
EP  - 34824
IS  - 41
SP  - 34818
VL  - 6
DO  - 10.1039/c6ra07521e
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Milosavić, Nenad and Bezbradica, Dejan and Drakulić, Branko and Gavrović-Jankulović, Marija and Pavlović, Marija and Rogniaux, Helene and Veličković, Dušan",
year = "2016",
abstract = "Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's -COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling",
pages = "34824-34818",
number = "41",
volume = "6",
doi = "10.1039/c6ra07521e"
}

Trbojević-Ivić, J., Dimitrijević, A., Milosavić, N., Bezbradica, D., Drakulić, B., Gavrović-Jankulović, M., Pavlović, M., Rogniaux, H.,& Veličković, D.. (2016). Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(41), 34818-34824.
https://doi.org/10.1039/c6ra07521e

Trbojević-Ivić J, Dimitrijević A, Milosavić N, Bezbradica D, Drakulić B, Gavrović-Jankulović M, Pavlović M, Rogniaux H, Veličković D. Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling. in RSC Advances. 2016;6(41):34818-34824.
doi:10.1039/c6ra07521e .

Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, Milosavić, Nenad, Bezbradica, Dejan, Drakulić, Branko, Gavrović-Jankulović, Marija, Pavlović, Marija, Rogniaux, Helene, Veličković, Dušan, "Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling" in RSC Advances, 6, no. 41 (2016):34818-34824,
https://doi.org/10.1039/c6ra07521e . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bezbradica, Dejan
AU  - Dragacević, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3225
AB  - BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market.
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry
EP  - 4287
IS  - 12
SP  - 4281
VL  - 96
DO  - 10.1002/jsfa.7641
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Bezbradica, Dejan and Dragacević, Vladimir and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2016",
abstract = "BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry",
pages = "4287-4281",
number = "12",
volume = "96",
doi = "10.1002/jsfa.7641"
}

Trbojević-Ivić, J., Veličković, D., Dimitrijević, A., Bezbradica, D., Dragacević, V., Gavrović-Jankulović, M.,& Milosavić, N.. (2016). Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Hoboken., 96(12), 4281-4287.
https://doi.org/10.1002/jsfa.7641

Trbojević-Ivić J, Veličković D, Dimitrijević A, Bezbradica D, Dragacević V, Gavrović-Jankulović M, Milosavić N. Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. in Journal of the Science of Food and Agriculture. 2016;96(12):4281-4287.
doi:10.1002/jsfa.7641 .

Trbojević-Ivić, Jovana, Veličković, Dušan, Dimitrijević, Aleksandra, Bezbradica, Dejan, Dragacević, Vladimir, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry" in Journal of the Science of Food and Agriculture, 96, no. 12 (2016):4281-4287,
https://doi.org/10.1002/jsfa.7641 . .

TY  - JOUR
AU  - Carević, Milica
AU  - Vukašinović-Sekulić, Maja
AU  - Grbavčić, Sanja
AU  - Stojanović, Marija
AU  - Mihailović, Mladen
AU  - Dimitrijević, Aleksandra
AU  - Bezbradica, Dejan
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2885
AB  - (-galactosidase, commonly known as lactase, represents commercially important enzyme that is prevalently used for lactose hydrolysis in milk and whey. To the date, it has been isolated from various sources. In this study different strains of lactic acid bacteria were assessed for their (-galactosidase productivity, and Lactobacillus acidophilus ATCC 4356 resulted with the highest production potential. Thereafter, optimal conditions for accomplishing high yields of (-galactosidase activity were determined. Maximal specific activity (1.01 IU mL-1) was accomplished after 2 days shake flask culture fermentation (150 rpm) at 37°C, with modified Man Rogosa Sharpe culture broth using lactose (2.5%) as sole carbon source. Finally, in order to intensify release of intracellular (-galactosidase different mechanical and chemical methods were conducted. Nevertheless, vortexing with quartz sand (150 μm) as abrasive was proven to be the most efficient method of cell disruption. The optimum temperature of obtained (-galactosidase was 45°C and the optimum range pH 6.5-7.5.
AB  - Enzim (-galaktozidaza, poznatija kao laktaza, predstavlja industrijski izuzetno važan enzim, koji ima primarnu ulogu u hidrolizi disaharida laktoze. Upotrebom ovog enzima u industriji mleka i mlečnih proizvoda dolazi do poboljšanja fizičkih i senzornih karakteristika proizvoda, kao i do povećanja svarljivosti proizvoda, a samim tim i prevazilaženja problema netolerancije na laktozu. Takođe, hidrolizom laktoze surutke, rešava se pitanje njenog ekološki prihvatljivog odlaganja. Sa druge strane, enzim pod kontrolisanim reakcionim uslovima može katalizovatii proces transgalaktozilacije, odnosno prenošenja galaktozil jedinica na druge šećere prisutne u sistemu (najčešće laktozu), pri čemu nastaju izuzetno važna funkcionalna jedinjenja galaktooligosaharidi. Enzim (-galaktozidaza može biti različitog porekla - biljnog, životinjskog ili mikrobnog. Međutim, najznačajniji među njima su mikrobni postupci proizvodnje, zbog lake fermentacije, velike brzine rasta i razmnožavanja ćelija, visokih prinosa, visoke aktivnosti, kao i stabilnosti enzima. Kao posledica velikog komercijalnog interesa za ovaj enzim, opisane su različite metode dobijanja i prečišćavanja dobijenih enzima iz različitih mikroorganizama. Poslednjih godina bakterije mlečne kiseline privlače sve više pažnje kao potencijalni izvori (-galaktozidaza najviše zahvaljujući svom statusu bezbednih za upotrebu u prehrambenoj i farmaceutskoj industriji, čime se omogućava neometano korišćenje enzima bez primene komplikovanih metoda prečišćavanja. U ovom radu ispitana je mogućnost proizvodnje (-galaktozidaza pomoću nekoliko vrsta bakterija mlečne kiseline. Kao najbolji producent među ispitanim bakterijama pokazala se bakterija Lactobacillus acidophilus. Najveća aktivnost (-galaktozidaze, dobijena je mikroaerofilnom fermentacijom u modifikovanoj komercijalnoj MRS podlozi, sa 2,5% laktoze kao jedinim izvorom ugljenika. Fermentacija je vršena na tresilici (150 rpm) u trajanju od 48 h i na temperaturi od 37°C. Kako je enzim intracelularan, u cilju razaranja ćelija i oslobađanja enzima, primenjeno je više različitih fizičkih i hemijskih metoda, a daleko najboljom pokazala se metoda vorteksiranja sa kvarcnim peskom (150 μm) kao abrazivnim sredstvom. Ovako dobijen enzim pokazao je maksimalnu aktivnost pri temperaturi od 45°C i pH u opsegu 6.5-7.5.
PB  - Association of Chemical Engineers of Serbia
T2  - Hemijska industrija
T1  - Optimization of (-galactosidase production from lactic acid bacteria
T1  - Optimizacija proizvodnje (-galaktozidaze pomoću bakterija mlečne kiseline
EP  - 312
IS  - 3
SP  - 305
VL  - 69
DO  - 10.2298/HEMIND140303044C
ER  - 

@article{
author = "Carević, Milica and Vukašinović-Sekulić, Maja and Grbavčić, Sanja and Stojanović, Marija and Mihailović, Mladen and Dimitrijević, Aleksandra and Bezbradica, Dejan",
year = "2015",
abstract = "(-galactosidase, commonly known as lactase, represents commercially important enzyme that is prevalently used for lactose hydrolysis in milk and whey. To the date, it has been isolated from various sources. In this study different strains of lactic acid bacteria were assessed for their (-galactosidase productivity, and Lactobacillus acidophilus ATCC 4356 resulted with the highest production potential. Thereafter, optimal conditions for accomplishing high yields of (-galactosidase activity were determined. Maximal specific activity (1.01 IU mL-1) was accomplished after 2 days shake flask culture fermentation (150 rpm) at 37°C, with modified Man Rogosa Sharpe culture broth using lactose (2.5%) as sole carbon source. Finally, in order to intensify release of intracellular (-galactosidase different mechanical and chemical methods were conducted. Nevertheless, vortexing with quartz sand (150 μm) as abrasive was proven to be the most efficient method of cell disruption. The optimum temperature of obtained (-galactosidase was 45°C and the optimum range pH 6.5-7.5., Enzim (-galaktozidaza, poznatija kao laktaza, predstavlja industrijski izuzetno važan enzim, koji ima primarnu ulogu u hidrolizi disaharida laktoze. Upotrebom ovog enzima u industriji mleka i mlečnih proizvoda dolazi do poboljšanja fizičkih i senzornih karakteristika proizvoda, kao i do povećanja svarljivosti proizvoda, a samim tim i prevazilaženja problema netolerancije na laktozu. Takođe, hidrolizom laktoze surutke, rešava se pitanje njenog ekološki prihvatljivog odlaganja. Sa druge strane, enzim pod kontrolisanim reakcionim uslovima može katalizovatii proces transgalaktozilacije, odnosno prenošenja galaktozil jedinica na druge šećere prisutne u sistemu (najčešće laktozu), pri čemu nastaju izuzetno važna funkcionalna jedinjenja galaktooligosaharidi. Enzim (-galaktozidaza može biti različitog porekla - biljnog, životinjskog ili mikrobnog. Međutim, najznačajniji među njima su mikrobni postupci proizvodnje, zbog lake fermentacije, velike brzine rasta i razmnožavanja ćelija, visokih prinosa, visoke aktivnosti, kao i stabilnosti enzima. Kao posledica velikog komercijalnog interesa za ovaj enzim, opisane su različite metode dobijanja i prečišćavanja dobijenih enzima iz različitih mikroorganizama. Poslednjih godina bakterije mlečne kiseline privlače sve više pažnje kao potencijalni izvori (-galaktozidaza najviše zahvaljujući svom statusu bezbednih za upotrebu u prehrambenoj i farmaceutskoj industriji, čime se omogućava neometano korišćenje enzima bez primene komplikovanih metoda prečišćavanja. U ovom radu ispitana je mogućnost proizvodnje (-galaktozidaza pomoću nekoliko vrsta bakterija mlečne kiseline. Kao najbolji producent među ispitanim bakterijama pokazala se bakterija Lactobacillus acidophilus. Najveća aktivnost (-galaktozidaze, dobijena je mikroaerofilnom fermentacijom u modifikovanoj komercijalnoj MRS podlozi, sa 2,5% laktoze kao jedinim izvorom ugljenika. Fermentacija je vršena na tresilici (150 rpm) u trajanju od 48 h i na temperaturi od 37°C. Kako je enzim intracelularan, u cilju razaranja ćelija i oslobađanja enzima, primenjeno je više različitih fizičkih i hemijskih metoda, a daleko najboljom pokazala se metoda vorteksiranja sa kvarcnim peskom (150 μm) kao abrazivnim sredstvom. Ovako dobijen enzim pokazao je maksimalnu aktivnost pri temperaturi od 45°C i pH u opsegu 6.5-7.5.",
publisher = "Association of Chemical Engineers of Serbia",
journal = "Hemijska industrija",
title = "Optimization of (-galactosidase production from lactic acid bacteria, Optimizacija proizvodnje (-galaktozidaze pomoću bakterija mlečne kiseline",
pages = "312-305",
number = "3",
volume = "69",
doi = "10.2298/HEMIND140303044C"
}

Carević, M., Vukašinović-Sekulić, M., Grbavčić, S., Stojanović, M., Mihailović, M., Dimitrijević, A.,& Bezbradica, D.. (2015). Optimization of (-galactosidase production from lactic acid bacteria. in Hemijska industrija
Association of Chemical Engineers of Serbia., 69(3), 305-312.
https://doi.org/10.2298/HEMIND140303044C

Carević M, Vukašinović-Sekulić M, Grbavčić S, Stojanović M, Mihailović M, Dimitrijević A, Bezbradica D. Optimization of (-galactosidase production from lactic acid bacteria. in Hemijska industrija. 2015;69(3):305-312.
doi:10.2298/HEMIND140303044C .

Carević, Milica, Vukašinović-Sekulić, Maja, Grbavčić, Sanja, Stojanović, Marija, Mihailović, Mladen, Dimitrijević, Aleksandra, Bezbradica, Dejan, "Optimization of (-galactosidase production from lactic acid bacteria" in Hemijska industrija, 69, no. 3 (2015):305-312,
https://doi.org/10.2298/HEMIND140303044C . .

TY  - JOUR
AU  - Stojanović, Marija
AU  - Simović, Milica
AU  - Mihailović, Mladen
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4720
AB  - Fatty acid (FA) ascorbyl esters are recently emerging food, cosmetic, and pharmaceutical additives, which can be prepared in an eco-friendly way by using lipases as catalysts. Because they are amphiphilic molecules, which possess high free radical scavenging capacity, they can be applied as liposoluble antioxidants as well as emulsifiers and biosurfactants. In this study, the influence of a wide range of acyl donors on ester yield in lipase-catalyzed synthesis and ester antioxidant activity was examined. Among saturated acyl donors, higher yields and antioxidant activities of esters were achieved when short-chain FAs were used. Oleic acid gave the highest yield overall and its ester exhibited a high antioxidant activity. Optimization of experimental factors showed that the highest conversion (60.5%) in acetone was achieved with 5 g L-1 of lipase, 50 mM of vitamin C, 10-fold molar excess of oleic acid, and 0.7 mL L-1 of initial water. Obtained results showed that even short- and medium-chain ascorbyl esters could be synthesized with high yields and retained (or even exceeded) free radical scavenging capacity of l-ascorbic acid, indicating prospects of broadening their application in emulsions and liposomes.
PB  - Wiley, Hoboken
T2  - Biotechnology and Applied Biochemistry
T1  - Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity
EP  - 466
IS  - 4
SP  - 458
VL  - 62
DO  - 10.1002/bab.1296
ER  - 

@article{
author = "Stojanović, Marija and Simović, Milica and Mihailović, Mladen and Veličković, Dušan and Dimitrijević, Aleksandra and Milosavić, Nenad and Bezbradica, Dejan",
year = "2015",
abstract = "Fatty acid (FA) ascorbyl esters are recently emerging food, cosmetic, and pharmaceutical additives, which can be prepared in an eco-friendly way by using lipases as catalysts. Because they are amphiphilic molecules, which possess high free radical scavenging capacity, they can be applied as liposoluble antioxidants as well as emulsifiers and biosurfactants. In this study, the influence of a wide range of acyl donors on ester yield in lipase-catalyzed synthesis and ester antioxidant activity was examined. Among saturated acyl donors, higher yields and antioxidant activities of esters were achieved when short-chain FAs were used. Oleic acid gave the highest yield overall and its ester exhibited a high antioxidant activity. Optimization of experimental factors showed that the highest conversion (60.5%) in acetone was achieved with 5 g L-1 of lipase, 50 mM of vitamin C, 10-fold molar excess of oleic acid, and 0.7 mL L-1 of initial water. Obtained results showed that even short- and medium-chain ascorbyl esters could be synthesized with high yields and retained (or even exceeded) free radical scavenging capacity of l-ascorbic acid, indicating prospects of broadening their application in emulsions and liposomes.",
publisher = "Wiley, Hoboken",
journal = "Biotechnology and Applied Biochemistry",
title = "Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity",
pages = "466-458",
number = "4",
volume = "62",
doi = "10.1002/bab.1296"
}

Stojanović, M., Simović, M., Mihailović, M., Veličković, D., Dimitrijević, A., Milosavić, N.,& Bezbradica, D.. (2015). Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity. in Biotechnology and Applied Biochemistry
Wiley, Hoboken., 62(4), 458-466.
https://doi.org/10.1002/bab.1296

Stojanović M, Simović M, Mihailović M, Veličković D, Dimitrijević A, Milosavić N, Bezbradica D. Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity. in Biotechnology and Applied Biochemistry. 2015;62(4):458-466.
doi:10.1002/bab.1296 .

Stojanović, Marija, Simović, Milica, Mihailović, Mladen, Veličković, Dušan, Dimitrijević, Aleksandra, Milosavić, Nenad, Bezbradica, Dejan, "Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity" in Biotechnology and Applied Biochemistry, 62, no. 4 (2015):458-466,
https://doi.org/10.1002/bab.1296 . .

TY  - JOUR
AU  - Stojanović, Marija
AU  - Simović, Milica
AU  - Mihailović, Mladen
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3146
AB  - Fatty acid (FA) ascorbyl esters are recently emerging food, cosmetic, and pharmaceutical additives, which can be prepared in an eco-friendly way by using lipases as catalysts. Because they are amphiphilic molecules, which possess high free radical scavenging capacity, they can be applied as liposoluble antioxidants as well as emulsifiers and biosurfactants. In this study, the influence of a wide range of acyl donors on ester yield in lipase-catalyzed synthesis and ester antioxidant activity was examined. Among saturated acyl donors, higher yields and antioxidant activities of esters were achieved when short-chain FAs were used. Oleic acid gave the highest yield overall and its ester exhibited a high antioxidant activity. Optimization of experimental factors showed that the highest conversion (60.5%) in acetone was achieved with 5 g L-1 of lipase, 50 mM of vitamin C, 10-fold molar excess of oleic acid, and 0.7 mL L-1 of initial water. Obtained results showed that even short- and medium-chain ascorbyl esters could be synthesized with high yields and retained (or even exceeded) free radical scavenging capacity of l-ascorbic acid, indicating prospects of broadening their application in emulsions and liposomes.
PB  - Wiley, Hoboken
T2  - Biotechnology and Applied Biochemistry
T1  - Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity
EP  - 466
IS  - 4
SP  - 458
VL  - 62
DO  - 10.1002/bab.1296
ER  - 

@article{
author = "Stojanović, Marija and Simović, Milica and Mihailović, Mladen and Veličković, Dušan and Dimitrijević, Aleksandra and Milosavić, Nenad and Bezbradica, Dejan",
year = "2015",
abstract = "Fatty acid (FA) ascorbyl esters are recently emerging food, cosmetic, and pharmaceutical additives, which can be prepared in an eco-friendly way by using lipases as catalysts. Because they are amphiphilic molecules, which possess high free radical scavenging capacity, they can be applied as liposoluble antioxidants as well as emulsifiers and biosurfactants. In this study, the influence of a wide range of acyl donors on ester yield in lipase-catalyzed synthesis and ester antioxidant activity was examined. Among saturated acyl donors, higher yields and antioxidant activities of esters were achieved when short-chain FAs were used. Oleic acid gave the highest yield overall and its ester exhibited a high antioxidant activity. Optimization of experimental factors showed that the highest conversion (60.5%) in acetone was achieved with 5 g L-1 of lipase, 50 mM of vitamin C, 10-fold molar excess of oleic acid, and 0.7 mL L-1 of initial water. Obtained results showed that even short- and medium-chain ascorbyl esters could be synthesized with high yields and retained (or even exceeded) free radical scavenging capacity of l-ascorbic acid, indicating prospects of broadening their application in emulsions and liposomes.",
publisher = "Wiley, Hoboken",
journal = "Biotechnology and Applied Biochemistry",
title = "Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity",
pages = "466-458",
number = "4",
volume = "62",
doi = "10.1002/bab.1296"
}

Stojanović, M., Simović, M., Mihailović, M., Veličković, D., Dimitrijević, A., Milosavić, N.,& Bezbradica, D.. (2015). Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity. in Biotechnology and Applied Biochemistry
Wiley, Hoboken., 62(4), 458-466.
https://doi.org/10.1002/bab.1296

Stojanović M, Simović M, Mihailović M, Veličković D, Dimitrijević A, Milosavić N, Bezbradica D. Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity. in Biotechnology and Applied Biochemistry. 2015;62(4):458-466.
doi:10.1002/bab.1296 .

Stojanović, Marija, Simović, Milica, Mihailović, Mladen, Veličković, Dušan, Dimitrijević, Aleksandra, Milosavić, Nenad, Bezbradica, Dejan, "Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity" in Biotechnology and Applied Biochemistry, 62, no. 4 (2015):458-466,
https://doi.org/10.1002/bab.1296 . .

TY  - JOUR
AU  - Pavlović, Marija
AU  - Dimitrijević, Aleksandra
AU  - Bezbradica, Dejan
AU  - Milosavić, Nenad
AU  - Gavrović-Jankulović, Marija
AU  - Šegan, Dejan M.
AU  - Veličković, Dušan
PY  - 2014
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2753
AB  - Benzyl alcohol, a potent anesthetic and bacteriostatic, can be efficiently glucosylated by alpha-glucosidase from Saccharomyces cerevisiae to produce benzyl alcohol alpha-glucoside with a 75% yield. However, while studying the transglucosylation reaction conditions, it was found out that benzyl alcohol is a non-competitive inhibitor of alpha-glucosidase's hydrolytic activity (K-i = 18 mM, toward maltose). Due to its interesting ability to be glycosylated by the enzyme and to inhibit its hydrolytic activity, we proposed a plausible mechanism for the phenolic alpha-glucosydase inhibitor's binding, since the mechanism of inhibition has not yet been elucidated.
PB  - Elsevier Sci Ltd, Oxford
T2  - Carbohydrate Research
T1  - Dual effect of benzyl alcohol on alpha-glucosidase activity: efficient substrate for high yield transglucosylation and non-competitive inhibitor of its hydrolytic activity
EP  - 18
SP  - 14
VL  - 387
DO  - 10.1016/j.carres.2013.08.028
ER  - 

@article{
author = "Pavlović, Marija and Dimitrijević, Aleksandra and Bezbradica, Dejan and Milosavić, Nenad and Gavrović-Jankulović, Marija and Šegan, Dejan M. and Veličković, Dušan",
year = "2014",
abstract = "Benzyl alcohol, a potent anesthetic and bacteriostatic, can be efficiently glucosylated by alpha-glucosidase from Saccharomyces cerevisiae to produce benzyl alcohol alpha-glucoside with a 75% yield. However, while studying the transglucosylation reaction conditions, it was found out that benzyl alcohol is a non-competitive inhibitor of alpha-glucosidase's hydrolytic activity (K-i = 18 mM, toward maltose). Due to its interesting ability to be glycosylated by the enzyme and to inhibit its hydrolytic activity, we proposed a plausible mechanism for the phenolic alpha-glucosydase inhibitor's binding, since the mechanism of inhibition has not yet been elucidated.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Carbohydrate Research",
title = "Dual effect of benzyl alcohol on alpha-glucosidase activity: efficient substrate for high yield transglucosylation and non-competitive inhibitor of its hydrolytic activity",
pages = "18-14",
volume = "387",
doi = "10.1016/j.carres.2013.08.028"
}

Pavlović, M., Dimitrijević, A., Bezbradica, D., Milosavić, N., Gavrović-Jankulović, M., Šegan, D. M.,& Veličković, D.. (2014). Dual effect of benzyl alcohol on alpha-glucosidase activity: efficient substrate for high yield transglucosylation and non-competitive inhibitor of its hydrolytic activity. in Carbohydrate Research
Elsevier Sci Ltd, Oxford., 387, 14-18.
https://doi.org/10.1016/j.carres.2013.08.028

Pavlović M, Dimitrijević A, Bezbradica D, Milosavić N, Gavrović-Jankulović M, Šegan DM, Veličković D. Dual effect of benzyl alcohol on alpha-glucosidase activity: efficient substrate for high yield transglucosylation and non-competitive inhibitor of its hydrolytic activity. in Carbohydrate Research. 2014;387:14-18.
doi:10.1016/j.carres.2013.08.028 .

Pavlović, Marija, Dimitrijević, Aleksandra, Bezbradica, Dejan, Milosavić, Nenad, Gavrović-Jankulović, Marija, Šegan, Dejan M., Veličković, Dušan, "Dual effect of benzyl alcohol on alpha-glucosidase activity: efficient substrate for high yield transglucosylation and non-competitive inhibitor of its hydrolytic activity" in Carbohydrate Research, 387 (2014):14-18,
https://doi.org/10.1016/j.carres.2013.08.028 . .

TY  - JOUR
AU  - Veličković, Dušan
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Bihelović, Filip
AU  - Segal, Ann Marie
AU  - Šegan, Dejan M.
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
PY  - 2014
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2788
AB  - Our investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation
EP  - 6328
IS  - 14
SP  - 6317
VL  - 98
DO  - 10.1007/s00253-014-5587-9
ER  - 

@article{
author = "Veličković, Dušan and Milosavić, Nenad and Bezbradica, Dejan and Bihelović, Filip and Segal, Ann Marie and Šegan, Dejan M. and Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra",
year = "2014",
abstract = "Our investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation",
pages = "6328-6317",
number = "14",
volume = "98",
doi = "10.1007/s00253-014-5587-9"
}

Veličković, D., Milosavić, N., Bezbradica, D., Bihelović, F., Segal, A. M., Šegan, D. M., Trbojević-Ivić, J.,& Dimitrijević, A.. (2014). The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation. in Applied Microbiology and Biotechnology
Springer, New York., 98(14), 6317-6328.
https://doi.org/10.1007/s00253-014-5587-9

Veličković D, Milosavić N, Bezbradica D, Bihelović F, Segal AM, Šegan DM, Trbojević-Ivić J, Dimitrijević A. The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation. in Applied Microbiology and Biotechnology. 2014;98(14):6317-6328.
doi:10.1007/s00253-014-5587-9 .

Veličković, Dušan, Milosavić, Nenad, Bezbradica, Dejan, Bihelović, Filip, Segal, Ann Marie, Šegan, Dejan M., Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, "The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation" in Applied Microbiology and Biotechnology, 98, no. 14 (2014):6317-6328,
https://doi.org/10.1007/s00253-014-5587-9 . .

TY  - JOUR
AU  - Bezbradica, Dejan
AU  - Stojanović, Marija
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Carević, Milica
AU  - Mihailović, Mladen
AU  - Milosavić, Nenad
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550
AB  - The kinetics of L-ascorbyl oleate synthesis catalyzed by immobilized lipase from Candida antarctica in acetone was investigated. Significant inhibition of synthesis with an excess of ascorbic acid was observed. Experimental data were successfully fitted with a ping-pong bi-bi kinetic model with substrate inhibition, and related kinetic constants were determined. The kinetic study was performed at optimum experimental factors (temperature, initial water content, and enzyme concentration), which were determined using response surface methodology. Then, a model for predicting product-time progress curves was developed by expanding the obtained ping-pang model with terms describing ester hydrolysis. Kinetic constants of the reverse reaction were determined, and good congruence between the model and experimental data was achieved. Calculated kinetic constants revealed that lipase has the highest affinity for ascorbyl oleate, slightly lower activity with ascorbic acid, and the lowest activity with oleic acid. The obtained results are valuable for elucidating the reaction mechanism and represent an important contribution for reaction optimization and creating strategies to increase the productivity of vitamin C ester synthesis.
PB  - Elsevier Science Sa, Lausanne
T2  - Biochemical Engineering Journal
T1  - Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester
EP  - 96
SP  - 89
VL  - 71
DO  - 10.1016/j.bej.2012.12.001
ER  - 

@article{
author = "Bezbradica, Dejan and Stojanović, Marija and Veličković, Dušan and Dimitrijević, Aleksandra and Carević, Milica and Mihailović, Mladen and Milosavić, Nenad",
year = "2013",
abstract = "The kinetics of L-ascorbyl oleate synthesis catalyzed by immobilized lipase from Candida antarctica in acetone was investigated. Significant inhibition of synthesis with an excess of ascorbic acid was observed. Experimental data were successfully fitted with a ping-pong bi-bi kinetic model with substrate inhibition, and related kinetic constants were determined. The kinetic study was performed at optimum experimental factors (temperature, initial water content, and enzyme concentration), which were determined using response surface methodology. Then, a model for predicting product-time progress curves was developed by expanding the obtained ping-pang model with terms describing ester hydrolysis. Kinetic constants of the reverse reaction were determined, and good congruence between the model and experimental data was achieved. Calculated kinetic constants revealed that lipase has the highest affinity for ascorbyl oleate, slightly lower activity with ascorbic acid, and the lowest activity with oleic acid. The obtained results are valuable for elucidating the reaction mechanism and represent an important contribution for reaction optimization and creating strategies to increase the productivity of vitamin C ester synthesis.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Biochemical Engineering Journal",
title = "Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester",
pages = "96-89",
volume = "71",
doi = "10.1016/j.bej.2012.12.001"
}

Bezbradica, D., Stojanović, M., Veličković, D., Dimitrijević, A., Carević, M., Mihailović, M.,& Milosavić, N.. (2013). Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester. in Biochemical Engineering Journal
Elsevier Science Sa, Lausanne., 71, 89-96.
https://doi.org/10.1016/j.bej.2012.12.001

Bezbradica D, Stojanović M, Veličković D, Dimitrijević A, Carević M, Mihailović M, Milosavić N. Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester. in Biochemical Engineering Journal. 2013;71:89-96.
doi:10.1016/j.bej.2012.12.001 .

Bezbradica, Dejan, Stojanović, Marija, Veličković, Dušan, Dimitrijević, Aleksandra, Carević, Milica, Mihailović, Mladen, Milosavić, Nenad, "Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester" in Biochemical Engineering Journal, 71 (2013):89-96,
https://doi.org/10.1016/j.bej.2012.12.001 . .

TY  - JOUR
AU  - Stojanović, Marija
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Knežević-Jugović, Zorica
AU  - Bezbradica, Dejan
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2413
AB  - Lipase-catalyzed ascorbyl oleate synthesis is eco-friendly and selective way of production of liposoluble biocompatible antioxidants, but still not present on an industrial level due to the high biocatalyst costs. In this study, response surface methodology was applied in order to estimate influence of individual experimental factors, identify interactions among them, and to determine optimum conditions for enzymatic synthesis of ascorbyl oleate in acetone, in terms of limiting substrate conversion, product yield, and yield per mass of consumed enzyme. As a biocatalyst, commercial immobilized preparation of lipase B from Candida antarctica, Novozym 435, was used. In order to develop cost-effective process, at reaction conditions at which maximum amount of product per mass of biocatalyst was produced (60 degrees C, 0.018 % (v/v) of water, 0.135 M of vitamin C, substrates molar ratio 1:8, and 0.2 % (w/v) of lipase), possibilities for further increase of ester yield were investigated. Addition of molecular sieves at 4th hour of reaction enabled increase of yield from 16.7 mmol g(-1) to 19.3 mmol g(-1). Operational stability study revealed that after ten reaction cycles enzyme retained 48 % of its initial activity. Optimized synthesis with well-timed molecular sieves addition and repeated use of lipase provided production of 153 mmol per gram of enzyme. Further improvement of productivity was achieved using procedure for the enzyme reactivation.
PB  - Japan Oil Chemists Soc, Tokyo
T2  - Journal of Oleo Science
T1  - Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability
EP  - 603
IS  - 8
SP  - 591
VL  - 62
DO  - 10.5650/jos.62.591
ER  - 

@article{
author = "Stojanović, Marija and Veličković, Dušan and Dimitrijević, Aleksandra and Milosavić, Nenad and Knežević-Jugović, Zorica and Bezbradica, Dejan",
year = "2013",
abstract = "Lipase-catalyzed ascorbyl oleate synthesis is eco-friendly and selective way of production of liposoluble biocompatible antioxidants, but still not present on an industrial level due to the high biocatalyst costs. In this study, response surface methodology was applied in order to estimate influence of individual experimental factors, identify interactions among them, and to determine optimum conditions for enzymatic synthesis of ascorbyl oleate in acetone, in terms of limiting substrate conversion, product yield, and yield per mass of consumed enzyme. As a biocatalyst, commercial immobilized preparation of lipase B from Candida antarctica, Novozym 435, was used. In order to develop cost-effective process, at reaction conditions at which maximum amount of product per mass of biocatalyst was produced (60 degrees C, 0.018 % (v/v) of water, 0.135 M of vitamin C, substrates molar ratio 1:8, and 0.2 % (w/v) of lipase), possibilities for further increase of ester yield were investigated. Addition of molecular sieves at 4th hour of reaction enabled increase of yield from 16.7 mmol g(-1) to 19.3 mmol g(-1). Operational stability study revealed that after ten reaction cycles enzyme retained 48 % of its initial activity. Optimized synthesis with well-timed molecular sieves addition and repeated use of lipase provided production of 153 mmol per gram of enzyme. Further improvement of productivity was achieved using procedure for the enzyme reactivation.",
publisher = "Japan Oil Chemists Soc, Tokyo",
journal = "Journal of Oleo Science",
title = "Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability",
pages = "603-591",
number = "8",
volume = "62",
doi = "10.5650/jos.62.591"
}

Stojanović, M., Veličković, D., Dimitrijević, A., Milosavić, N., Knežević-Jugović, Z.,& Bezbradica, D.. (2013). Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability. in Journal of Oleo Science
Japan Oil Chemists Soc, Tokyo., 62(8), 591-603.
https://doi.org/10.5650/jos.62.591

Stojanović M, Veličković D, Dimitrijević A, Milosavić N, Knežević-Jugović Z, Bezbradica D. Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability. in Journal of Oleo Science. 2013;62(8):591-603.
doi:10.5650/jos.62.591 .

Stojanović, Marija, Veličković, Dušan, Dimitrijević, Aleksandra, Milosavić, Nenad, Knežević-Jugović, Zorica, Bezbradica, Dejan, "Lipase-Catalyzed Synthesis of Ascorbyl Oleate in Acetone: Optimization of Reaction Conditions and Lipase Reusability" in Journal of Oleo Science, 62, no. 8 (2013):591-603,
https://doi.org/10.5650/jos.62.591 . .

TY  - JOUR
AU  - Pavlović, Marijana
AU  - Dimitrijević, Aleksandra
AU  - Trbojević-Ivić, Jovana
AU  - Milosavić, Nenad
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Veličković, Dušan
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2448
AB  - alpha-1,4-Glucosidase from Saccharomyces cerevisiae is an enzyme which is widely used in synthesis of different drugs. Glucosidase inhibitors are studied as potential drugs for prevention of HIV and diabetes. For understanding of these processes it is very important to have insights in the transglucosylation activity of this enzyme. In this paper the kinetics of transglucosylation reaction catalyzed by this enzyme in the synthesis of benzyl alcohol glucoside was studied and all relevant kinetic constants for this system are found. It was shown one additional property of transglycosylation reactions catalyzed by glycosidases-inhibition by both, glucose acceptor and glucose donor, and mechanisms for these inhibitions were proposed.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Russian Journal of Physical Chemistry A
T1  - A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae
EP  - 2288
IS  - 13
SP  - 2285
VL  - 87
DO  - 10.1134/S0036024413130207
ER  - 

@article{
author = "Pavlović, Marijana and Dimitrijević, Aleksandra and Trbojević-Ivić, Jovana and Milosavić, Nenad and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Veličković, Dušan",
year = "2013",
abstract = "alpha-1,4-Glucosidase from Saccharomyces cerevisiae is an enzyme which is widely used in synthesis of different drugs. Glucosidase inhibitors are studied as potential drugs for prevention of HIV and diabetes. For understanding of these processes it is very important to have insights in the transglucosylation activity of this enzyme. In this paper the kinetics of transglucosylation reaction catalyzed by this enzyme in the synthesis of benzyl alcohol glucoside was studied and all relevant kinetic constants for this system are found. It was shown one additional property of transglycosylation reactions catalyzed by glycosidases-inhibition by both, glucose acceptor and glucose donor, and mechanisms for these inhibitions were proposed.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Russian Journal of Physical Chemistry A",
title = "A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae",
pages = "2288-2285",
number = "13",
volume = "87",
doi = "10.1134/S0036024413130207"
}

Pavlović, M., Dimitrijević, A., Trbojević-Ivić, J., Milosavić, N., Gavrović-Jankulović, M., Bezbradica, D.,& Veličković, D.. (2013). A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae. in Russian Journal of Physical Chemistry A
Maik Nauka/Interperiodica/Springer, New York., 87(13), 2285-2288.
https://doi.org/10.1134/S0036024413130207

Pavlović M, Dimitrijević A, Trbojević-Ivić J, Milosavić N, Gavrović-Jankulović M, Bezbradica D, Veličković D. A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae. in Russian Journal of Physical Chemistry A. 2013;87(13):2285-2288.
doi:10.1134/S0036024413130207 .

Pavlović, Marijana, Dimitrijević, Aleksandra, Trbojević-Ivić, Jovana, Milosavić, Nenad, Gavrović-Jankulović, Marija, Bezbradica, Dejan, Veličković, Dušan, "A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae" in Russian Journal of Physical Chemistry A, 87, no. 13 (2013):2285-2288,
https://doi.org/10.1134/S0036024413130207 . .

TY  - CONF
AU  - Stojanović, M.M.
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Knežević-Jugović, Zorica
AU  - Bezbradica, Dejan
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1976
AB  - L-ascorbic acid has good antioxidative properties but its efficiency in stabilizing fats and oils in products with high lipid content is negligible due to its hydrophilic characteristics. On the other hand, fatty acid ascorbyl esters are liposoluble, with even better antioxidative properties comparing to L-ascorbic acid. Therefore, developing of industrial process for lipase-catalyzed synthesis of vitamin C fatty acid esters, considering numerous advantages over conventional chemical methods (mild reaction conditions, high regioselectivity, and simplified downstream processing), is of great interest. In this study, L-ascorbyl oleate was synthesized in esterification reaction between vitamin C and oleic acid catalyzed by immobilized lipase from Candida antarctica in acetone as a reaction medium. Response surface methodology and 5-level-5-factor central composite rotatable design were employed in order to investigate interactions between experimental factors (initial water content, temperature, substrates molar ratio, vitamin C concentration, and enzyme amount), determine their individual influence on molar conversion, and eventually optimize the synthesis. Based on the experimental data, regression model, expressed with second order polynomial equation, was obtained. At values in the range of examination, enzyme amount had no influence on conversion so it was fixed at the minimum (0.2 % (w/v)). The maximum molar conversion of 91.3 % was predicted and corresponding, optimal reaction conditions were: temperature - 60 °C, initial water content - 0 % (v/v), vitamin C concentration - 0.02 M, and substrate molar ratio - 1:15. Our system provided reaction conditions which enabled high conversions, thus obtained results may be used as a starting point for the process scale-up.
PB  - 6th Central European Congress on Food, CEFood 2012
C3  - CEFood 2012 - Proceedings of 6th Central European Congress on Food
T1  - Study of lipase-catalyzed synthesis of ascorbyl oleate using response surface methodology
EP  - 813
SP  - 807
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1976
ER  - 

@conference{
author = "Stojanović, M.M. and Veličković, Dušan and Dimitrijević, Aleksandra and Milosavić, Nenad and Knežević-Jugović, Zorica and Bezbradica, Dejan",
year = "2012",
abstract = "L-ascorbic acid has good antioxidative properties but its efficiency in stabilizing fats and oils in products with high lipid content is negligible due to its hydrophilic characteristics. On the other hand, fatty acid ascorbyl esters are liposoluble, with even better antioxidative properties comparing to L-ascorbic acid. Therefore, developing of industrial process for lipase-catalyzed synthesis of vitamin C fatty acid esters, considering numerous advantages over conventional chemical methods (mild reaction conditions, high regioselectivity, and simplified downstream processing), is of great interest. In this study, L-ascorbyl oleate was synthesized in esterification reaction between vitamin C and oleic acid catalyzed by immobilized lipase from Candida antarctica in acetone as a reaction medium. Response surface methodology and 5-level-5-factor central composite rotatable design were employed in order to investigate interactions between experimental factors (initial water content, temperature, substrates molar ratio, vitamin C concentration, and enzyme amount), determine their individual influence on molar conversion, and eventually optimize the synthesis. Based on the experimental data, regression model, expressed with second order polynomial equation, was obtained. At values in the range of examination, enzyme amount had no influence on conversion so it was fixed at the minimum (0.2 % (w/v)). The maximum molar conversion of 91.3 % was predicted and corresponding, optimal reaction conditions were: temperature - 60 °C, initial water content - 0 % (v/v), vitamin C concentration - 0.02 M, and substrate molar ratio - 1:15. Our system provided reaction conditions which enabled high conversions, thus obtained results may be used as a starting point for the process scale-up.",
publisher = "6th Central European Congress on Food, CEFood 2012",
journal = "CEFood 2012 - Proceedings of 6th Central European Congress on Food",
title = "Study of lipase-catalyzed synthesis of ascorbyl oleate using response surface methodology",
pages = "813-807",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1976"
}

Stojanović, M.M., Veličković, D., Dimitrijević, A., Milosavić, N., Knežević-Jugović, Z.,& Bezbradica, D.. (2012). Study of lipase-catalyzed synthesis of ascorbyl oleate using response surface methodology. in CEFood 2012 - Proceedings of 6th Central European Congress on Food
6th Central European Congress on Food, CEFood 2012., 807-813.
https://hdl.handle.net/21.15107/rcub_technorep_1976

Stojanović M, Veličković D, Dimitrijević A, Milosavić N, Knežević-Jugović Z, Bezbradica D. Study of lipase-catalyzed synthesis of ascorbyl oleate using response surface methodology. in CEFood 2012 - Proceedings of 6th Central European Congress on Food. 2012;:807-813.
https://hdl.handle.net/21.15107/rcub_technorep_1976 .

Stojanović, M.M., Veličković, Dušan, Dimitrijević, Aleksandra, Milosavić, Nenad, Knežević-Jugović, Zorica, Bezbradica, Dejan, "Study of lipase-catalyzed synthesis of ascorbyl oleate using response surface methodology" in CEFood 2012 - Proceedings of 6th Central European Congress on Food (2012):807-813,
https://hdl.handle.net/21.15107/rcub_technorep_1976 .

TY  - CHAP
AU  - Milosavić, Nenad
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bezbradica, Dejan
AU  - Knežević-Jugović, Zorica
AU  - Jankov, Ratko
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1968
AB  - Enzymes are a particularly versatile class of catalysts that perform and regulate processes in living matter. Enzymatic regio-, chemo- and enantioselectivity were used in industry and in organic synthesis. The common perception is however, that enzymes are sensitive, unstable and have to be used in water, features that are not ideal for a catalyst and undesirable in most syntheses. In many cases a way to avoid at least part of these complaints is to immobilize enzymes. There are several immobilization techniques, and the best means of avoiding any negative influence on the structure of an enzyme is to encapsulate it. Due to its ability to form gel with multivalent cations under relatively mild conditions, alginates are very important in cell and enzyme encapsulation. Entrapment within insoluble alginate gel is recognized as a rapid, nontoxic, inexpensive and versatile method for immobilization of enzymes as well as cells. The resultant gel is biochemically inert and mechanically stable with interstitial spaces that are suitable for cell immobilization.
T2  - Alginates: Production, Types and Applications
T1  - Application of alginates in cell and enzyme immobilization
EP  - 60
SP  - 37
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1968
ER  - 

@inbook{
author = "Milosavić, Nenad and Dimitrijević, Aleksandra and Veličković, Dušan and Bezbradica, Dejan and Knežević-Jugović, Zorica and Jankov, Ratko",
year = "2012",
abstract = "Enzymes are a particularly versatile class of catalysts that perform and regulate processes in living matter. Enzymatic regio-, chemo- and enantioselectivity were used in industry and in organic synthesis. The common perception is however, that enzymes are sensitive, unstable and have to be used in water, features that are not ideal for a catalyst and undesirable in most syntheses. In many cases a way to avoid at least part of these complaints is to immobilize enzymes. There are several immobilization techniques, and the best means of avoiding any negative influence on the structure of an enzyme is to encapsulate it. Due to its ability to form gel with multivalent cations under relatively mild conditions, alginates are very important in cell and enzyme encapsulation. Entrapment within insoluble alginate gel is recognized as a rapid, nontoxic, inexpensive and versatile method for immobilization of enzymes as well as cells. The resultant gel is biochemically inert and mechanically stable with interstitial spaces that are suitable for cell immobilization.",
journal = "Alginates: Production, Types and Applications",
booktitle = "Application of alginates in cell and enzyme immobilization",
pages = "60-37",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1968"
}

Milosavić, N., Dimitrijević, A., Veličković, D., Bezbradica, D., Knežević-Jugović, Z.,& Jankov, R.. (2012). Application of alginates in cell and enzyme immobilization. in Alginates: Production, Types and Applications, 37-60.
https://hdl.handle.net/21.15107/rcub_technorep_1968

Milosavić N, Dimitrijević A, Veličković D, Bezbradica D, Knežević-Jugović Z, Jankov R. Application of alginates in cell and enzyme immobilization. in Alginates: Production, Types and Applications. 2012;:37-60.
https://hdl.handle.net/21.15107/rcub_technorep_1968 .

Milosavić, Nenad, Dimitrijević, Aleksandra, Veličković, Dušan, Bezbradica, Dejan, Knežević-Jugović, Zorica, Jankov, Ratko, "Application of alginates in cell and enzyme immobilization" in Alginates: Production, Types and Applications (2012):37-60,
https://hdl.handle.net/21.15107/rcub_technorep_1968 .

TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko
AU  - Milosavić, Nenad
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2201
AB  - Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite
EP  - 362
SP  - 358
VL  - 107
DO  - 10.1016/j.biortech.2011.11.077
ER  - 

@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Bihelović, Filip and Bezbradica, Dejan and Jankov, Ratko and Milosavić, Nenad",
year = "2012",
abstract = "Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite",
pages = "362-358",
volume = "107",
doi = "10.1016/j.biortech.2011.11.077"
}

Dimitrijević, A., Veličković, D., Bihelović, F., Bezbradica, D., Jankov, R.,& Milosavić, N.. (2012). One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 107, 358-362.
https://doi.org/10.1016/j.biortech.2011.11.077

Dimitrijević A, Veličković D, Bihelović F, Bezbradica D, Jankov R, Milosavić N. One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite. in Bioresource Technology. 2012;107:358-362.
doi:10.1016/j.biortech.2011.11.077 .

Dimitrijević, Aleksandra, Veličković, Dušan, Bihelović, Filip, Bezbradica, Dejan, Jankov, Ratko, Milosavić, Nenad, "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite" in Bioresource Technology, 107 (2012):358-362,
https://doi.org/10.1016/j.biortech.2011.11.077 . .

TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2157
AB  - Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be a-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate.
PB  - Wiley, Hoboken
T2  - Biotechnology Progress
T1  - Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis
EP  - 1456
IS  - 6
SP  - 1450
VL  - 28
DO  - 10.1002/btpr.1628
ER  - 

@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Milosavić, Nenad and Bezbradica, Dejan",
year = "2012",
abstract = "Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be a-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate.",
publisher = "Wiley, Hoboken",
journal = "Biotechnology Progress",
title = "Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis",
pages = "1456-1450",
number = "6",
volume = "28",
doi = "10.1002/btpr.1628"
}

Dimitrijević, A., Veličković, D., Milosavić, N.,& Bezbradica, D.. (2012). Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. in Biotechnology Progress
Wiley, Hoboken., 28(6), 1450-1456.
https://doi.org/10.1002/btpr.1628

Dimitrijević A, Veličković D, Milosavić N, Bezbradica D. Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. in Biotechnology Progress. 2012;28(6):1450-1456.
doi:10.1002/btpr.1628 .

Dimitrijević, Aleksandra, Veličković, Dušan, Milosavić, Nenad, Bezbradica, Dejan, "Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis" in Biotechnology Progress, 28, no. 6 (2012):1450-1456,
https://doi.org/10.1002/btpr.1628 . .

TY  - JOUR
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Knežević-Jugović, Zorica
AU  - Milosavić, Nenad
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2109
AB  - Novel glucoside of physiological active vanillyl alcohol was synthesized for the first time using maltase from Saccharomyces cerevisiae as catalyst, and established its structure as 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside. The key reaction factors for this transglucosylation reaction were optimized using response surface methodology and the highest yield so far in maltase catalyzed transglucosylation reaction was obtained. It was found out that optimum temperature of reaction was 37 A degrees C, optimal maltose concentration was 60% (w/v), optimal pH was 6.6, and optimal concentration of vanillyl alcohol was 158 mM. Under these conditions, yield of glucoside was 90 mM with no by product formation. It was shown that this compound posses good antioxidant activity as well as stability in gastrointestinal tract. It was demonstrated that it is hydrolyzed on brush border membrane of enterocytes, so it can serve in protecting gastrointestinal system from oxidation, as well as source of anticonvulsive drug after the hydrolysis of glucoside on brush border membrane of small intestine.
PB  - Springer, New York
T2  - Bioprocess and Biosystems Engineering
T1  - Novel glycoside of vanillyl alcohol, 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside: study of enzymatic synthesis, in vitro digestion and antioxidant activity
EP  - 1115
IS  - 7
SP  - 1107
VL  - 35
DO  - 10.1007/s00449-012-0695-3
ER  - 

@article{
author = "Veličković, Dušan and Dimitrijević, Aleksandra and Bihelović, Filip and Bezbradica, Dejan and Knežević-Jugović, Zorica and Milosavić, Nenad",
year = "2012",
abstract = "Novel glucoside of physiological active vanillyl alcohol was synthesized for the first time using maltase from Saccharomyces cerevisiae as catalyst, and established its structure as 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside. The key reaction factors for this transglucosylation reaction were optimized using response surface methodology and the highest yield so far in maltase catalyzed transglucosylation reaction was obtained. It was found out that optimum temperature of reaction was 37 A degrees C, optimal maltose concentration was 60% (w/v), optimal pH was 6.6, and optimal concentration of vanillyl alcohol was 158 mM. Under these conditions, yield of glucoside was 90 mM with no by product formation. It was shown that this compound posses good antioxidant activity as well as stability in gastrointestinal tract. It was demonstrated that it is hydrolyzed on brush border membrane of enterocytes, so it can serve in protecting gastrointestinal system from oxidation, as well as source of anticonvulsive drug after the hydrolysis of glucoside on brush border membrane of small intestine.",
publisher = "Springer, New York",
journal = "Bioprocess and Biosystems Engineering",
title = "Novel glycoside of vanillyl alcohol, 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside: study of enzymatic synthesis, in vitro digestion and antioxidant activity",
pages = "1115-1107",
number = "7",
volume = "35",
doi = "10.1007/s00449-012-0695-3"
}

Veličković, D., Dimitrijević, A., Bihelović, F., Bezbradica, D., Knežević-Jugović, Z.,& Milosavić, N.. (2012). Novel glycoside of vanillyl alcohol, 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside: study of enzymatic synthesis, in vitro digestion and antioxidant activity. in Bioprocess and Biosystems Engineering
Springer, New York., 35(7), 1107-1115.
https://doi.org/10.1007/s00449-012-0695-3

Veličković D, Dimitrijević A, Bihelović F, Bezbradica D, Knežević-Jugović Z, Milosavić N. Novel glycoside of vanillyl alcohol, 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside: study of enzymatic synthesis, in vitro digestion and antioxidant activity. in Bioprocess and Biosystems Engineering. 2012;35(7):1107-1115.
doi:10.1007/s00449-012-0695-3 .

Veličković, Dušan, Dimitrijević, Aleksandra, Bihelović, Filip, Bezbradica, Dejan, Knežević-Jugović, Zorica, Milosavić, Nenad, "Novel glycoside of vanillyl alcohol, 4-hydroxy-3-methoxybenzyl-alpha-d-glucopyranoside: study of enzymatic synthesis, in vitro digestion and antioxidant activity" in Bioprocess and Biosystems Engineering, 35, no. 7 (2012):1107-1115,
https://doi.org/10.1007/s00449-012-0695-3 . .

TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bezbradica, Dejan
AU  - Bihelović, Filip
AU  - Jankov, Ratko
AU  - Milosavić, Nenad
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1800
AB  - The production of lipase from Pseudozyma aphidis (DSM 70725) was determined in six different media. The highest lipase production was observed in a medium with glucose as the sole carbon source, and yeast extract and sodium nitrate as the nitrogen sources. The time course studies of growth and lipase production in the optimal medium revealed that the highest lipase production was achieved at the end of the log phase of growth, reaching the value of 35.0 U cm-3 in the fifth day of cultivation. The effects of various polar, water-miscible, organic solvents on the activity and stability of the crude lipase produced by P. aphidis were evaluated. The hydrolytic activity of the crude lipase towards p-nitrophenyl palmitate (p-NPP) in aqueous media and in organic solvents was determined, using the same spectrophotometric assay in both the aqueous and organic media. The crude lipase preparation exhibited activity towards p-NPP only in acetone and acetonitrile, while the lipase was stable only in acetone, with 23% residual activity after 24 h of incubation. These results suggested that lipase from P. aphidis can be used as a biocatalyst for potential applications in such organic solvents.
AB  - Proizvodnja lipaze iz Pseudozyma aphidis utvrđena je u šest različitih medijuma. Najviša proizvodnja uočena je u medijumu gde je glukoza bila izvor ugljenika, a ekstrakt kvasca i natrijum-nitrat izvori azota. Praćenjem dinamike rasta i proizvodnje lipaze u optimalnom medijumu, uočeno je da se najviša proizvodnja lipaze dostiže pred kraj logaritamske faze rasta, i dostiže vrednost od 35 U cm-3 u petom danu kultivacije, što je četri puta veća proizvodnja od one do sada prijavljene u literaturi. Utvrđen je efekat različitih polarnih organskih rastvarača, mešljivih sa vodom, na aktivnost i stabilnost lipaze iz P. aphidis. Hidrolitička aktivnost lipaze prema para-nitrofenil-palmitatu (p-NPP-u) u vo- denoj sredini i organskim rastvaračima utvrđena je upotrebom istog spektrofotometrijskog testa. Pokazano je da lipaza ima aktivnost prema p-NPP-u samo u acetonu i acetonitrilu, dok je enzim stabilan jedino u acetonu i zadržava 23% aktivnosti nakon 24 časa inkubacije. Dobijeni rezultati ukazuju da lipaza iz P. aphidis može biti korišćena kao biokatalizator za potencijalne primene u acetonu kao medijumu.
PB  - Serbian Chemical Society, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents
T1  - Proizvodnja lipaze iz Pseudozyma aphidis i utvrđivanje aktivnosti i stabilnosti lipaze u polarnim organskim rastvaračima
EP  - 1092
IS  - 8
SP  - 1081
VL  - 76
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1800
ER  - 

@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Bezbradica, Dejan and Bihelović, Filip and Jankov, Ratko and Milosavić, Nenad",
year = "2011",
abstract = "The production of lipase from Pseudozyma aphidis (DSM 70725) was determined in six different media. The highest lipase production was observed in a medium with glucose as the sole carbon source, and yeast extract and sodium nitrate as the nitrogen sources. The time course studies of growth and lipase production in the optimal medium revealed that the highest lipase production was achieved at the end of the log phase of growth, reaching the value of 35.0 U cm-3 in the fifth day of cultivation. The effects of various polar, water-miscible, organic solvents on the activity and stability of the crude lipase produced by P. aphidis were evaluated. The hydrolytic activity of the crude lipase towards p-nitrophenyl palmitate (p-NPP) in aqueous media and in organic solvents was determined, using the same spectrophotometric assay in both the aqueous and organic media. The crude lipase preparation exhibited activity towards p-NPP only in acetone and acetonitrile, while the lipase was stable only in acetone, with 23% residual activity after 24 h of incubation. These results suggested that lipase from P. aphidis can be used as a biocatalyst for potential applications in such organic solvents., Proizvodnja lipaze iz Pseudozyma aphidis utvrđena je u šest različitih medijuma. Najviša proizvodnja uočena je u medijumu gde je glukoza bila izvor ugljenika, a ekstrakt kvasca i natrijum-nitrat izvori azota. Praćenjem dinamike rasta i proizvodnje lipaze u optimalnom medijumu, uočeno je da se najviša proizvodnja lipaze dostiže pred kraj logaritamske faze rasta, i dostiže vrednost od 35 U cm-3 u petom danu kultivacije, što je četri puta veća proizvodnja od one do sada prijavljene u literaturi. Utvrđen je efekat različitih polarnih organskih rastvarača, mešljivih sa vodom, na aktivnost i stabilnost lipaze iz P. aphidis. Hidrolitička aktivnost lipaze prema para-nitrofenil-palmitatu (p-NPP-u) u vo- denoj sredini i organskim rastvaračima utvrđena je upotrebom istog spektrofotometrijskog testa. Pokazano je da lipaza ima aktivnost prema p-NPP-u samo u acetonu i acetonitrilu, dok je enzim stabilan jedino u acetonu i zadržava 23% aktivnosti nakon 24 časa inkubacije. Dobijeni rezultati ukazuju da lipaza iz P. aphidis može biti korišćena kao biokatalizator za potencijalne primene u acetonu kao medijumu.",
publisher = "Serbian Chemical Society, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents, Proizvodnja lipaze iz Pseudozyma aphidis i utvrđivanje aktivnosti i stabilnosti lipaze u polarnim organskim rastvaračima",
pages = "1092-1081",
number = "8",
volume = "76",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1800"
}

Dimitrijević, A., Veličković, D., Bezbradica, D., Bihelović, F., Jankov, R.,& Milosavić, N.. (2011). Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents. in Journal of the Serbian Chemical Society
Serbian Chemical Society, Belgrade., 76(8), 1081-1092.
https://hdl.handle.net/21.15107/rcub_technorep_1800

Dimitrijević A, Veličković D, Bezbradica D, Bihelović F, Jankov R, Milosavić N. Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents. in Journal of the Serbian Chemical Society. 2011;76(8):1081-1092.
https://hdl.handle.net/21.15107/rcub_technorep_1800 .

Dimitrijević, Aleksandra, Veličković, Dušan, Bezbradica, Dejan, Bihelović, Filip, Jankov, Ratko, Milosavić, Nenad, "Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents" in Journal of the Serbian Chemical Society, 76, no. 8 (2011):1081-1092,
https://hdl.handle.net/21.15107/rcub_technorep_1800 .

TY  - JOUR
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko
AU  - Milosavić, Nenad
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1891
AB  - In this report, alpha-isosalicin, a potent anticoagulant and skin whitening agent, was synthesized by a highly efficient chemoselective and diastereoselective reaction, catalyzed by maltase from bakers' yeast (Saccharomyces cerevisiae). The highest yield of this one-step transglucosylation reaction was achieved with 50 mM of salicyl alcohol as a glucose acceptor. The key reaction factors were optimized using response surface methodology (RSM) with an enzyme concentration of 10 U/mL. The optimum temperature of the reaction was determined as 36.5 degrees C, the optimal maltose concentration was 40% (w/v), the optimal pH was 6.5, and the optimal reaction time was 16 h. Under these conditions 75% of alpha-isosalicin was obtained, with a yield of 10 g/L, and no by product formation was observed.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae
EP  - 1702
IS  - 8
SP  - 1698
VL  - 46
DO  - 10.1016/j.procbio.2011.05.007
ER  - 

@article{
author = "Veličković, Dušan and Dimitrijević, Aleksandra and Bihelović, Filip and Bezbradica, Dejan and Jankov, Ratko and Milosavić, Nenad",
year = "2011",
abstract = "In this report, alpha-isosalicin, a potent anticoagulant and skin whitening agent, was synthesized by a highly efficient chemoselective and diastereoselective reaction, catalyzed by maltase from bakers' yeast (Saccharomyces cerevisiae). The highest yield of this one-step transglucosylation reaction was achieved with 50 mM of salicyl alcohol as a glucose acceptor. The key reaction factors were optimized using response surface methodology (RSM) with an enzyme concentration of 10 U/mL. The optimum temperature of the reaction was determined as 36.5 degrees C, the optimal maltose concentration was 40% (w/v), the optimal pH was 6.5, and the optimal reaction time was 16 h. Under these conditions 75% of alpha-isosalicin was obtained, with a yield of 10 g/L, and no by product formation was observed.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae",
pages = "1702-1698",
number = "8",
volume = "46",
doi = "10.1016/j.procbio.2011.05.007"
}

Veličković, D., Dimitrijević, A., Bihelović, F., Bezbradica, D., Jankov, R.,& Milosavić, N.. (2011). A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 46(8), 1698-1702.
https://doi.org/10.1016/j.procbio.2011.05.007

Veličković D, Dimitrijević A, Bihelović F, Bezbradica D, Jankov R, Milosavić N. A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae. in Process Biochemistry. 2011;46(8):1698-1702.
doi:10.1016/j.procbio.2011.05.007 .

Veličković, Dušan, Dimitrijević, Aleksandra, Bihelović, Filip, Bezbradica, Dejan, Jankov, Ratko, Milosavić, Nenad, "A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae" in Process Biochemistry, 46, no. 8 (2011):1698-1702,
https://doi.org/10.1016/j.procbio.2011.05.007 . .