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  - 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  - 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 . .