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  - https://cherry.chem.bg.ac.rs/handle/123456789/2338
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
VL  - 218
SP  - 505
EP  - 508
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",
volume = "218",
pages = "505-508",
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 J.
AU  - Gavrović-Jankulović, Marija
AU  - Pavlović, Marija
AU  - Rogniaux, Helene
AU  - Veličković, Dušan
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1914
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
VL  - 6
IS  - 41
SP  - 34818
EP  - 34824
DO  - 10.1039/c6ra07521e
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Milosavić, Nenad and Bezbradica, Dejan and Drakulić, Branko J. 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",
volume = "6",
number = "41",
pages = "34818-34824",
doi = "10.1039/c6ra07521e"
}

Trbojević-Ivić, J., Dimitrijević, A., Milosavić, N., Bezbradica, D., Drakulić, B. J., 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 BJ, 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 J., 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  - Dragacevic, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1943
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. (c) 2016 Society of Chemical Industry
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
VL  - 96
IS  - 12
SP  - 4281
EP  - 4287
DO  - 10.1002/jsfa.7641
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Bezbradica, Dejan and Dragacevic, 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. (c) 2016 Society of Chemical Industry",
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",
volume = "96",
number = "12",
pages = "4281-4287",
doi = "10.1002/jsfa.7641"
}

Trbojević-Ivić, J., Veličković, D., Dimitrijević, A., Bezbradica, D., Dragacevic, 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, Dragacevic 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, Dragacevic, 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  - Mihailović, Mladen
AU  - Trbojević-Ivić, Jovana
AU  - Banjanac, Katarina
AU  - Milosavić, Nenad
AU  - Veličković, Dušan
AU  - Carević, Milica
AU  - Bezbradica, Dejan
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2391
AB  - In this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports
VL  - 81
IS  - 12
SP  - 1371
EP  - 1382
DO  - 10.2298/JSC160730099M
ER  - 

@article{
author = "Mihailović, Mladen and Trbojević-Ivić, Jovana and Banjanac, Katarina and Milosavić, Nenad and Veličković, Dušan and Carević, Milica and Bezbradica, Dejan",
year = "2016",
abstract = "In this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports",
volume = "81",
number = "12",
pages = "1371-1382",
doi = "10.2298/JSC160730099M"
}

Mihailović, M., Trbojević-Ivić, J., Banjanac, K., Milosavić, N., Veličković, D., Carević, M.,& Bezbradica, D.. (2016). Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 81(12), 1371-1382.
https://doi.org/10.2298/JSC160730099M

Mihailović M, Trbojević-Ivić J, Banjanac K, Milosavić N, Veličković D, Carević M, Bezbradica D. Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports. in Journal of the Serbian Chemical Society. 2016;81(12):1371-1382.
doi:10.2298/JSC160730099M .

Mihailović, Mladen, Trbojević-Ivić, Jovana, Banjanac, Katarina, Milosavić, Nenad, Veličković, Dušan, Carević, Milica, Bezbradica, Dejan, "Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports" in Journal of the Serbian Chemical Society, 81, no. 12 (2016):1371-1382,
https://doi.org/10.2298/JSC160730099M . .

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  - https://cherry.chem.bg.ac.rs/handle/123456789/1516
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. (C) 2013 Elsevier Ltd. All rights reserved.
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
VL  - 387
SP  - 14
EP  - 18
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. (C) 2013 Elsevier Ltd. All rights reserved.",
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",
volume = "387",
pages = "14-18",
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  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko M.
AU  - Milosavić, Nenad
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1264
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. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite
VL  - 107
SP  - 358
EP  - 362
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 M. 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. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite",
volume = "107",
pages = "358-362",
doi = "10.1016/j.biortech.2011.11.077"
}

Dimitrijević, A., Veličković, D., Bihelović, F., Bezbradica, D., Jankov, R. M.,& 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 RM, 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 M., 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  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Knezevic-Jugovic, Zorica
AU  - Milosavić, Nenad
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1325
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
VL  - 35
IS  - 7
SP  - 1107
EP  - 1115
DO  - 10.1007/s00449-012-0695-3
ER  - 

@article{
author = "Veličković, Dušan and Dimitrijević, Aleksandra and Bihelović, Filip and Bezbradica, Dejan and Knezevic-Jugovic, 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",
volume = "35",
number = "7",
pages = "1107-1115",
doi = "10.1007/s00449-012-0695-3"
}

Veličković, D., Dimitrijević, A., Bihelović, F., Bezbradica, D., Knezevic-Jugovic, 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, Knezevic-Jugovic 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, Knezevic-Jugovic, 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 M.
AU  - Milosavić, Nenad
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1198
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 Soc, 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
VL  - 76
IS  - 8
SP  - 1081
EP  - 1092
DO  - 10.2298/JSC110428096D
ER  - 

@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Bezbradica, Dejan and Bihelović, Filip and Jankov, Ratko M. 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 Soc, 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",
volume = "76",
number = "8",
pages = "1081-1092",
doi = "10.2298/JSC110428096D"
}

Dimitrijević, A., Veličković, D., Bezbradica, D., Bihelović, F., Jankov, R. M.,& 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 Soc, Belgrade., 76(8), 1081-1092.
https://doi.org/10.2298/JSC110428096D

Dimitrijević A, Veličković D, Bezbradica D, Bihelović F, Jankov RM, 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.
doi:10.2298/JSC110428096D .

Dimitrijević, Aleksandra, Veličković, Dušan, Bezbradica, Dejan, Bihelović, Filip, Jankov, Ratko M., 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://doi.org/10.2298/JSC110428096D . .

TY  - JOUR
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko M.
AU  - Milosavić, Nenad
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1186
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
VL  - 46
IS  - 8
SP  - 1698
EP  - 1702
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 M. 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",
volume = "46",
number = "8",
pages = "1698-1702",
doi = "10.1016/j.procbio.2011.05.007"
}

Veličković, D., Dimitrijević, A., Bihelović, F., Bezbradica, D., Jankov, R. M.,& 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 RM, 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 M., 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 . .

TY  - CONF
AU  - Milosavić, Nenad
AU  - Prodanović, Radivoje
AU  - Jankov, Ratko M.
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/577
PB  - Elsevier Science Bv, Amsterdam
C3  - Journal of Biotechnology
T1  - Stereoselectivity of alpha-glucosidase from baker's yeast for transglucosylation reaction
VL  - 136
DO  - 10.1016/j.jbiotec.2008.07.830
ER  - 

@conference{
author = "Milosavić, Nenad and Prodanović, Radivoje and Jankov, Ratko M.",
year = "2008",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Biotechnology",
title = "Stereoselectivity of alpha-glucosidase from baker's yeast for transglucosylation reaction",
volume = "136",
doi = "10.1016/j.jbiotec.2008.07.830"
}

Milosavić, N., Prodanović, R.,& Jankov, R. M.. (2008). Stereoselectivity of alpha-glucosidase from baker's yeast for transglucosylation reaction. in Journal of Biotechnology
Elsevier Science Bv, Amsterdam., 136.
https://doi.org/10.1016/j.jbiotec.2008.07.830

Milosavić N, Prodanović R, Jankov RM. Stereoselectivity of alpha-glucosidase from baker's yeast for transglucosylation reaction. in Journal of Biotechnology. 2008;136.
doi:10.1016/j.jbiotec.2008.07.830 .

Milosavić, Nenad, Prodanović, Radivoje, Jankov, Ratko M., "Stereoselectivity of alpha-glucosidase from baker's yeast for transglucosylation reaction" in Journal of Biotechnology, 136 (2008),
https://doi.org/10.1016/j.jbiotec.2008.07.830 . .

TY  - JOUR
AU  - Bogdanović, Jelena
AU  - Milosavić, Nenad
AU  - Prodanović, Radivoje
AU  - Ducic, Tanja
AU  - Radotić, Ksenija
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/829
AB  - Variations were studied of the activity and isoenzyme patterns of soluble peroxidase, catalase, catechol oxidase and superoxide dismutase, in needles of the Balkan endemic conifer Serbian spruce, Picea omorika (Panc.) Purkinye. The samples were collected from the natural habitat of the species, Mt. Tara. Seasonal changes were found to affect enzymatic activities and isoenzyme profiles. Total protein content was significantly lower in the summer than in other seasons. Several isoforms of peroxidase, catechol oxidase and superoxide dismutase (SOD), as well as two catalase isoenzymes were detected. The number of peroxidase isoenzymes was greatest during the vegetative season. Catalase and catechol oxidase peaked in summer and spring, respectively. Total SOD and Mn-SOD activities were significantly higher in the winter samples than the summer ones. (C) 2006 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Biochemical Systematics and Ecology
T1  - Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panc.) Purkinye)
VL  - 35
IS  - 5
SP  - 263
EP  - 273
DO  - 10.1016/j.bse.2006.12.001
ER  - 

@article{
author = "Bogdanović, Jelena and Milosavić, Nenad and Prodanović, Radivoje and Ducic, Tanja and Radotić, Ksenija",
year = "2007",
abstract = "Variations were studied of the activity and isoenzyme patterns of soluble peroxidase, catalase, catechol oxidase and superoxide dismutase, in needles of the Balkan endemic conifer Serbian spruce, Picea omorika (Panc.) Purkinye. The samples were collected from the natural habitat of the species, Mt. Tara. Seasonal changes were found to affect enzymatic activities and isoenzyme profiles. Total protein content was significantly lower in the summer than in other seasons. Several isoforms of peroxidase, catechol oxidase and superoxide dismutase (SOD), as well as two catalase isoenzymes were detected. The number of peroxidase isoenzymes was greatest during the vegetative season. Catalase and catechol oxidase peaked in summer and spring, respectively. Total SOD and Mn-SOD activities were significantly higher in the winter samples than the summer ones. (C) 2006 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Biochemical Systematics and Ecology",
title = "Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panc.) Purkinye)",
volume = "35",
number = "5",
pages = "263-273",
doi = "10.1016/j.bse.2006.12.001"
}

Bogdanović, J., Milosavić, N., Prodanović, R., Ducic, T.,& Radotić, K.. (2007). Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panc.) Purkinye). in Biochemical Systematics and Ecology
Pergamon-Elsevier Science Ltd, Oxford., 35(5), 263-273.
https://doi.org/10.1016/j.bse.2006.12.001

Bogdanović J, Milosavić N, Prodanović R, Ducic T, Radotić K. Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panc.) Purkinye). in Biochemical Systematics and Ecology. 2007;35(5):263-273.
doi:10.1016/j.bse.2006.12.001 .

Bogdanović, Jelena, Milosavić, Nenad, Prodanović, Radivoje, Ducic, Tanja, Radotić, Ksenija, "Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panc.) Purkinye)" in Biochemical Systematics and Ecology, 35, no. 5 (2007):263-273,
https://doi.org/10.1016/j.bse.2006.12.001 . .

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Milosavić, Nenad
AU  - Jovanović, Slobodan
AU  - Prodanović, Olivera
AU  - Ćirković-Veličković, Tanja
AU  - Vujčić, Zoran
AU  - Jankov, Ratko M.
PY  - 2006
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/791
AB  - The activity of alpha-glucosidase from baker's yeast was determined in various concentrations of dioxan, tetrahydrofuran, tert-butanol, dimethylformamide, methanol and dimethylsulfoxide (DMSO). Higher activities were observed with sucrose than with nitrophenylglucoside as substrate in cosolvent mixtures. In 30% (v/v) DMSO, 25% of the activity obtained in pure water was detected, and in 30% (v/v) methanol 12.5% of the activity in pure water was detected, while in other cosolvents there was almost no activity under these conditions. alpha-glucosidase was immobilized onto a macroporous copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate, poly(GMA-co-EGDMA), by the glutaraldehyde method. By immobilization, the half-life of the enzyme in 35% (v/v) methanol was increased from 6 to 60min and from 4 to 15min in 45% (v/v) DMSO. The activity of the immobilized enzyme in 30% (v/v) DMSO and 30% (v/v) methanol was 22% and 18% of the activity in pure water, respectively.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Biocatalysis and Biotransformation
T1  - Activity and stability of soluble and immobilized alpha-glucosidase from baker's yeast in cosolvent systems
VL  - 24
IS  - 3
SP  - 195
EP  - 200
DO  - 10.1080/10242420600655903
ER  - 

@article{
author = "Prodanović, Radivoje and Milosavić, Nenad and Jovanović, Slobodan and Prodanović, Olivera and Ćirković-Veličković, Tanja and Vujčić, Zoran and Jankov, Ratko M.",
year = "2006",
abstract = "The activity of alpha-glucosidase from baker's yeast was determined in various concentrations of dioxan, tetrahydrofuran, tert-butanol, dimethylformamide, methanol and dimethylsulfoxide (DMSO). Higher activities were observed with sucrose than with nitrophenylglucoside as substrate in cosolvent mixtures. In 30% (v/v) DMSO, 25% of the activity obtained in pure water was detected, and in 30% (v/v) methanol 12.5% of the activity in pure water was detected, while in other cosolvents there was almost no activity under these conditions. alpha-glucosidase was immobilized onto a macroporous copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate, poly(GMA-co-EGDMA), by the glutaraldehyde method. By immobilization, the half-life of the enzyme in 35% (v/v) methanol was increased from 6 to 60min and from 4 to 15min in 45% (v/v) DMSO. The activity of the immobilized enzyme in 30% (v/v) DMSO and 30% (v/v) methanol was 22% and 18% of the activity in pure water, respectively.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Biocatalysis and Biotransformation",
title = "Activity and stability of soluble and immobilized alpha-glucosidase from baker's yeast in cosolvent systems",
volume = "24",
number = "3",
pages = "195-200",
doi = "10.1080/10242420600655903"
}

Prodanović, R., Milosavić, N., Jovanović, S., Prodanović, O., Ćirković-Veličković, T., Vujčić, Z.,& Jankov, R. M.. (2006). Activity and stability of soluble and immobilized alpha-glucosidase from baker's yeast in cosolvent systems. in Biocatalysis and Biotransformation
Taylor & Francis Ltd, Abingdon., 24(3), 195-200.
https://doi.org/10.1080/10242420600655903

Prodanović R, Milosavić N, Jovanović S, Prodanović O, Ćirković-Veličković T, Vujčić Z, Jankov RM. Activity and stability of soluble and immobilized alpha-glucosidase from baker's yeast in cosolvent systems. in Biocatalysis and Biotransformation. 2006;24(3):195-200.
doi:10.1080/10242420600655903 .

Prodanović, Radivoje, Milosavić, Nenad, Jovanović, Slobodan, Prodanović, Olivera, Ćirković-Veličković, Tanja, Vujčić, Zoran, Jankov, Ratko M., "Activity and stability of soluble and immobilized alpha-glucosidase from baker's yeast in cosolvent systems" in Biocatalysis and Biotransformation, 24, no. 3 (2006):195-200,
https://doi.org/10.1080/10242420600655903 . .

TY  - JOUR
AU  - Knezevic, Zorica
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Jakovljević, Živana
AU  - Prodanović, Radivoje
PY  - 2006
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/787
AB  - The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system. (c) 2006 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Sa, Lausanne
T2  - Biochemical Engineering Journal
T1  - Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment
VL  - 30
IS  - 3
SP  - 269
EP  - 278
DO  - 10.1016/j.bej.2006.05.009
ER  - 

@article{
author = "Knezevic, Zorica and Milosavić, Nenad and Bezbradica, Dejan and Jakovljević, Živana and Prodanović, Radivoje",
year = "2006",
abstract = "The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system. (c) 2006 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Biochemical Engineering Journal",
title = "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment",
volume = "30",
number = "3",
pages = "269-278",
doi = "10.1016/j.bej.2006.05.009"
}

Knezevic, Z., Milosavić, N., Bezbradica, D., Jakovljević, Ž.,& Prodanović, R.. (2006). Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment. in Biochemical Engineering Journal
Elsevier Science Sa, Lausanne., 30(3), 269-278.
https://doi.org/10.1016/j.bej.2006.05.009

Knezevic Z, Milosavić N, Bezbradica D, Jakovljević Ž, Prodanović R. Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment. in Biochemical Engineering Journal. 2006;30(3):269-278.
doi:10.1016/j.bej.2006.05.009 .

Knezevic, Zorica, Milosavić, Nenad, Bezbradica, Dejan, Jakovljević, Živana, Prodanović, Radivoje, "Immobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachment" in Biochemical Engineering Journal, 30, no. 3 (2006):269-278,
https://doi.org/10.1016/j.bej.2006.05.009 . .