Trbojević-Ivić, Jovana

Link to this page

Authority KeyName Variants
orcid::0000-0003-0984-9193
  • Trbojević-Ivić, Jovana (8)
  • Trbojević Ivić, Jovana (1)
Projects

Author's Bibliography

Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj

Trbojević Ivić, Jovana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Trbojević Ivić, Jovana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7117
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:20779/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=51817999
UR  - http://nardus.mpn.gov.rs/123456789/11808
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3911
AB  - U ovoj doktorskoj disertaciji je ispitan potencijal HAP za imobilizaciju industrijski značajnih enzima na primeru 4 lipaze i 4 glikozidaze različitog porekla, strukture i supstratne specifičnosti. Od testiranih enzima za HAP se najefikasnije vezuju lipaza iz Candida rugosa (CRL) i β-galaktozidaza (laktaza) iz Aspergillus oryzae (AOL). Oba enzima se imobilizuju na HAP jednostavnom, brzom i efikasnom fizičkom adsorpcijom po mehanizmu metal-koordinatne veze. Kombinovanjem bioinformatičkog pristupa i molekulskog modelovanja za oba enzima su identifikovani i opisani površinski HAP-vezujući motivi.Imobilizacija na HAP je uzrokovala promenu supstratne specifičnosti CRL ka supstratima sa kraćim alkil-nizom i drastično povećanje stabilnosti i aktivnosti enzima u metanolu. Ove karakteristike imobilizata CRL na HAP (CRL-HAP) su prvi put u literaturi primenjene za sintezu metil-acetata, estra sa mirisom jabuke, koga slobodna CRL sintetiše u zanemarljivom prinosu. Pažljivim odabirom rastvarača i supstrata je, takođe po prvi put pokazano kako ovaj popularni i jeftin enzim, u slobodnom ili imobilizovanom obliku, može da se primeni i za efikasnu sintezu kapsinoida direktnom esterifikacijom vanilil-alkohola (VA) i masnih kiselina (MK) i transesterifikacijom kokosovog ulja.Efikasnost imobilizovanog preparata AOL (AOL-HAP) je ispitana u sintezi bioaktivnih supstanci, vanilil-galaktozida (VG) i galakto-oligosaharida (GOS). Po efikasnosti u sintezi ovih proizvoda preparat AOL-HAP se našao u rangu sa kovalentno imobilizovanim preparatima AOL. Jedna ista šarža AOL-HAP može se iskoristiti u 10 uzastopnih reakcionih ciklusa sinteze VG, odnosno GOS, sa poluživotom od 15 h.
AB  - Potential of hydroxyapatite (HAP) as immobilization carrier for industrially important enzymes was examined in a study, comprising of 4 lipases and 4 glycosidases of different origin, structure and substrate specificity. Lipase from Candida rugosa (CRL) and β-galactosidase (lactase) from Aspergillus oryzae (AOL) exhibited the most efficient binding to HAP. Both of the enzymes were immobilized on HAP by simple, fast and efficient physical adsorption through formation of metal-coordinative bond. Furthermore, by the combining of bioinformatic approach and molecular modeling, HAP-speciffic superficial motif on both selected enzymes was identified and described for the first time in the literature.Immobilization on HAP has shifted substrate specificity of CRL towards shorter alkyl-chains, coupled with significant increase in stability and activity of CRL in methanol. These characteristics of immobilized Candida rugosa lipase preparation (CRL-HAP) were sucessfully implemented in synthesis of methyl-acetate, an apple flavour for the first time in the literature. Free CRL synthesized methyl-acetate in very low yield, because of methanol-induced inactivation. By a meticulous selection of organic solvent and susbtrates, it was shown also for the first time that this popular and cost-effective microbial lipase, free or immobilized on HAP, can be used for efficient synthesis of capsinoids in two distinctive reactions: direct esterification of vanillyl-alcohol (VA) with free fatty acids and transesterification of coconut oil.Efficiency of AOL immobilized on HAP (AOL-HAP), was evaluated in synthesis of bioactive compounds: vanillyl-galactoside (VG) and galacto-oligosaccharide (GOS) probiotics. Efficiency of AOL-HAP in synthesis of these compounds was in a good correlation with the procedures in which covalently immobilized AOL was employed. Immobilized AOL preparation can be used in maximum 10 consecutive reaction cycles during VG and GOS synthesis, with the half-life of 15 hours.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj
ER  - 
@phdthesis{
author = "Trbojević Ivić, Jovana",
year = "2019",
abstract = "U ovoj doktorskoj disertaciji je ispitan potencijal HAP za imobilizaciju industrijski značajnih enzima na primeru 4 lipaze i 4 glikozidaze različitog porekla, strukture i supstratne specifičnosti. Od testiranih enzima za HAP se najefikasnije vezuju lipaza iz Candida rugosa (CRL) i β-galaktozidaza (laktaza) iz Aspergillus oryzae (AOL). Oba enzima se imobilizuju na HAP jednostavnom, brzom i efikasnom fizičkom adsorpcijom po mehanizmu metal-koordinatne veze. Kombinovanjem bioinformatičkog pristupa i molekulskog modelovanja za oba enzima su identifikovani i opisani površinski HAP-vezujući motivi.Imobilizacija na HAP je uzrokovala promenu supstratne specifičnosti CRL ka supstratima sa kraćim alkil-nizom i drastično povećanje stabilnosti i aktivnosti enzima u metanolu. Ove karakteristike imobilizata CRL na HAP (CRL-HAP) su prvi put u literaturi primenjene za sintezu metil-acetata, estra sa mirisom jabuke, koga slobodna CRL sintetiše u zanemarljivom prinosu. Pažljivim odabirom rastvarača i supstrata je, takođe po prvi put pokazano kako ovaj popularni i jeftin enzim, u slobodnom ili imobilizovanom obliku, može da se primeni i za efikasnu sintezu kapsinoida direktnom esterifikacijom vanilil-alkohola (VA) i masnih kiselina (MK) i transesterifikacijom kokosovog ulja.Efikasnost imobilizovanog preparata AOL (AOL-HAP) je ispitana u sintezi bioaktivnih supstanci, vanilil-galaktozida (VG) i galakto-oligosaharida (GOS). Po efikasnosti u sintezi ovih proizvoda preparat AOL-HAP se našao u rangu sa kovalentno imobilizovanim preparatima AOL. Jedna ista šarža AOL-HAP može se iskoristiti u 10 uzastopnih reakcionih ciklusa sinteze VG, odnosno GOS, sa poluživotom od 15 h., Potential of hydroxyapatite (HAP) as immobilization carrier for industrially important enzymes was examined in a study, comprising of 4 lipases and 4 glycosidases of different origin, structure and substrate specificity. Lipase from Candida rugosa (CRL) and β-galactosidase (lactase) from Aspergillus oryzae (AOL) exhibited the most efficient binding to HAP. Both of the enzymes were immobilized on HAP by simple, fast and efficient physical adsorption through formation of metal-coordinative bond. Furthermore, by the combining of bioinformatic approach and molecular modeling, HAP-speciffic superficial motif on both selected enzymes was identified and described for the first time in the literature.Immobilization on HAP has shifted substrate specificity of CRL towards shorter alkyl-chains, coupled with significant increase in stability and activity of CRL in methanol. These characteristics of immobilized Candida rugosa lipase preparation (CRL-HAP) were sucessfully implemented in synthesis of methyl-acetate, an apple flavour for the first time in the literature. Free CRL synthesized methyl-acetate in very low yield, because of methanol-induced inactivation. By a meticulous selection of organic solvent and susbtrates, it was shown also for the first time that this popular and cost-effective microbial lipase, free or immobilized on HAP, can be used for efficient synthesis of capsinoids in two distinctive reactions: direct esterification of vanillyl-alcohol (VA) with free fatty acids and transesterification of coconut oil.Efficiency of AOL immobilized on HAP (AOL-HAP), was evaluated in synthesis of bioactive compounds: vanillyl-galactoside (VG) and galacto-oligosaccharide (GOS) probiotics. Efficiency of AOL-HAP in synthesis of these compounds was in a good correlation with the procedures in which covalently immobilized AOL was employed. Immobilized AOL preparation can be used in maximum 10 consecutive reaction cycles during VG and GOS synthesis, with the half-life of 15 hours.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj"
}
Trbojević Ivić, J.. (2019). Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Trbojević Ivić J. Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj. in Универзитет у Београду. 2019;..
Trbojević Ivić, Jovana, "Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj" in Универзитет у Београду (2019).

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases

Trbojević-Ivić, Jovana; Milosavić, Nenad; Dimitrijević, Aleksandra; Gavrović-Jankulović, Marija; Bezbradica, Dejan; Kolarski, Dušan; Veličković, Dušan

(Elsevier Sci Ltd, Oxford, 2017)

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://cherry.chem.bg.ac.rs/handle/123456789/3102
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 . .
12
8
9

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases

Trbojević-Ivić, Jovana; Milosavić, Nenad; Dimitrijević, Aleksandra; Gavrović-Jankulović, Marija; Bezbradica, Dejan; Kolarski, Dušan; Veličković, Dušan

(Elsevier Sci Ltd, Oxford, 2017)

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://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
UR  - Kon_3154
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",
url = "Kon_3154"
}
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
Kon_3154
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
Kon_3154 .
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 .,
Kon_3154 .
12
8
9

Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports

Mihailović, Mladen; Trbojević-Ivić, Jovana; Banjanac, Katarina; Milosavić, Nenad; Veličković, Dušan; Carević, Milica; Bezbradica, Dejan

(Serbian Chemical Soc, Belgrade, 2016)

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  - http://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
UR  - Kon_3207
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",
url = "Kon_3207"
}
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
Kon_3207
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
Kon_3207 .
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 .,
Kon_3207 .

Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry

Trbojević-Ivić, Jovana; Veličković, Dušan; Dimitrijević, Aleksandra; Bezbradica, Dejan; Dragacevic, Vladimir; Gavrović-Jankulović, Marija; Milosavić, Nenad

(Wiley-Blackwell, Hoboken, 2016)

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  - http://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
UR  - Kon_3062
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",
url = "Kon_3062"
}
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
Kon_3062
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
Kon_3062 .
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 .,
Kon_3062 .
21
17
20

Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling

Trbojević-Ivić, Jovana; Dimitrijević, Aleksandra; Milosavić, Nenad; Bezbradica, Dejan; Drakulić, Branko J.; Gavrović-Jankulović, Marija; Pavlović, Marija; Rogniaux, Helene; Veličković, Dušan

(Royal Soc Chemistry, Cambridge, 2016)

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  - http://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
UR  - Kon_3033
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",
url = "Kon_3033"
}
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
Kon_3033
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
Kon_3033 .
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 .,
Kon_3033 .
6
6
6

The specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation

Dusan, Velickovic; Nenad, Milosavic; Dejan, Bezbradica; Bihelović, Filip; Segal, Ann Marie; Šegan, Dejan M.; Trbojević-Ivić, Jovana; Aleksandra, Dimitrijevic

(Springer, New York, 2014)

TY  - JOUR
AU  - Dusan, Velickovic
AU  - Nenad, Milosavic
AU  - Dejan, Bezbradica
AU  - Bihelović, Filip
AU  - Segal, Ann Marie
AU  - Šegan, Dejan M.
AU  - Trbojević-Ivić, Jovana
AU  - Aleksandra, Dimitrijevic
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1797
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
VL  - 98
IS  - 14
SP  - 6317
EP  - 6328
DO  - 10.1007/s00253-014-5587-9
UR  - Kon_2680
ER  - 
@article{
author = "Dusan, Velickovic and Nenad, Milosavic and Dejan, Bezbradica and Bihelović, Filip and Segal, Ann Marie and Šegan, Dejan M. and Trbojević-Ivić, Jovana and Aleksandra, Dimitrijevic",
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",
volume = "98",
number = "14",
pages = "6317-6328",
doi = "10.1007/s00253-014-5587-9",
url = "Kon_2680"
}
Dusan, V., Nenad, M., Dejan, B., Bihelović, F., Segal, A. M., Šegan, D. M., Trbojević-Ivić, J.,& Aleksandra, D.. (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
Kon_2680
Dusan V, Nenad M, Dejan B, Bihelović F, Segal AM, Šegan DM, Trbojević-Ivić J, Aleksandra D. 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
Kon_2680 .
Dusan, Velickovic, Nenad, Milosavic, Dejan, Bezbradica, Bihelović, Filip, Segal, Ann Marie, Šegan, Dejan M., Trbojević-Ivić, Jovana, Aleksandra, Dimitrijevic, "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 .,
Kon_2680 .
2
1
2

Isolation of Candida rugosa lipase isoforms

Trbojević-Ivić, Jovana; Dimitrijević, Aleksandra; Veličković, Dušan; Gavrović-Jankulović, Marija; Milosavić, Nenad

(Assoc Chemists & Chemical Engineers Of Serbia, Belgrade, 2013)

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1456
AB  - The yeast Candida rugosa is a convenient source of lipases for science and industry. Crude preparation of Candida rugosa lipase (CRL) consists of several extracellular lipases. Isoenzyme profile depends on the culture or fermentation conditions. All isoforms are coded by the lip pseudogene family; they are monomers of 534 amino acids and molecular weight of about 60 kDa. They share the same catalytic mechanism and interfacial mode of activation. Isoenzymes differ in isoelectric points, post-translational modifications, substrate specificity and hydrophobicity. The presence of different lipase isoforms and other substances (i.e., inhibitors) in crude preparation leads to lack of their productivity in biocatalytic reactions. Purification of specific isoform improves its overall performance and stability. This paper provides an overview of different methods for purification of CRL isoenzymes up to date, their advantages and disadvantages.
AB  - Lipaze (hidrolaze estara glicerola, E.C.3.1.3.3) su važna grupa enzima, široko rasprostranjenih u prirodi. Mogu se izolovati iz materijala biljnog, životinjskog ili mikrobnog porekla. Zahvaljujući svojim karakteristikama, pobuđuju sve više pažnje kao efikasni biokatalizatori u različitim sintetičkim i hidrolitičkim procesima. Među lipazama, poreklom iz mikroorganizama, posebno su značajne one koje produkuje kvasac Candida rugosa. Komercijalni preparat lipaza iz C. rugosa može sadržati 5-7 izoformi ekstracelularnih lipaza. Sve te izoforme kodirane su od strane lip familije pseudogena, a na njihovu ekspresiju utiču uslovi u kojima se mikroorganizam gaji (sastav hranljive podloge je najvažniji). Ekstracelularne lipaze, koje proizvodi C. rugosa su monomerni glikoproteini, molekulske mase od oko 60 kDa, sa 534 aminokiseline. Za sve izoforme je karakterističan isti složeni mehanizam aktivacije na granici faza i mehanizam katalize, kakav se sreće i kod serin-proteaza. Izoenzimi se međusobno razlikuju po post-translacionim modifikacijama (udelu ugljohidratne komponente), supstratnoj specifičnosti, izoelektričnim tačkama i hidrofobnosti. Prisustvo više izoformi lipaza u komercijalnom preparatu utiče na njihovu produktivnost u reakcijama koje katalizuju. Takvi preparati često sadrže i druge supstance koje mogu uticati na aktivnost enzima (na primer inhibitore). Razdvajanjem pojedinačnih izoformi iz komercijalnog preparata poboljšavaju se njihova enantioselektivnost, specifična aktivnost i stabilnost enzima, što je od izuzetnog značaja za njihovu dalju primenu. U ovom radu su predstavljeni različiti pristupi u razdvajanju pojedinačnih izoformi vanćelijskih lipaza iz komercijalnog preparata C. rugosa, njihove prednosti i nedostaci.
PB  - Assoc Chemists & Chemical Engineers Of Serbia, Belgrade
T2  - Hemijska industrija
T1  - Isolation of Candida rugosa lipase isoforms
T1  - Izolovanje izoformi lipaze iz Candida rugosa
VL  - 67
IS  - 5
SP  - 703
EP  - 706
DO  - 10.2298/HEMIND120828113T
UR  - Kon_2576
ER  - 
@article{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Veličković, Dušan and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2013",
abstract = "The yeast Candida rugosa is a convenient source of lipases for science and industry. Crude preparation of Candida rugosa lipase (CRL) consists of several extracellular lipases. Isoenzyme profile depends on the culture or fermentation conditions. All isoforms are coded by the lip pseudogene family; they are monomers of 534 amino acids and molecular weight of about 60 kDa. They share the same catalytic mechanism and interfacial mode of activation. Isoenzymes differ in isoelectric points, post-translational modifications, substrate specificity and hydrophobicity. The presence of different lipase isoforms and other substances (i.e., inhibitors) in crude preparation leads to lack of their productivity in biocatalytic reactions. Purification of specific isoform improves its overall performance and stability. This paper provides an overview of different methods for purification of CRL isoenzymes up to date, their advantages and disadvantages., Lipaze (hidrolaze estara glicerola, E.C.3.1.3.3) su važna grupa enzima, široko rasprostranjenih u prirodi. Mogu se izolovati iz materijala biljnog, životinjskog ili mikrobnog porekla. Zahvaljujući svojim karakteristikama, pobuđuju sve više pažnje kao efikasni biokatalizatori u različitim sintetičkim i hidrolitičkim procesima. Među lipazama, poreklom iz mikroorganizama, posebno su značajne one koje produkuje kvasac Candida rugosa. Komercijalni preparat lipaza iz C. rugosa može sadržati 5-7 izoformi ekstracelularnih lipaza. Sve te izoforme kodirane su od strane lip familije pseudogena, a na njihovu ekspresiju utiču uslovi u kojima se mikroorganizam gaji (sastav hranljive podloge je najvažniji). Ekstracelularne lipaze, koje proizvodi C. rugosa su monomerni glikoproteini, molekulske mase od oko 60 kDa, sa 534 aminokiseline. Za sve izoforme je karakterističan isti složeni mehanizam aktivacije na granici faza i mehanizam katalize, kakav se sreće i kod serin-proteaza. Izoenzimi se međusobno razlikuju po post-translacionim modifikacijama (udelu ugljohidratne komponente), supstratnoj specifičnosti, izoelektričnim tačkama i hidrofobnosti. Prisustvo više izoformi lipaza u komercijalnom preparatu utiče na njihovu produktivnost u reakcijama koje katalizuju. Takvi preparati često sadrže i druge supstance koje mogu uticati na aktivnost enzima (na primer inhibitore). Razdvajanjem pojedinačnih izoformi iz komercijalnog preparata poboljšavaju se njihova enantioselektivnost, specifična aktivnost i stabilnost enzima, što je od izuzetnog značaja za njihovu dalju primenu. U ovom radu su predstavljeni različiti pristupi u razdvajanju pojedinačnih izoformi vanćelijskih lipaza iz komercijalnog preparata C. rugosa, njihove prednosti i nedostaci.",
publisher = "Assoc Chemists & Chemical Engineers Of Serbia, Belgrade",
journal = "Hemijska industrija",
title = "Isolation of Candida rugosa lipase isoforms, Izolovanje izoformi lipaze iz Candida rugosa",
volume = "67",
number = "5",
pages = "703-706",
doi = "10.2298/HEMIND120828113T",
url = "Kon_2576"
}
Trbojević-Ivić, J., Dimitrijević, A., Veličković, D., Gavrović-Jankulović, M.,& Milosavić, N.. (2013). Isolation of Candida rugosa lipase isoforms. in Hemijska industrija
Assoc Chemists & Chemical Engineers Of Serbia, Belgrade., 67(5), 703-706.
https://doi.org/10.2298/HEMIND120828113T
Kon_2576
Trbojević-Ivić J, Dimitrijević A, Veličković D, Gavrović-Jankulović M, Milosavić N. Isolation of Candida rugosa lipase isoforms. in Hemijska industrija. 2013;67(5):703-706.
doi:10.2298/HEMIND120828113T
Kon_2576 .
Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, Veličković, Dušan, Gavrović-Jankulović, Marija, Milosavić, Nenad, "Isolation of Candida rugosa lipase isoforms" in Hemijska industrija, 67, no. 5 (2013):703-706,
https://doi.org/10.2298/HEMIND120828113T .,
Kon_2576 .
7
5
6

A study of transglucosylation kinetic in an enzymatic synthesis of benzyl alcohol glucoside by alpha-glucosidase from S-cerevisiae

Pavlović, Marijana; Dimitrijevic, A.; Trbojević-Ivić, Jovana; Milosavic, N.; Gavrović-Jankulović, Marija; Bezbradica, Dejan; Velickovic, D.

(Maik Nauka/Interperiodica/Springer, New York, 2013)

TY  - JOUR
AU  - Pavlović, Marijana
AU  - Dimitrijevic, A.
AU  - Trbojević-Ivić, Jovana
AU  - Milosavic, N.
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Velickovic, D.
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1432
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
VL  - 87
IS  - 13
SP  - 2285
EP  - 2288
DO  - 10.1134/S0036024413130207
UR  - Kon_2552
ER  - 
@article{
author = "Pavlović, Marijana and Dimitrijevic, A. and Trbojević-Ivić, Jovana and Milosavic, N. and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Velickovic, D.",
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",
volume = "87",
number = "13",
pages = "2285-2288",
doi = "10.1134/S0036024413130207",
url = "Kon_2552"
}
Pavlović, M., Dimitrijevic, A., Trbojević-Ivić, J., Milosavic, N., Gavrović-Jankulović, M., Bezbradica, D.,& Velickovic, 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
Kon_2552
Pavlović M, Dimitrijevic A, Trbojević-Ivić J, Milosavic N, Gavrović-Jankulović M, Bezbradica D, Velickovic 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
Kon_2552 .
Pavlović, Marijana, Dimitrijevic, A., Trbojević-Ivić, Jovana, Milosavic, N., Gavrović-Jankulović, Marija, Bezbradica, Dejan, Velickovic, 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, 87, no. 13 (2013):2285-2288,
https://doi.org/10.1134/S0036024413130207 .,
Kon_2552 .
3
3
3