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  - https://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
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"
}

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

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 .

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 . .

TY  - JOUR
AU  - Velickovic, D. V.
AU  - Dimitrijevic, A. S.
AU  - Bihelović, Filip
AU  - Jankov, Ratko M.
AU  - Milosavic, N.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1231
AB  - One of the key elements for understanding enzyme reactions is determination of its kinetic parameters. Since transglucosylation is kinetically controlled reaction, besides the reaction of synthesis, very important is the reaction of enzymatic hydrolysis of created product. Therefore, in this study, kinetic parameters for synthesis and secondary hydrolysis of pharmacologically active alpha isosalicin by baker's yeast maltase were calculated, and it was shown that specifity of maltase for hydrolysis is approximately 150 times higher then for synthesis.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Russian Journal of Physical Chemistry A
T1  - Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase
VL  - 85
IS  - 13
SP  - 2317
EP  - 2321
DO  - 10.1134/S0036024411130346
ER  - 

@article{
author = "Velickovic, D. V. and Dimitrijevic, A. S. and Bihelović, Filip and Jankov, Ratko M. and Milosavic, N.",
year = "2011",
abstract = "One of the key elements for understanding enzyme reactions is determination of its kinetic parameters. Since transglucosylation is kinetically controlled reaction, besides the reaction of synthesis, very important is the reaction of enzymatic hydrolysis of created product. Therefore, in this study, kinetic parameters for synthesis and secondary hydrolysis of pharmacologically active alpha isosalicin by baker's yeast maltase were calculated, and it was shown that specifity of maltase for hydrolysis is approximately 150 times higher then for synthesis.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Russian Journal of Physical Chemistry A",
title = "Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase",
volume = "85",
number = "13",
pages = "2317-2321",
doi = "10.1134/S0036024411130346"
}

Velickovic, D. V., Dimitrijevic, A. S., Bihelović, F., Jankov, R. M.,& Milosavic, N.. (2011). Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase. in Russian Journal of Physical Chemistry A
Maik Nauka/Interperiodica/Springer, New York., 85(13), 2317-2321.
https://doi.org/10.1134/S0036024411130346

Velickovic DV, Dimitrijevic AS, Bihelović F, Jankov RM, Milosavic N. Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase. in Russian Journal of Physical Chemistry A. 2011;85(13):2317-2321.
doi:10.1134/S0036024411130346 .

Velickovic, D. V., Dimitrijevic, A. S., Bihelović, Filip, Jankov, Ratko M., Milosavic, N., "Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase" in Russian Journal of Physical Chemistry A, 85, no. 13 (2011):2317-2321,
https://doi.org/10.1134/S0036024411130346 . .

TY  - JOUR
AU  - Milosavic, N.
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan
AU  - Vujčić, Zoran
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/826
AB  - We succeeded in the immobilization of 190 mg of periodate oxidized glucoamylase per gram of macroporous polymer. The covalently immobilized enzyme had a specific activity of 1100 U/g. The temperature and pH optimum as well as kinetic parameters were determined. The immobilized enzyme was tested in different types of reactors for hydrolysis of concentrated maltose and starch hydrolysate syrups. The DE value of 98.6, obtained the immobilized enzyme, was slightly higher than that for the soluble form, when acting on 20% substrates. During continuous use in a packed bed reactor over a period of 4 weeks the immobilized enzyme produced 1300 kg of glucose per 1 L of reactor volume without any decrease in its activity. (c) 2006 Elsevier Inc. All rights reserved.
PB  - Elsevier Science Inc, New York
T2  - Enzyme and Microbial Technology
T1  - Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)
VL  - 40
IS  - 5
SP  - 1422
EP  - 1426
DO  - 10.1016/j.enzmictec.2006.10.018
ER  - 

@article{
author = "Milosavic, N. and Prodanović, Radivoje and Jovanović, Slobodan and Vujčić, Zoran",
year = "2007",
abstract = "We succeeded in the immobilization of 190 mg of periodate oxidized glucoamylase per gram of macroporous polymer. The covalently immobilized enzyme had a specific activity of 1100 U/g. The temperature and pH optimum as well as kinetic parameters were determined. The immobilized enzyme was tested in different types of reactors for hydrolysis of concentrated maltose and starch hydrolysate syrups. The DE value of 98.6, obtained the immobilized enzyme, was slightly higher than that for the soluble form, when acting on 20% substrates. During continuous use in a packed bed reactor over a period of 4 weeks the immobilized enzyme produced 1300 kg of glucose per 1 L of reactor volume without any decrease in its activity. (c) 2006 Elsevier Inc. All rights reserved.",
publisher = "Elsevier Science Inc, New York",
journal = "Enzyme and Microbial Technology",
title = "Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)",
volume = "40",
number = "5",
pages = "1422-1426",
doi = "10.1016/j.enzmictec.2006.10.018"
}

Milosavic, N., Prodanović, R., Jovanović, S.,& Vujčić, Z.. (2007). Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). in Enzyme and Microbial Technology
Elsevier Science Inc, New York., 40(5), 1422-1426.
https://doi.org/10.1016/j.enzmictec.2006.10.018

Milosavic N, Prodanović R, Jovanović S, Vujčić Z. Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). in Enzyme and Microbial Technology. 2007;40(5):1422-1426.
doi:10.1016/j.enzmictec.2006.10.018 .

Milosavic, N., Prodanović, Radivoje, Jovanović, Slobodan, Vujčić, Zoran, "Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)" in Enzyme and Microbial Technology, 40, no. 5 (2007):1422-1426,
https://doi.org/10.1016/j.enzmictec.2006.10.018 . .

TY  - JOUR
AU  - Milosavic, N
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan
AU  - Novaković, Irena T.
AU  - Vujčić, Zoran
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/717
AB  - Amyloglucosidase from A. niger was covalently immobilized onto poly(GMA-co-EGDMA) by the glutaraldehyde and periodate method. The immobilization of amyloglucosidase after periodate oxidation gave a preparate with the highest specific activity reported so far on similar polymers. The obtained immobilized preparates show the same pH optimum, but a higher temperature optimum compared with the soluble enzyme. The kinetic parameters for the hydrolysis of soluble starch by free and both immobilized enzymes were determined.
AB  - Amiloglukozidaza iz A.niger je imobilizovana na poly(GMA-co-EGDMA) glutaraldehidnom i perjodatnom metodom. Imobilizacija amiloglukozidaze nakon perjodatne oksidacije daje preparat sa najvećom do sada objavljenom specifičnom aktivnosti na sličnim polimerima. Dobijeni imobilizovani preparat ima isti pH optimum ali povećani termooptimum u poređenju sa rastvornim enzimom. Određeni su i kinetički parametri za hidrolizu rastvornog skroba imobilizovanim kao i rastvornim enzimom.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and characterization of two types of covalently immobilized amyloglucosidase
T1  - Dobijanje i karakterizacija dva tipa imobilizovane amiloglukozidaze
VL  - 70
IS  - 5
SP  - 713
EP  - 719
DO  - 10.2298/JSC0505713M
ER  - 

@article{
author = "Milosavic, N and Prodanović, Radivoje and Jovanović, Slobodan and Novaković, Irena T. and Vujčić, Zoran",
year = "2005",
abstract = "Amyloglucosidase from A. niger was covalently immobilized onto poly(GMA-co-EGDMA) by the glutaraldehyde and periodate method. The immobilization of amyloglucosidase after periodate oxidation gave a preparate with the highest specific activity reported so far on similar polymers. The obtained immobilized preparates show the same pH optimum, but a higher temperature optimum compared with the soluble enzyme. The kinetic parameters for the hydrolysis of soluble starch by free and both immobilized enzymes were determined., Amiloglukozidaza iz A.niger je imobilizovana na poly(GMA-co-EGDMA) glutaraldehidnom i perjodatnom metodom. Imobilizacija amiloglukozidaze nakon perjodatne oksidacije daje preparat sa najvećom do sada objavljenom specifičnom aktivnosti na sličnim polimerima. Dobijeni imobilizovani preparat ima isti pH optimum ali povećani termooptimum u poređenju sa rastvornim enzimom. Određeni su i kinetički parametri za hidrolizu rastvornog skroba imobilizovanim kao i rastvornim enzimom.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and characterization of two types of covalently immobilized amyloglucosidase, Dobijanje i karakterizacija dva tipa imobilizovane amiloglukozidaze",
volume = "70",
number = "5",
pages = "713-719",
doi = "10.2298/JSC0505713M"
}

Milosavic, N., Prodanović, R., Jovanović, S., Novaković, I. T.,& Vujčić, Z.. (2005). Preparation and characterization of two types of covalently immobilized amyloglucosidase. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 70(5), 713-719.
https://doi.org/10.2298/JSC0505713M

Milosavic N, Prodanović R, Jovanović S, Novaković IT, Vujčić Z. Preparation and characterization of two types of covalently immobilized amyloglucosidase. in Journal of the Serbian Chemical Society. 2005;70(5):713-719.
doi:10.2298/JSC0505713M .

Milosavic, N, Prodanović, Radivoje, Jovanović, Slobodan, Novaković, Irena T., Vujčić, Zoran, "Preparation and characterization of two types of covalently immobilized amyloglucosidase" in Journal of the Serbian Chemical Society, 70, no. 5 (2005):713-719,
https://doi.org/10.2298/JSC0505713M . .

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Milosavic, N
AU  - Sladić, Dušan
AU  - Zlatović, Mario
AU  - Božić, Bojana
AU  - Ćirković-Veličković, Tanja
AU  - Vujčić, Zoran
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/728
AB  - Hydroquinone alpha-isomaltoside and hydroquinone alpha-glucoside were synthesized by transglucosylation in an aqueous system with baker's yeast alpha-glucosidase from hydroquinone and maltose as a glucosyl donor. Only one phenolic group was glucosylated, with alpha-selectivity, and the nature of the reaction products was governed by the concentration of hydroquinone. The optimal conditions for synthesis of glycosides were 9 mM hydroquinone and 1.5 M maltose in a 100 mM sodium citrate/phosphate buffer at pH 5.0 and 30 degrees C for 20 h. Under these conditions both hydroquinone alpha-glycosides were obtained in nearly equimolar amounts with a total molar yield of 28% with respect to hydroquinone and a total glycoside concentration of 1 mg/mL in the reaction mixture. (c) 2005 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Transglucosylation of hydroquinone catalysed by alpha-glucosidase from baker's yeast
VL  - 35
IS  - 4-6
SP  - 142
EP  - 146
DO  - 10.1016/j.molcatb.2005.06.011
ER  - 

@article{
author = "Prodanović, Radivoje and Milosavic, N and Sladić, Dušan and Zlatović, Mario and Božić, Bojana and Ćirković-Veličković, Tanja and Vujčić, Zoran",
year = "2005",
abstract = "Hydroquinone alpha-isomaltoside and hydroquinone alpha-glucoside were synthesized by transglucosylation in an aqueous system with baker's yeast alpha-glucosidase from hydroquinone and maltose as a glucosyl donor. Only one phenolic group was glucosylated, with alpha-selectivity, and the nature of the reaction products was governed by the concentration of hydroquinone. The optimal conditions for synthesis of glycosides were 9 mM hydroquinone and 1.5 M maltose in a 100 mM sodium citrate/phosphate buffer at pH 5.0 and 30 degrees C for 20 h. Under these conditions both hydroquinone alpha-glycosides were obtained in nearly equimolar amounts with a total molar yield of 28% with respect to hydroquinone and a total glycoside concentration of 1 mg/mL in the reaction mixture. (c) 2005 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Transglucosylation of hydroquinone catalysed by alpha-glucosidase from baker's yeast",
volume = "35",
number = "4-6",
pages = "142-146",
doi = "10.1016/j.molcatb.2005.06.011"
}

Prodanović, R., Milosavic, N., Sladić, D., Zlatović, M., Božić, B., Ćirković-Veličković, T.,& Vujčić, Z.. (2005). Transglucosylation of hydroquinone catalysed by alpha-glucosidase from baker's yeast. in Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam., 35(4-6), 142-146.
https://doi.org/10.1016/j.molcatb.2005.06.011

Prodanović R, Milosavic N, Sladić D, Zlatović M, Božić B, Ćirković-Veličković T, Vujčić Z. Transglucosylation of hydroquinone catalysed by alpha-glucosidase from baker's yeast. in Journal of Molecular Catalysis. B: Enzymatic. 2005;35(4-6):142-146.
doi:10.1016/j.molcatb.2005.06.011 .

Prodanović, Radivoje, Milosavic, N, Sladić, Dušan, Zlatović, Mario, Božić, Bojana, Ćirković-Veličković, Tanja, Vujčić, Zoran, "Transglucosylation of hydroquinone catalysed by alpha-glucosidase from baker's yeast" in Journal of Molecular Catalysis. B: Enzymatic, 35, no. 4-6 (2005):142-146,
https://doi.org/10.1016/j.molcatb.2005.06.011 . .

TY  - JOUR
AU  - Novaković, Irena T.
AU  - Vujčić, Zoran
AU  - Božić, Tatjana T.
AU  - Božić, Nataša
AU  - Milosavic, N
AU  - Sladić, Dušan
PY  - 2003
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/552
AB  - The avarone/avarol quinone/hydroquinone couple. as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of beta-lactogglobulin. isolated from cow milk by avarone, its model compound 2-tert-butyl-1,4-benzoquinone. and several of their alkylthio derivatives were studied. The techniques applied for as-saying the modifications were: UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of die reaction of beta-lactoglobulin with the quinones.
AB  - Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima pokazuje da su amino grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of beta-lactoglobulin by quinones
T1  - Hemijske modifikacije β-laktoglobulina hinonima
VL  - 68
IS  - 4-5
SP  - 243
EP  - 248
DO  - 10.2298/JSC0305243N
ER  - 

@article{
author = "Novaković, Irena T. and Vujčić, Zoran and Božić, Tatjana T. and Božić, Nataša and Milosavic, N and Sladić, Dušan",
year = "2003",
abstract = "The avarone/avarol quinone/hydroquinone couple. as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of beta-lactogglobulin. isolated from cow milk by avarone, its model compound 2-tert-butyl-1,4-benzoquinone. and several of their alkylthio derivatives were studied. The techniques applied for as-saying the modifications were: UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of die reaction of beta-lactoglobulin with the quinones., Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima pokazuje da su amino grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of beta-lactoglobulin by quinones, Hemijske modifikacije β-laktoglobulina hinonima",
volume = "68",
number = "4-5",
pages = "243-248",
doi = "10.2298/JSC0305243N"
}

Novaković, I. T., Vujčić, Z., Božić, T. T., Božić, N., Milosavic, N.,& Sladić, D.. (2003). Chemical modification of beta-lactoglobulin by quinones. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 68(4-5), 243-248.
https://doi.org/10.2298/JSC0305243N

Novaković IT, Vujčić Z, Božić TT, Božić N, Milosavic N, Sladić D. Chemical modification of beta-lactoglobulin by quinones. in Journal of the Serbian Chemical Society. 2003;68(4-5):243-248.
doi:10.2298/JSC0305243N .

Novaković, Irena T., Vujčić, Zoran, Božić, Tatjana T., Božić, Nataša, Milosavic, N, Sladić, Dušan, "Chemical modification of beta-lactoglobulin by quinones" in Journal of the Serbian Chemical Society, 68, no. 4-5 (2003):243-248,
https://doi.org/10.2298/JSC0305243N . .