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  - Jovanović, Slobodan
AU  - Vujčić, Zoran
PY  - 2001
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/464
AB  - Invertase was immobilized via its carbohydrate moiety. The immobilized enzyme has a specific activity of 5500 IU g(-1), with 45% activity yield on immobilization. In a packed bed reactor, 90% 2.5 M sucrose was converted at a flow rate of 4 bed volumes h(-1). The obtained specific productivity at 40 degreesC of 3 kg l(-1) h(-1) is the best one so far. Long-term stability was 290 days in 2.5 M sucrose at 40 degreesC and at a flow rate of 3 bed volumes h(-1).
PB  - Kluwer Academic Publ, Dordrecht
T2  - Biotechnology Letters
T1  - Immobilization of invertase on a new type of macroporous glycidyl methacrylate
VL  - 23
IS  - 14
SP  - 1171
EP  - 1174
DO  - 10.1023/A:1010560911400
ER  - 

@article{
author = "Prodanović, Radivoje and Jovanović, Slobodan and Vujčić, Zoran",
year = "2001",
abstract = "Invertase was immobilized via its carbohydrate moiety. The immobilized enzyme has a specific activity of 5500 IU g(-1), with 45% activity yield on immobilization. In a packed bed reactor, 90% 2.5 M sucrose was converted at a flow rate of 4 bed volumes h(-1). The obtained specific productivity at 40 degreesC of 3 kg l(-1) h(-1) is the best one so far. Long-term stability was 290 days in 2.5 M sucrose at 40 degreesC and at a flow rate of 3 bed volumes h(-1).",
publisher = "Kluwer Academic Publ, Dordrecht",
journal = "Biotechnology Letters",
title = "Immobilization of invertase on a new type of macroporous glycidyl methacrylate",
volume = "23",
number = "14",
pages = "1171-1174",
doi = "10.1023/A:1010560911400"
}

Prodanović, R., Jovanović, S.,& Vujčić, Z.. (2001). Immobilization of invertase on a new type of macroporous glycidyl methacrylate. in Biotechnology Letters
Kluwer Academic Publ, Dordrecht., 23(14), 1171-1174.
https://doi.org/10.1023/A:1010560911400

Prodanović R, Jovanović S, Vujčić Z. Immobilization of invertase on a new type of macroporous glycidyl methacrylate. in Biotechnology Letters. 2001;23(14):1171-1174.
doi:10.1023/A:1010560911400 .

Prodanović, Radivoje, Jovanović, Slobodan, Vujčić, Zoran, "Immobilization of invertase on a new type of macroporous glycidyl methacrylate" in Biotechnology Letters, 23, no. 14 (2001):1171-1174,
https://doi.org/10.1023/A:1010560911400 . .