Milosavić, Nenad B.

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  • Milosavić, Nenad B. (3)
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Author's Bibliography

Covalent immobilization of lipase from Candida rugosa on Eupergit®

Bezbradica, Dejan; Ćorović, Jasmina J.; Prodanović, Radivoje; Milosavić, Nenad B.; Knežević, Zorica D.

(2005)

TY  - JOUR
AU  - Bezbradica, Dejan
AU  - Ćorović, Jasmina J.
AU  - Prodanović, Radivoje
AU  - Milosavić, Nenad B.
AU  - Knežević, Zorica D.
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/210
AB  - An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit® with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit® among methods applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme.
AB  - U ovom radu je ispitana mogućnost primene metode za kovalentno vezivanje lipaze iz Candida rugosa za komercijalni polimerni nosač Eupergit® kojom se dobijaju stabilni i aktivni imobilisani enzimi. Vezivanje se odvija preko ugljenohidratne komponente enzima, koja je prethodno modifikovana oksidacijom pomoću perjodata, a ne preko proteinske komponente, koja je važna za katalitičku aktivnost enzima. Hidrolitička aktivnost na ovaj način imobilisane lipaze upoređena je sa aktivnostima lipaza koje su imobilisane pomoću dve konvencionalne metode (vezivanje preko epoksidnih grupa nosača i vezivanje za nosač modifikovan glutaraldehidom). Rezultati ovog istraživanja pokazuju da je perjodatna metoda pogodnija za imobilizaciju lipaze na Eupergit® sa oba ispitivana aspekta: prinosa imobilizacije i hidrolitičke aktivnosti imobilisanog enzima.
T2  - Acta periodica technologica
T1  - Covalent immobilization of lipase from Candida rugosa on Eupergit®
T1  - Kovalentna imobilizacija lipaze iz Candida rugosa za Eupergit®
IS  - 36
SP  - 179
EP  - 186
DO  - 10.2298/APT0536179B
UR  - Kon_141
ER  - 
@article{
author = "Bezbradica, Dejan and Ćorović, Jasmina J. and Prodanović, Radivoje and Milosavić, Nenad B. and Knežević, Zorica D.",
year = "2005",
abstract = "An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit® with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit® among methods applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme., U ovom radu je ispitana mogućnost primene metode za kovalentno vezivanje lipaze iz Candida rugosa za komercijalni polimerni nosač Eupergit® kojom se dobijaju stabilni i aktivni imobilisani enzimi. Vezivanje se odvija preko ugljenohidratne komponente enzima, koja je prethodno modifikovana oksidacijom pomoću perjodata, a ne preko proteinske komponente, koja je važna za katalitičku aktivnost enzima. Hidrolitička aktivnost na ovaj način imobilisane lipaze upoređena je sa aktivnostima lipaza koje su imobilisane pomoću dve konvencionalne metode (vezivanje preko epoksidnih grupa nosača i vezivanje za nosač modifikovan glutaraldehidom). Rezultati ovog istraživanja pokazuju da je perjodatna metoda pogodnija za imobilizaciju lipaze na Eupergit® sa oba ispitivana aspekta: prinosa imobilizacije i hidrolitičke aktivnosti imobilisanog enzima.",
journal = "Acta periodica technologica",
title = "Covalent immobilization of lipase from Candida rugosa on Eupergit®, Kovalentna imobilizacija lipaze iz Candida rugosa za Eupergit®",
number = "36",
pages = "179-186",
doi = "10.2298/APT0536179B",
url = "Kon_141"
}
Bezbradica, D., Ćorović, J. J., Prodanović, R., Milosavić, N. B.,& Knežević, Z. D.. (2005). Covalent immobilization of lipase from Candida rugosa on Eupergit®. in Acta periodica technologica(36), 179-186.
https://doi.org/10.2298/APT0536179B
Kon_141
Bezbradica D, Ćorović JJ, Prodanović R, Milosavić NB, Knežević ZD. Covalent immobilization of lipase from Candida rugosa on Eupergit®. in Acta periodica technologica. 2005;(36):179-186.
doi:10.2298/APT0536179B
Kon_141 .
Bezbradica, Dejan, Ćorović, Jasmina J., Prodanović, Radivoje, Milosavić, Nenad B., Knežević, Zorica D., "Covalent immobilization of lipase from Candida rugosa on Eupergit®" in Acta periodica technologica, no. 36 (2005):179-186,
https://doi.org/10.2298/APT0536179B .,
Kon_141 .
1

Porosom: A new cell structure

Milosavić, Nenad B.; Prodanović, Radivoje

(2004)

TY  - JOUR
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje
PY  - 2004
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/251
AB  - The discovery of porosome and elucidation of its morphology, dynamics, and composition, reveled where membrane-bound secretory vesicles dock and fuse to release their contents. How membrane-bounded secretori vesicles fuse at plasa membrane-associated porosome has also been eluciated. This discovery has also revealed how little we know about the cell, and thus heralds a new revolution in cell biology, i.e. the birth of nano cell biology.
T2  - Hemijski pregled
T1  - Porosom: A new cell structure
T1  - Porozom - nova ćelijska struktura
VL  - 45
IS  - 5
SP  - 102
EP  - 103
UR  - https://hdl.handle.net/21.15107/rcub_cherry_251
UR  - Kon_488
ER  - 
@article{
author = "Milosavić, Nenad B. and Prodanović, Radivoje",
year = "2004",
abstract = "The discovery of porosome and elucidation of its morphology, dynamics, and composition, reveled where membrane-bound secretory vesicles dock and fuse to release their contents. How membrane-bounded secretori vesicles fuse at plasa membrane-associated porosome has also been eluciated. This discovery has also revealed how little we know about the cell, and thus heralds a new revolution in cell biology, i.e. the birth of nano cell biology.",
journal = "Hemijski pregled",
title = "Porosom: A new cell structure, Porozom - nova ćelijska struktura",
volume = "45",
number = "5",
pages = "102-103",
url = "https://hdl.handle.net/21.15107/rcub_cherry_251, Kon_488"
}
Milosavić, N. B.,& Prodanović, R.. (2004). Porosom: A new cell structure. in Hemijski pregled, 45(5), 102-103.
https://hdl.handle.net/21.15107/rcub_cherry_251
Milosavić NB, Prodanović R. Porosom: A new cell structure. in Hemijski pregled. 2004;45(5):102-103.
https://hdl.handle.net/21.15107/rcub_cherry_251 .
Milosavić, Nenad B., Prodanović, Radivoje, "Porosom: A new cell structure" in Hemijski pregled, 45, no. 5 (2004):102-103,
https://hdl.handle.net/21.15107/rcub_cherry_251 .

Immobilization of glucoamylase on macroporous spheres

Milosavić, Nenad B.; Prodanović, Radivoje; Jovanović, Slobodan M.; Vujčić, Zoran

(2004)

TY  - JOUR
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan M.
AU  - Vujčić, Zoran
PY  - 2004
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/209
AB  - Glucoamylase was covalently immobilized through the spacer-arm of the poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) spheres by using a glutaraldehyde as a coupling agent. The influence of the enzyme load applied to the support on immobilization, yield and specific activity, has been determined. Obtained specific activity was 700 U/g with immobilization yield of 35 %. The Km value for immobilized glucoamylase was 1.28 % (w/v), pH and temperature optimum were 4.5 and 70°C, respectively. The conversion of 20 % (w/w) starch hydrolysate achieved with the immobilized glucoamylase was 97 % after 5 hours.
AB  - Glukoamilaza je imobilizovana preko spejsera na sfere kopolimera glicidil metakrilata i etilen glikol dimetakrilata uz pomoć glutaraldehida. Određen je uticaj količine dodatog enzima na prinos imobilizacije kao i na specifičnu aktivnost dobijenog imobilizata. Dobijena je specifična aktivnost od 700 U/g sa prinosom imobilizacije od 35%. Km vrednost imobilizovane glukoamilaze je 1,28 % (w/v), pH i temperaturni optimumi su 4,5 i 70°S. Imobilizovani enzim je pri hidrolizi 20 % (w/w) hidrolizata skroba postigao konverziju od 97 % nakon 5 sati.
T2  - Acta periodica technologica
T1  - Immobilization of glucoamylase on macroporous spheres
T1  - Imobilizacija glukoamilaze na makroporoznim sferama
IS  - 35
SP  - 207
EP  - 214
DO  - 10.2298/APT0435207M
UR  - Kon_140
ER  - 
@article{
author = "Milosavić, Nenad B. and Prodanović, Radivoje and Jovanović, Slobodan M. and Vujčić, Zoran",
year = "2004",
abstract = "Glucoamylase was covalently immobilized through the spacer-arm of the poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) spheres by using a glutaraldehyde as a coupling agent. The influence of the enzyme load applied to the support on immobilization, yield and specific activity, has been determined. Obtained specific activity was 700 U/g with immobilization yield of 35 %. The Km value for immobilized glucoamylase was 1.28 % (w/v), pH and temperature optimum were 4.5 and 70°C, respectively. The conversion of 20 % (w/w) starch hydrolysate achieved with the immobilized glucoamylase was 97 % after 5 hours., Glukoamilaza je imobilizovana preko spejsera na sfere kopolimera glicidil metakrilata i etilen glikol dimetakrilata uz pomoć glutaraldehida. Određen je uticaj količine dodatog enzima na prinos imobilizacije kao i na specifičnu aktivnost dobijenog imobilizata. Dobijena je specifična aktivnost od 700 U/g sa prinosom imobilizacije od 35%. Km vrednost imobilizovane glukoamilaze je 1,28 % (w/v), pH i temperaturni optimumi su 4,5 i 70°S. Imobilizovani enzim je pri hidrolizi 20 % (w/w) hidrolizata skroba postigao konverziju od 97 % nakon 5 sati.",
journal = "Acta periodica technologica",
title = "Immobilization of glucoamylase on macroporous spheres, Imobilizacija glukoamilaze na makroporoznim sferama",
number = "35",
pages = "207-214",
doi = "10.2298/APT0435207M",
url = "Kon_140"
}
Milosavić, N. B., Prodanović, R., Jovanović, S. M.,& Vujčić, Z.. (2004). Immobilization of glucoamylase on macroporous spheres. in Acta periodica technologica(35), 207-214.
https://doi.org/10.2298/APT0435207M
Kon_140
Milosavić NB, Prodanović R, Jovanović SM, Vujčić Z. Immobilization of glucoamylase on macroporous spheres. in Acta periodica technologica. 2004;(35):207-214.
doi:10.2298/APT0435207M
Kon_140 .
Milosavić, Nenad B., Prodanović, Radivoje, Jovanović, Slobodan M., Vujčić, Zoran, "Immobilization of glucoamylase on macroporous spheres" in Acta periodica technologica, no. 35 (2004):207-214,
https://doi.org/10.2298/APT0435207M .,
Kon_140 .
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