Milosavić, Nenad B.

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  • Milosavić, Nenad B. (2)
  • Milosavić, Nenad (1)
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Author's Bibliography

Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions

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

(2004)

TY  - JOUR
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan M.
AU  - Maksimović, Vuk
AU  - Vujčić, Zoran
PY  - 2004
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/87
AB  - The application of amyloglucosidase immobilized on the macroporous co-polymer of ethylene glycol dimethacrylate and glycidyl methacrylate (poly (GMA-co-EGDMA)) in an enzyme reactor was shown. The higher thermostability of immobilized glucoamylases than the soluble one was demonstrated. Immobilized amyloglucosidase obtained by the periodate method shows two times higher thermo stability than the soluble form. Glucoamylases immobilized on poly (GMA-co-EGDMA) have good mechanical and chemical features in the reactor and when applied in a continuous flow reactor for 28 days no changes are observed. In this period periodate immobilized amyloglucosidase shows no decrease in activity. It showed potential for the continuous production of glucose from starch over a prolonged period of time.
AB  - U okviru ovoga rada prikazani su rezultati dobijeni izučavanjem termostabilnosti dva kovalentna imobilizata amiloglukozidaze na makroporoznom poli(GMA-co-EGDMA), kao i njihova primena za hidrolizu škroba pri simuliranim industrijskim uslovima. U svim eksperimentima sa reaktorima, bilo šaržnim, bilo da se radi o reaktoru sa napakovanim slojem kao supstrat korišćen je 20 % (m/m) industrijski hidrolizat škroba. Oba imobilizata su pokazala povećanu termostabilnost u odnosu na rastvoreni enzim, ali je ona značajno veća kod imobilizata dobijenog perjodatnom metodom. Prilikom upotrebe u bač reaktoru imobilizati su deset puta brže dali krajnje DE vrednosti slične onoj koju daje rastvorni enzim. Količina i sastav šećera je po završenoj hidrolizi analiziran i HPLC-om. Određena je operativna stabilnost perjodatno imobilizovane amiloglukozidaze u reaktoru sa napakovnim slojem i pri tome je konstatovano da imobilizat ne gubi aktivnost u trajanju od 28 dana.
T2  - Hemijska industrija
T1  - Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions
T1  - Karakterizacija i primena amiloglukozidaze imobilizovane na makroporoznom polkgma-co-egdma) u simuliranim industrijskim uslovima
VL  - 58
IS  - 11
SP  - 493
EP  - 498
DO  - 10.2298/HEMIND0411493M
UR  - Kon_51
ER  - 
@article{
author = "Milosavić, Nenad B. and Prodanović, Radivoje and Jovanović, Slobodan M. and Maksimović, Vuk and Vujčić, Zoran",
year = "2004",
abstract = "The application of amyloglucosidase immobilized on the macroporous co-polymer of ethylene glycol dimethacrylate and glycidyl methacrylate (poly (GMA-co-EGDMA)) in an enzyme reactor was shown. The higher thermostability of immobilized glucoamylases than the soluble one was demonstrated. Immobilized amyloglucosidase obtained by the periodate method shows two times higher thermo stability than the soluble form. Glucoamylases immobilized on poly (GMA-co-EGDMA) have good mechanical and chemical features in the reactor and when applied in a continuous flow reactor for 28 days no changes are observed. In this period periodate immobilized amyloglucosidase shows no decrease in activity. It showed potential for the continuous production of glucose from starch over a prolonged period of time., U okviru ovoga rada prikazani su rezultati dobijeni izučavanjem termostabilnosti dva kovalentna imobilizata amiloglukozidaze na makroporoznom poli(GMA-co-EGDMA), kao i njihova primena za hidrolizu škroba pri simuliranim industrijskim uslovima. U svim eksperimentima sa reaktorima, bilo šaržnim, bilo da se radi o reaktoru sa napakovanim slojem kao supstrat korišćen je 20 % (m/m) industrijski hidrolizat škroba. Oba imobilizata su pokazala povećanu termostabilnost u odnosu na rastvoreni enzim, ali je ona značajno veća kod imobilizata dobijenog perjodatnom metodom. Prilikom upotrebe u bač reaktoru imobilizati su deset puta brže dali krajnje DE vrednosti slične onoj koju daje rastvorni enzim. Količina i sastav šećera je po završenoj hidrolizi analiziran i HPLC-om. Određena je operativna stabilnost perjodatno imobilizovane amiloglukozidaze u reaktoru sa napakovnim slojem i pri tome je konstatovano da imobilizat ne gubi aktivnost u trajanju od 28 dana.",
journal = "Hemijska industrija",
title = "Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions, Karakterizacija i primena amiloglukozidaze imobilizovane na makroporoznom polkgma-co-egdma) u simuliranim industrijskim uslovima",
volume = "58",
number = "11",
pages = "493-498",
doi = "10.2298/HEMIND0411493M",
url = "Kon_51"
}
Milosavić, N. B., Prodanović, R., Jovanović, S. M., Maksimović, V.,& Vujčić, Z.. (2004). Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions. in Hemijska industrija, 58(11), 493-498.
https://doi.org/10.2298/HEMIND0411493M
Kon_51
Milosavić NB, Prodanović R, Jovanović SM, Maksimović V, Vujčić Z. Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions. in Hemijska industrija. 2004;58(11):493-498.
doi:10.2298/HEMIND0411493M
Kon_51 .
Milosavić, Nenad B., Prodanović, Radivoje, Jovanović, Slobodan M., Maksimović, Vuk, Vujčić, Zoran, "Characterization of amyloglucosidase immobilized on the copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate in simulated industrial conditions" in Hemijska industrija, 58, no. 11 (2004):493-498,
https://doi.org/10.2298/HEMIND0411493M .,
Kon_51 .
1

Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology

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

(2003)

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Milosavić, Nenad B.
AU  - Jovanović, Slobodan M.
AU  - Vujčić, Zoran
PY  - 2003
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/86
AB  - The optimal conditions for the immobilization of invertase and glucoamylasewere found via their carbohydrate moiety on a macroporous copolymer of ehtyleneglycoldimethacry late and glycidylmethacrylate. Almost all of the added enzyme was bound to the polymer by increasing the time of incubation of the oxidized enzyme with polymer. A specific activity of 5500 U/g for invertase was obtained and 1100 U/g for glucoamylase. The specific productivity for invertase in a packed bed reactor was 3.5 kg/lh and for glucoamylase 1.9 kg/lh. During continuous use in a packed bed the reactor operational half life for invertase was 290 days, while no decrease in activity was observed for glucoamylase. In 50% (v/v) ethanol the immobilized enzymes were five to ten times more stable, and more than 200 times more stable in 25% (v/v) dioxane. The immobilized enzymes retained all activity in petroleum ether after 3 days of incubation. Because of their higher stability over native enzymes, and the large surface area of the polymer immobilized glucoamylase and invertase could be more useful for glycoside synthesis in non-aqueous solvents than native ones.
AB  - Određeni su optimalni uslovi za imobilizaciju invertaze i glukoamilaze prekonjihove ugljenohidratne komponente u strukturi na makroporoznom kopolimeru glicidilmetakrilata i etilenglikoldimetakrilata. Dobijeni su imobilizati invertaze specifične aktivnosti od 5500 ILJ/g i glukoamilaze specifične aktivnosti od 1100 U/g. Specificna produktivnost cevastog protočnog reaktora sa imobilizovanom invertazom je bila 3,5 kg/dm3, a sa glukoamilazom 1,5 kg/dm3h. Operativna stabilnost imobilizovane invertaze tokom dvonedeljne upotrebe je procenjena na 290 dana, dok imobilizat glukoamilaze nije gubio aktivnost tokom 30 dana kontinuirane upotrebe. U 50% (v/v) etanolu imobilizovani enzimi su bili 10 puta stabilniji, u 25% (v/v) dioksanu preko 200 puta, dok u petrol etru nisu gubili aktivnost ni posle 3 dana.
T2  - Hemijska industrija
T1  - Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology
T1  - Imobilizacija invertaze i glukoamilaze na makroporoznom kopolimeru glicidilmetakrilata i etilenglikoldimetakrilata i njihova potencijalna primena u biotehnologiji
VL  - 57
IS  - 11
SP  - 536
EP  - 542
DO  - 10.2298/HEMIND0311536P
UR  - Kon_49
ER  - 
@article{
author = "Prodanović, Radivoje and Milosavić, Nenad B. and Jovanović, Slobodan M. and Vujčić, Zoran",
year = "2003",
abstract = "The optimal conditions for the immobilization of invertase and glucoamylasewere found via their carbohydrate moiety on a macroporous copolymer of ehtyleneglycoldimethacry late and glycidylmethacrylate. Almost all of the added enzyme was bound to the polymer by increasing the time of incubation of the oxidized enzyme with polymer. A specific activity of 5500 U/g for invertase was obtained and 1100 U/g for glucoamylase. The specific productivity for invertase in a packed bed reactor was 3.5 kg/lh and for glucoamylase 1.9 kg/lh. During continuous use in a packed bed the reactor operational half life for invertase was 290 days, while no decrease in activity was observed for glucoamylase. In 50% (v/v) ethanol the immobilized enzymes were five to ten times more stable, and more than 200 times more stable in 25% (v/v) dioxane. The immobilized enzymes retained all activity in petroleum ether after 3 days of incubation. Because of their higher stability over native enzymes, and the large surface area of the polymer immobilized glucoamylase and invertase could be more useful for glycoside synthesis in non-aqueous solvents than native ones., Određeni su optimalni uslovi za imobilizaciju invertaze i glukoamilaze prekonjihove ugljenohidratne komponente u strukturi na makroporoznom kopolimeru glicidilmetakrilata i etilenglikoldimetakrilata. Dobijeni su imobilizati invertaze specifične aktivnosti od 5500 ILJ/g i glukoamilaze specifične aktivnosti od 1100 U/g. Specificna produktivnost cevastog protočnog reaktora sa imobilizovanom invertazom je bila 3,5 kg/dm3, a sa glukoamilazom 1,5 kg/dm3h. Operativna stabilnost imobilizovane invertaze tokom dvonedeljne upotrebe je procenjena na 290 dana, dok imobilizat glukoamilaze nije gubio aktivnost tokom 30 dana kontinuirane upotrebe. U 50% (v/v) etanolu imobilizovani enzimi su bili 10 puta stabilniji, u 25% (v/v) dioksanu preko 200 puta, dok u petrol etru nisu gubili aktivnost ni posle 3 dana.",
journal = "Hemijska industrija",
title = "Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology, Imobilizacija invertaze i glukoamilaze na makroporoznom kopolimeru glicidilmetakrilata i etilenglikoldimetakrilata i njihova potencijalna primena u biotehnologiji",
volume = "57",
number = "11",
pages = "536-542",
doi = "10.2298/HEMIND0311536P",
url = "Kon_49"
}
Prodanović, R., Milosavić, N. B., Jovanović, S. M.,& Vujčić, Z.. (2003). Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology. in Hemijska industrija, 57(11), 536-542.
https://doi.org/10.2298/HEMIND0311536P
Kon_49
Prodanović R, Milosavić NB, Jovanović SM, Vujčić Z. Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology. in Hemijska industrija. 2003;57(11):536-542.
doi:10.2298/HEMIND0311536P
Kon_49 .
Prodanović, Radivoje, Milosavić, Nenad B., Jovanović, Slobodan M., Vujčić, Zoran, "Immobilization of invertase and glucoamylase on a macroporous copolymer of etyleneglycoldimethacrylate and glycidyl methacrylate and potential applications in biotechnology" in Hemijska industrija, 57, no. 11 (2003):536-542,
https://doi.org/10.2298/HEMIND0311536P .,
Kon_49 .
2

Production and properties of glucoamylase from Aspergillus niger WT

Milosavić, Nenad; Prodanović, Radivoje; Vujčić, Zoran

(2001)

TY  - JOUR
AU  - Milosavić, Nenad
AU  - Prodanović, Radivoje
AU  - Vujčić, Zoran
PY  - 2001
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/174
AB  - Aspergillus niger WT was cultivated in a liquid medium containing corn meal, on two types of shakers. Measured glucoamylase production reached maximum after 96 h. When the organism was grown on a rotary shaker it produced two times more enzyme than when it was grown on a reciprocal shaker. Studies of glucoamylase characteristics revealed that the optimum temperature for its activity was 65 oC. Half life of the obtained enzyme was 120 min at 60 oC. The optimum pH of the enzyme was 4.5. A procedure for detecting the activity of glucoamylase on a isoelectric focusing (IEF) gel by KI reagent was described. Since the method is very sensitive, it will be useful for enzyme engineering studies that involve screening of various mutations.
AB  - Aspergillus niger WT je gajen u tečnom medijumu koji sadrži kukuruzni griz na dva tipa mućkalica. Produkcija glukoamilaze dostigla je maksimum posle 96h. Kada se organizam gaji na rotacionoj mućkalici produkcija enzima je dva puta veća nego kada se gaji na recipročnoj mućkalici. Proučavanje karakteristika glukoamilaze pokazalo je da je temperaturni optimum za njenu aktivnost 65 oC. Poluživot dobijenog enzima je 120 min na 60 oC. pH optimum enzima je 4,5. U radu je opisana i procedura za detektovanje aktivnosti glukoamilaze u gelu nakon IEF koristeći KI reagens. Metoda je veoma osetljiva i može se koristiti za proučavanje strukture enzima skriningom različitih mutacija.
T2  - Acta biologica iugoslavica - serija B: Mikrobiologija
T1  - Production and properties of glucoamylase from Aspergillus niger WT
T1  - Produkcija i osobine glukoamilaze iz divljeg soja Aspergillus niger
VL  - 38
IS  - 2
SP  - 71
EP  - 78
UR  - Kon_593
ER  - 
@article{
author = "Milosavić, Nenad and Prodanović, Radivoje and Vujčić, Zoran",
year = "2001",
abstract = "Aspergillus niger WT was cultivated in a liquid medium containing corn meal, on two types of shakers. Measured glucoamylase production reached maximum after 96 h. When the organism was grown on a rotary shaker it produced two times more enzyme than when it was grown on a reciprocal shaker. Studies of glucoamylase characteristics revealed that the optimum temperature for its activity was 65 oC. Half life of the obtained enzyme was 120 min at 60 oC. The optimum pH of the enzyme was 4.5. A procedure for detecting the activity of glucoamylase on a isoelectric focusing (IEF) gel by KI reagent was described. Since the method is very sensitive, it will be useful for enzyme engineering studies that involve screening of various mutations., Aspergillus niger WT je gajen u tečnom medijumu koji sadrži kukuruzni griz na dva tipa mućkalica. Produkcija glukoamilaze dostigla je maksimum posle 96h. Kada se organizam gaji na rotacionoj mućkalici produkcija enzima je dva puta veća nego kada se gaji na recipročnoj mućkalici. Proučavanje karakteristika glukoamilaze pokazalo je da je temperaturni optimum za njenu aktivnost 65 oC. Poluživot dobijenog enzima je 120 min na 60 oC. pH optimum enzima je 4,5. U radu je opisana i procedura za detektovanje aktivnosti glukoamilaze u gelu nakon IEF koristeći KI reagens. Metoda je veoma osetljiva i može se koristiti za proučavanje strukture enzima skriningom različitih mutacija.",
journal = "Acta biologica iugoslavica - serija B: Mikrobiologija",
title = "Production and properties of glucoamylase from Aspergillus niger WT, Produkcija i osobine glukoamilaze iz divljeg soja Aspergillus niger",
volume = "38",
number = "2",
pages = "71-78",
url = "Kon_593"
}
Milosavić, N., Prodanović, R.,& Vujčić, Z.. (2001). Production and properties of glucoamylase from Aspergillus niger WT. in Acta biologica iugoslavica - serija B: Mikrobiologija, 38(2), 71-78.
Kon_593
Milosavić N, Prodanović R, Vujčić Z. Production and properties of glucoamylase from Aspergillus niger WT. in Acta biologica iugoslavica - serija B: Mikrobiologija. 2001;38(2):71-78.
Kon_593 .
Milosavić, Nenad, Prodanović, Radivoje, Vujčić, Zoran, "Production and properties of glucoamylase from Aspergillus niger WT" in Acta biologica iugoslavica - serija B: Mikrobiologija, 38, no. 2 (2001):71-78,
Kon_593 .