Jovanović, Slobodan M.

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  • Jovanović, Slobodan M. (4)
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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  - https://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 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 .
6

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  - https://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 .
3

Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate

Prodanović, Radivoje; Jovanović, Slobodan M.; Vujčić, Zoran

(2001)

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan M.
AU  - Vujčić, Zoran
PY  - 2001
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/208
AB  - Immobilization via carbohydrate moiety is suitable for immobilization of glycoenzymes because it has little effect on enzyme active site. Macroporous glycidyl methacrylate is better support for enzyme immobilization from the much more used polystyrene because of its lesser hydrophobicity. We found optimal conditions for invertase immobilization via its carbohydrate moiety on macroporous glycidyl methacryate by varying enzyme concentration. We obtained immobilized enzyme with specific activity of 5500 lU/g, which is the highest activity reported in the literature. Immobilized enzyme has Km=43 mmol/l, temperature optimum of 60ºC, and pH optimum between 3.5 and 5.5.
AB  - Imobilizacija preko šećernog dela je pogodna za glikoenzime zato što ima malo uticaja na aktivno mesto enzima. Makroporozni glicidil metakrilat je bolji nosač za imobilizaciju enzima od više korišćenog polistirena zbog svoje hidrofilnosti. Utvrđeni su optimalni uslovi za imobilizaciju invertaze preko šećernog dela na makroporozni glicidil metalkrilat variranjem koncentracije enizima. Dobijen je imobilizovani enzim specifične aktivnosti 5000 IU/g, što je najveća aktivnost do sada opisana u literaturi. Imobilizovani enzim je imao Km 43 mmol/l, temperaturni optimum na 60ºC i pH optimum između 4 i 5.
T2  - Acta periodica technologica
T1  - Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate
T1  - Imobilizacija invertaze preko ugljenohidratnog dela na makroporozni glicidil metakrilat
IS  - 32
SP  - 151
EP  - 156
UR  - Kon_139
UR  - https://hdl.handle.net/21.15107/rcub_cherry_208
ER  - 
@article{
author = "Prodanović, Radivoje and Jovanović, Slobodan M. and Vujčić, Zoran",
year = "2001",
abstract = "Immobilization via carbohydrate moiety is suitable for immobilization of glycoenzymes because it has little effect on enzyme active site. Macroporous glycidyl methacrylate is better support for enzyme immobilization from the much more used polystyrene because of its lesser hydrophobicity. We found optimal conditions for invertase immobilization via its carbohydrate moiety on macroporous glycidyl methacryate by varying enzyme concentration. We obtained immobilized enzyme with specific activity of 5500 lU/g, which is the highest activity reported in the literature. Immobilized enzyme has Km=43 mmol/l, temperature optimum of 60ºC, and pH optimum between 3.5 and 5.5., Imobilizacija preko šećernog dela je pogodna za glikoenzime zato što ima malo uticaja na aktivno mesto enzima. Makroporozni glicidil metakrilat je bolji nosač za imobilizaciju enzima od više korišćenog polistirena zbog svoje hidrofilnosti. Utvrđeni su optimalni uslovi za imobilizaciju invertaze preko šećernog dela na makroporozni glicidil metalkrilat variranjem koncentracije enizima. Dobijen je imobilizovani enzim specifične aktivnosti 5000 IU/g, što je najveća aktivnost do sada opisana u literaturi. Imobilizovani enzim je imao Km 43 mmol/l, temperaturni optimum na 60ºC i pH optimum između 4 i 5.",
journal = "Acta periodica technologica",
title = "Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate, Imobilizacija invertaze preko ugljenohidratnog dela na makroporozni glicidil metakrilat",
number = "32",
pages = "151-156",
url = "Kon_139, https://hdl.handle.net/21.15107/rcub_cherry_208"
}
Prodanović, R., Jovanović, S. M.,& Vujčić, Z.. (2001). Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate. in Acta periodica technologica(32), 151-156.
Kon_139
Prodanović R, Jovanović SM, Vujčić Z. Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate. in Acta periodica technologica. 2001;(32):151-156.
Kon_139 .
Prodanović, Radivoje, Jovanović, Slobodan M., Vujčić, Zoran, "Immobilization of invertase via its carbohydrate moiety on macroporous glycidyl methacrylate" in Acta periodica technologica, no. 32 (2001):151-156,
Kon_139 .