TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Anđelković, Ivan
AU  - Milovanovic, Aleksandra
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Roglić, Goran
AU  - Vujčić, Zoran
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1339
AB  - Phenols containing halogens, which tend to deactivate the aromatic nuclei, constitute a significant category of highly toxic and difficult-to-degrade pollutants, which arise from a wide variety of industries. The main purpose of this study was to obtain an inexpensive immobilized enzyme for the removal of phenols. Partially purified potato polyphenol oxidase (PPO) was immobilized onto different commercial and laboratory produced carriers. Three of the obtained biocatalysts, with the highest PPO activities, namely Eupergit C250L-PPO; Celite-PPO and CelluloseM-PPO, were tested in a batch reactor for the removal of phenol, 4-chlorophenol and 4-bromophenol. In the case of 2.5 mM substrates with Eupergit C250L-PPO, an around 45 % removal of 4-bromophenol was achieved, while the removals 4-chlorophenol and phenol were 35 and 20 %, respectively. The reusability of Eupergit C250L-PPO for the removal of 4-chlorophenol was tested. After eight repeated tests, the efficiency of 4-chlorophenol removal by Eupergit C250L-PPO immobilisate had decreased to 55 %.
AB  - Halogenovani fenoli imaju dezaktivirano aromatično jezgro i čine značajnu kategoriju veoma toksičnih i teško razgradivih zagađivača u raznim industrijskim granama. Glavni cilj ovog rada je bio dobijanje jeftinog imobilizovanog enzima za uklanjanje fenola. Delimično prečišćena polifenol-oksidaza (PFO) iz krompira je imobilizovana na različitim komercijalnim i laboratorijski sintetizovanim nosačima. Od dobijenih biokatalizatora, tri sa najvećim aktivnostima PPO, nazvani Eupergit C250L-PFO; Celit-PFO i CelulozaM-PFO, testirani su u reaktoru za uklanjanje fenola, 4-hlorfenola i 4-bromfenola. U slučaju 2,5 mM supstrata sa Eupergit C250L-PFO, postignuto je oko 45 % razgradnje 4-bromfenola, dok su 4-hlorfenol i fenol razgrađeni 35, odnosno 20 %. Testirana je i sposobnost višestruke upotrebe Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola. Nakon osam ponovljenih ciklusa efikasnost Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola je pala na 55%.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase
T1  - Uklanjanje fenola i fenolnih derivata iz vode imobilizovanom polifenol-oksidazom iz krompira
VL  - 76
IS  - 4
SP  - 513
EP  - 522
DO  - 10.2298/JSC100619046L
ER  - 

@article{
author = "Lončar, Nikola L. and Božić, Nataša and Anđelković, Ivan and Milovanovic, Aleksandra and Dojnov, Biljana and Vujčić, Miroslava and Roglić, Goran and Vujčić, Zoran",
year = "2011",
abstract = "Phenols containing halogens, which tend to deactivate the aromatic nuclei, constitute a significant category of highly toxic and difficult-to-degrade pollutants, which arise from a wide variety of industries. The main purpose of this study was to obtain an inexpensive immobilized enzyme for the removal of phenols. Partially purified potato polyphenol oxidase (PPO) was immobilized onto different commercial and laboratory produced carriers. Three of the obtained biocatalysts, with the highest PPO activities, namely Eupergit C250L-PPO; Celite-PPO and CelluloseM-PPO, were tested in a batch reactor for the removal of phenol, 4-chlorophenol and 4-bromophenol. In the case of 2.5 mM substrates with Eupergit C250L-PPO, an around 45 % removal of 4-bromophenol was achieved, while the removals 4-chlorophenol and phenol were 35 and 20 %, respectively. The reusability of Eupergit C250L-PPO for the removal of 4-chlorophenol was tested. After eight repeated tests, the efficiency of 4-chlorophenol removal by Eupergit C250L-PPO immobilisate had decreased to 55 %., Halogenovani fenoli imaju dezaktivirano aromatično jezgro i čine značajnu kategoriju veoma toksičnih i teško razgradivih zagađivača u raznim industrijskim granama. Glavni cilj ovog rada je bio dobijanje jeftinog imobilizovanog enzima za uklanjanje fenola. Delimično prečišćena polifenol-oksidaza (PFO) iz krompira je imobilizovana na različitim komercijalnim i laboratorijski sintetizovanim nosačima. Od dobijenih biokatalizatora, tri sa najvećim aktivnostima PPO, nazvani Eupergit C250L-PFO; Celit-PFO i CelulozaM-PFO, testirani su u reaktoru za uklanjanje fenola, 4-hlorfenola i 4-bromfenola. U slučaju 2,5 mM supstrata sa Eupergit C250L-PFO, postignuto je oko 45 % razgradnje 4-bromfenola, dok su 4-hlorfenol i fenol razgrađeni 35, odnosno 20 %. Testirana je i sposobnost višestruke upotrebe Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola. Nakon osam ponovljenih ciklusa efikasnost Eupergit C250L-PFO imobilizata za uklanjanje 4-hlorfenola je pala na 55%.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase, Uklanjanje fenola i fenolnih derivata iz vode imobilizovanom polifenol-oksidazom iz krompira",
volume = "76",
number = "4",
pages = "513-522",
doi = "10.2298/JSC100619046L"
}

Lončar, N. L., Božić, N., Anđelković, I., Milovanovic, A., Dojnov, B., Vujčić, M., Roglić, G.,& Vujčić, Z.. (2011). Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(4), 513-522.
https://doi.org/10.2298/JSC100619046L

Lončar NL, Božić N, Anđelković I, Milovanovic A, Dojnov B, Vujčić M, Roglić G, Vujčić Z. Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase. in Journal of the Serbian Chemical Society. 2011;76(4):513-522.
doi:10.2298/JSC100619046L .

Lončar, Nikola L., Božić, Nataša, Anđelković, Ivan, Milovanovic, Aleksandra, Dojnov, Biljana, Vujčić, Miroslava, Roglić, Goran, Vujčić, Zoran, "Removal of aqueous phenol and phenol derivatives by immobilized potato polyphenol oxidase" in Journal of the Serbian Chemical Society, 76, no. 4 (2011):513-522,
https://doi.org/10.2298/JSC100619046L . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Miloradovic, Zoran
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1147
AB  - Yeast cell wall invertase (CWI) was immobilised within 10% gelatin hydrogel. The result of entrapment was the complete immobilisation of all the added CWI. The activity of immobilised biocatalyst was 93 +/- 3 U/g, with activity yield of 30%. The optimum pH was in range of 4.5-5.0 for free and immobilised biocatalyst. The optimum temperature was 60 degrees C for both free and gelatin immobilised CWI. Immobilised CWI was more stable than free CWI above optimum activity temperatures. The K-m of free and immobilised CWI was 35.10 +/- 2.99 mM and 71.45 +/- 3.23 mM, respectively. The V-max, values were estimated as 8.23 +/- 0.24 mM/min and 0.121 +/- 0.002 mM/min, respectively. Immobilised CWI was tested in a batch reactor using 50% sucrose (w/v). After 70 consecutive cycles gelatin immobilised CWI retained 75% of its original activity. (C) 2010 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Cell wall invertase immobilisation within gelatin gel
VL  - 126
IS  - 1
SP  - 236
EP  - 240
DO  - 10.1016/j.foodchem.2010.11.010
ER  - 

@article{
author = "Vujčić, Zoran and Miloradovic, Zoran and Milovanovic, Aleksandra and Božić, Nataša",
year = "2011",
abstract = "Yeast cell wall invertase (CWI) was immobilised within 10% gelatin hydrogel. The result of entrapment was the complete immobilisation of all the added CWI. The activity of immobilised biocatalyst was 93 +/- 3 U/g, with activity yield of 30%. The optimum pH was in range of 4.5-5.0 for free and immobilised biocatalyst. The optimum temperature was 60 degrees C for both free and gelatin immobilised CWI. Immobilised CWI was more stable than free CWI above optimum activity temperatures. The K-m of free and immobilised CWI was 35.10 +/- 2.99 mM and 71.45 +/- 3.23 mM, respectively. The V-max, values were estimated as 8.23 +/- 0.24 mM/min and 0.121 +/- 0.002 mM/min, respectively. Immobilised CWI was tested in a batch reactor using 50% sucrose (w/v). After 70 consecutive cycles gelatin immobilised CWI retained 75% of its original activity. (C) 2010 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Cell wall invertase immobilisation within gelatin gel",
volume = "126",
number = "1",
pages = "236-240",
doi = "10.1016/j.foodchem.2010.11.010"
}

Vujčić, Z., Miloradovic, Z., Milovanovic, A.,& Božić, N.. (2011). Cell wall invertase immobilisation within gelatin gel. in Food Chemistry
Elsevier Sci Ltd, Oxford., 126(1), 236-240.
https://doi.org/10.1016/j.foodchem.2010.11.010

Vujčić Z, Miloradovic Z, Milovanovic A, Božić N. Cell wall invertase immobilisation within gelatin gel. in Food Chemistry. 2011;126(1):236-240.
doi:10.1016/j.foodchem.2010.11.010 .

Vujčić, Zoran, Miloradovic, Zoran, Milovanovic, Aleksandra, Božić, Nataša, "Cell wall invertase immobilisation within gelatin gel" in Food Chemistry, 126, no. 1 (2011):236-240,
https://doi.org/10.1016/j.foodchem.2010.11.010 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Lončar, Nikola L.
AU  - Dojnov, Biljana
AU  - Milovanovic, Aleksandra
AU  - Vujčić, Miroslava
AU  - Božić, Nataša
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1060
AB  - Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber
VL  - 121
IS  - 2
SP  - 418
EP  - 423
DO  - 10.1016/j.foodchem.2009.12.058
ER  - 

@article{
author = "Vujčić, Zoran and Lončar, Nikola L. and Dojnov, Biljana and Milovanovic, Aleksandra and Vujčić, Miroslava and Božić, Nataša",
year = "2010",
abstract = "Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber",
volume = "121",
number = "2",
pages = "418-423",
doi = "10.1016/j.foodchem.2009.12.058"
}

Vujčić, Z., Lončar, N. L., Dojnov, B., Milovanovic, A., Vujčić, M.,& Božić, N.. (2010). Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. in Food Chemistry
Elsevier Sci Ltd, Oxford., 121(2), 418-423.
https://doi.org/10.1016/j.foodchem.2009.12.058

Vujčić Z, Lončar NL, Dojnov B, Milovanovic A, Vujčić M, Božić N. Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. in Food Chemistry. 2010;121(2):418-423.
doi:10.1016/j.foodchem.2009.12.058 .

Vujčić, Zoran, Lončar, Nikola L., Dojnov, Biljana, Milovanovic, Aleksandra, Vujčić, Miroslava, Božić, Nataša, "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber" in Food Chemistry, 121, no. 2 (2010):418-423,
https://doi.org/10.1016/j.foodchem.2009.12.058 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Anđelković, Uroš
AU  - Lončar, Nikola L.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1133
AB  - Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.
PB  - Amer Chemical Soc, Washington
T2  - Journal of Agricultural and Food Chemistry
T1  - Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar
VL  - 58
IS  - 22
SP  - 11896
EP  - 11900
DO  - 10.1021/jf101836r
ER  - 

@article{
author = "Vujčić, Zoran and Milovanovic, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava and Anđelković, Uroš and Lončar, Nikola L.",
year = "2010",
abstract = "Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.",
publisher = "Amer Chemical Soc, Washington",
journal = "Journal of Agricultural and Food Chemistry",
title = "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar",
volume = "58",
number = "22",
pages = "11896-11900",
doi = "10.1021/jf101836r"
}

Vujčić, Z., Milovanovic, A., Božić, N., Dojnov, B., Vujčić, M., Anđelković, U.,& Lončar, N. L.. (2010). Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry
Amer Chemical Soc, Washington., 58(22), 11896-11900.
https://doi.org/10.1021/jf101836r

Vujčić Z, Milovanovic A, Božić N, Dojnov B, Vujčić M, Anđelković U, Lončar NL. Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry. 2010;58(22):11896-11900.
doi:10.1021/jf101836r .

Vujčić, Zoran, Milovanovic, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, Anđelković, Uroš, Lončar, Nikola L., "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar" in Journal of Agricultural and Food Chemistry, 58, no. 22 (2010):11896-11900,
https://doi.org/10.1021/jf101836r . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Milovanovic, Aleksandra
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/963
AB  - Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities.
AB  - Primenom specifičnih hromogenih supstrata, klasno-specifičnih inhibitora i zimogramske analize identifikovano je nekoliko klasa peptidaza u sirovom ekstraktu srednjeg creva larvi koleoptere Morimus funereus. Zimogramskom analizom sa želatinom kao supstratom i fenilmetilsulfonil-fluoridom kao inhibitorom utvrđeno je da su serin-peptidaze najzastupljenije peptidaze u ekstraktu srednjeg creva larvi M. funereus. Zimogramskom analizom sa želatinom kao supstratom i 1,10-fenantrolinom kaoinhibitorom takođe su detektovane metalopeptidaze. Analizom serin-peptidaza, upotrebom specifičnih hromogenih supstrata, dokazano je da su dominantni elastazi-slični enzimi u sirovom ekstraktu srednjeg creva larvi M. funereus, dok su himotripsinima- i tripsinima-slični enzimi manje zastupljeni.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae
T1  - Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)
VL  - 60
IS  - 3
SP  - 403
EP  - 409
DO  - 10.2298/ABS0803403B
ER  - 

@article{
author = "Božić, Nataša and Dojnov, Biljana and Milovanovic, Aleksandra and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2008",
abstract = "Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities., Primenom specifičnih hromogenih supstrata, klasno-specifičnih inhibitora i zimogramske analize identifikovano je nekoliko klasa peptidaza u sirovom ekstraktu srednjeg creva larvi koleoptere Morimus funereus. Zimogramskom analizom sa želatinom kao supstratom i fenilmetilsulfonil-fluoridom kao inhibitorom utvrđeno je da su serin-peptidaze najzastupljenije peptidaze u ekstraktu srednjeg creva larvi M. funereus. Zimogramskom analizom sa želatinom kao supstratom i 1,10-fenantrolinom kaoinhibitorom takođe su detektovane metalopeptidaze. Analizom serin-peptidaza, upotrebom specifičnih hromogenih supstrata, dokazano je da su dominantni elastazi-slični enzimi u sirovom ekstraktu srednjeg creva larvi M. funereus, dok su himotripsinima- i tripsinima-slični enzimi manje zastupljeni.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae, Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)",
volume = "60",
number = "3",
pages = "403-409",
doi = "10.2298/ABS0803403B"
}

Božić, N., Dojnov, B., Milovanovic, A., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2008). Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 60(3), 403-409.
https://doi.org/10.2298/ABS0803403B

Božić N, Dojnov B, Milovanovic A, Nenadovic V, Ivanovic J, Vujčić Z. Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae. in Archives of biological sciences. 2008;60(3):403-409.
doi:10.2298/ABS0803403B .

Božić, Nataša, Dojnov, Biljana, Milovanovic, Aleksandra, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae" in Archives of biological sciences, 60, no. 3 (2008):403-409,
https://doi.org/10.2298/ABS0803403B . .

TY  - JOUR
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/831
AB  - Yeast cell wall invertase (CWI) was immobilized within calcium alginate beads. The result of entrapment was the complete immobilization of all the added CWI. Three types of biocatalysts were prepared: CWI-S, CWI-155 and CWI-157. The optimum pH values were 4.5 and 5.0 for free and immobilized invertase, respectively. The optimum temperature was 60 degrees C, for both free CWI and CWI-S immobilizate. 80 degrees C was the optimum temperature for CWI-155 whereas the optimum temperature for CWI-157 ranged from 50 degrees C to 80 degrees C. Immobilized CWI was more stable than was free CWI above optimum activity temperatures. The activation energies were 32 kJ/mol for free CWI and 45, 21 and 25 kJ/mol for CWI-S, CWI-155 and CWI-157, respectively. The Km values of free and immobilized CWI-157 were 28.4 mM and 72 mM, respectively. The V-max values were estimated as 4.5 mM/min and 0.42 mM/min, respectively. Immobilized CWI-157 was tested in a batch reactor using 70% sucrose (w/v). Complete sucrose conversion was achieved after 55 h. After 40 consecutive cycles, CWI-157 retained 90% of its activity. (c) 2006 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Cell wall invertase immobilization within calcium alginate beads
VL  - 104
IS  - 1
SP  - 81
EP  - 86
DO  - 10.1016/j.foodchem.2006.11.001
ER  - 

@article{
author = "Milovanovic, Aleksandra and Božić, Nataša and Vujčić, Zoran",
year = "2007",
abstract = "Yeast cell wall invertase (CWI) was immobilized within calcium alginate beads. The result of entrapment was the complete immobilization of all the added CWI. Three types of biocatalysts were prepared: CWI-S, CWI-155 and CWI-157. The optimum pH values were 4.5 and 5.0 for free and immobilized invertase, respectively. The optimum temperature was 60 degrees C, for both free CWI and CWI-S immobilizate. 80 degrees C was the optimum temperature for CWI-155 whereas the optimum temperature for CWI-157 ranged from 50 degrees C to 80 degrees C. Immobilized CWI was more stable than was free CWI above optimum activity temperatures. The activation energies were 32 kJ/mol for free CWI and 45, 21 and 25 kJ/mol for CWI-S, CWI-155 and CWI-157, respectively. The Km values of free and immobilized CWI-157 were 28.4 mM and 72 mM, respectively. The V-max values were estimated as 4.5 mM/min and 0.42 mM/min, respectively. Immobilized CWI-157 was tested in a batch reactor using 70% sucrose (w/v). Complete sucrose conversion was achieved after 55 h. After 40 consecutive cycles, CWI-157 retained 90% of its activity. (c) 2006 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Cell wall invertase immobilization within calcium alginate beads",
volume = "104",
number = "1",
pages = "81-86",
doi = "10.1016/j.foodchem.2006.11.001"
}

Milovanovic, A., Božić, N.,& Vujčić, Z.. (2007). Cell wall invertase immobilization within calcium alginate beads. in Food Chemistry
Elsevier Sci Ltd, Oxford., 104(1), 81-86.
https://doi.org/10.1016/j.foodchem.2006.11.001

Milovanovic A, Božić N, Vujčić Z. Cell wall invertase immobilization within calcium alginate beads. in Food Chemistry. 2007;104(1):81-86.
doi:10.1016/j.foodchem.2006.11.001 .

Milovanovic, Aleksandra, Božić, Nataša, Vujčić, Zoran, "Cell wall invertase immobilization within calcium alginate beads" in Food Chemistry, 104, no. 1 (2007):81-86,
https://doi.org/10.1016/j.foodchem.2006.11.001 . .