Radovanović, Mirjana N.

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Polyaniline stabilization of magnetic particles and immobilization of α-amylase

Radovanović, Mirjana N.; Nikolić, Milan P.; Đurović, Vesna M.; Jugović, Branimir; Gvozdenović, Milica M.; Grgur, Branimir; Knežević Jugović, Zorica

(Belgrade : Association of Chemists and Chemical Engineers of Serbia, 2018)

TY  - JOUR
AU  - Radovanović, Mirjana N.
AU  - Nikolić, Milan P.
AU  - Đurović, Vesna M.
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica M.
AU  - Grgur, Branimir
AU  - Knežević Jugović, Zorica
PY  - 2018
UR  - https://dais.sanu.ac.rs/123456789/3749
AB  - Magnetic particles (MAG), obtained by standard procedure of coprecipitation of Fe2+ and Fe3+ in an excess of ammonia, and polyaniline modified magnetic particles MAG-PANI were used as carriers for immobilization of α-amylase from Bacillus licheniformis. The formation of a polyaniline layer (PANI) on MAG particles was achieved by chemical polymerization of aniline. Immobilization was carried out by adsorption, as a simple, inexpensive and fast method that allows retention of a large portion of the initial activity of the immobilized enzyme. FTIR spectroscopy was used to characterize the obtained particles and to confirm changes dueto formation of a PANI layer and conjugation of α-amylase on the particle surfaces. Particle size distribution was bimodal and three-modal for MAG and MAG-PANI, respectively. Appearance of a fraction of smaller MAG-PANI particles than MAG particles could be attributed to the formation of PANI particles without the MAG core. Measured values of Zeta potential for MAG-PANI were higher as compared to MAG indicating stabilization of particles in the presence of PANI. Relevant kinetic parameters for immobilized enzyme were determined from the Hanes plot. The apparent Km constant was 1.91 and 1.48 g L–1 for MAG-A and MAG-PANI-A, respectively, while Vm was 0.19 g L–1 min–1 for MAG and 0.32 g L–1 min–1 for MAG-PANI. The obtained values of Km indicated that modification of MAG by PANI enhanced kinetic properties of the immobilized enzyme. Moreover, the modification of MAG by PANI showed the increase in both pH and thermal stabilities of the immobilized enzyme. Studies of the operational activity of the immobilized enzyme on MAG-PANI have shown that 98.8% of starch was hydro-lyzed over 20.0 min. In the first cycle in the packed bed reactor operated in a recycling mode, but approximately five times longer period was required to hyd-rolyze 93.5 of starch in the fifth cycle. In the continuous packed bed reactor without recycling, the degree of starch hydrolysis was not changed significantly during 4 h and was 88.8±1.6%, whereas the half-life of the biocatalyst was 6.2 h. Although coating MAG particles with a polyaniline offers many advantages, the main disadvantage is possible appearance of residues of aniline monomers and dimmers. The potential toxicity of these residues requires precise composition analysis of the product of starch hydrolysis catalyzed by α-amylase adsorbed onto MAG-PANI. © 2018, Association of Chemists and Chemical Engineers of Serbia. All rights reserved.
PB  - Belgrade : Association of Chemists and Chemical Engineers of Serbia
T2  - Hemijska industrija
T1  - Polyaniline stabilization of magnetic particles and immobilization of α-amylase
SP  - 1
EP  - 12
VL  - 72
IS  - 1
DO  - 10.2298/HEMIND161213016R
UR  - https://hdl.handle.net/21.15107/rcub_dais_3749
ER  - 
@article{
author = "Radovanović, Mirjana N. and Nikolić, Milan P. and Đurović, Vesna M. and Jugović, Branimir and Gvozdenović, Milica M. and Grgur, Branimir and Knežević Jugović, Zorica",
year = "2018",
abstract = "Magnetic particles (MAG), obtained by standard procedure of coprecipitation of Fe2+ and Fe3+ in an excess of ammonia, and polyaniline modified magnetic particles MAG-PANI were used as carriers for immobilization of α-amylase from Bacillus licheniformis. The formation of a polyaniline layer (PANI) on MAG particles was achieved by chemical polymerization of aniline. Immobilization was carried out by adsorption, as a simple, inexpensive and fast method that allows retention of a large portion of the initial activity of the immobilized enzyme. FTIR spectroscopy was used to characterize the obtained particles and to confirm changes dueto formation of a PANI layer and conjugation of α-amylase on the particle surfaces. Particle size distribution was bimodal and three-modal for MAG and MAG-PANI, respectively. Appearance of a fraction of smaller MAG-PANI particles than MAG particles could be attributed to the formation of PANI particles without the MAG core. Measured values of Zeta potential for MAG-PANI were higher as compared to MAG indicating stabilization of particles in the presence of PANI. Relevant kinetic parameters for immobilized enzyme were determined from the Hanes plot. The apparent Km constant was 1.91 and 1.48 g L–1 for MAG-A and MAG-PANI-A, respectively, while Vm was 0.19 g L–1 min–1 for MAG and 0.32 g L–1 min–1 for MAG-PANI. The obtained values of Km indicated that modification of MAG by PANI enhanced kinetic properties of the immobilized enzyme. Moreover, the modification of MAG by PANI showed the increase in both pH and thermal stabilities of the immobilized enzyme. Studies of the operational activity of the immobilized enzyme on MAG-PANI have shown that 98.8% of starch was hydro-lyzed over 20.0 min. In the first cycle in the packed bed reactor operated in a recycling mode, but approximately five times longer period was required to hyd-rolyze 93.5 of starch in the fifth cycle. In the continuous packed bed reactor without recycling, the degree of starch hydrolysis was not changed significantly during 4 h and was 88.8±1.6%, whereas the half-life of the biocatalyst was 6.2 h. Although coating MAG particles with a polyaniline offers many advantages, the main disadvantage is possible appearance of residues of aniline monomers and dimmers. The potential toxicity of these residues requires precise composition analysis of the product of starch hydrolysis catalyzed by α-amylase adsorbed onto MAG-PANI. © 2018, Association of Chemists and Chemical Engineers of Serbia. All rights reserved.",
publisher = "Belgrade : Association of Chemists and Chemical Engineers of Serbia",
journal = "Hemijska industrija",
title = "Polyaniline stabilization of magnetic particles and immobilization of α-amylase",
pages = "1-12",
volume = "72",
number = "1",
doi = "10.2298/HEMIND161213016R",
url = "https://hdl.handle.net/21.15107/rcub_dais_3749"
}
Radovanović, M. N., Nikolić, M. P., Đurović, V. M., Jugović, B., Gvozdenović, M. M., Grgur, B.,& Knežević Jugović, Z.. (2018). Polyaniline stabilization of magnetic particles and immobilization of α-amylase. in Hemijska industrija
Belgrade : Association of Chemists and Chemical Engineers of Serbia., 72(1), 1-12.
https://doi.org/10.2298/HEMIND161213016R
https://hdl.handle.net/21.15107/rcub_dais_3749
Radovanović MN, Nikolić MP, Đurović VM, Jugović B, Gvozdenović MM, Grgur B, Knežević Jugović Z. Polyaniline stabilization of magnetic particles and immobilization of α-amylase. in Hemijska industrija. 2018;72(1):1-12.
doi:10.2298/HEMIND161213016R
https://hdl.handle.net/21.15107/rcub_dais_3749 .
Radovanović, Mirjana N., Nikolić, Milan P., Đurović, Vesna M., Jugović, Branimir, Gvozdenović, Milica M., Grgur, Branimir, Knežević Jugović, Zorica, "Polyaniline stabilization of magnetic particles and immobilization of α-amylase" in Hemijska industrija, 72, no. 1 (2018):1-12,
https://doi.org/10.2298/HEMIND161213016R .,
https://hdl.handle.net/21.15107/rcub_dais_3749 .