Radovanović, Mirjana N.

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orcid::0000-0003-0337-8706
  • Radovanović, Mirjana N. (2)
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Author's Bibliography

Polyaniline stabilization of magnetic particles and immobilization of alpha-amylase

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

(Savez hemijskih inženjera, Beograd, 2018)

TY  - JOUR
AU  - Radovanović, Mirjana N.
AU  - Nikolić, Milan P.
AU  - Đurović, Vesna M.
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Grgur, Branimir
AU  - Knežević-Jugović, Zorica
PY  - 2018
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4026
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 a-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 a-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 K-m constant was 1.91 and 1.48 g L-1 for MAG-A and MAG-PANI-A, respectively, while V-m 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 K-m 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 hydrolyzed 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 hydrolyze 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 a-amylase adsorbed onto MAG-PANI.
PB  - Savez hemijskih inženjera, Beograd
T2  - Hemijska industrija
T1  - Polyaniline stabilization of magnetic particles and immobilization of alpha-amylase
EP  - 12
IS  - 1
SP  - 1
VL  - 72
DO  - 10.2298/HEMIND161213016R
ER  - 
@article{
author = "Radovanović, Mirjana N. and Nikolić, Milan P. and Đurović, Vesna M. and Jugović, Branimir and Gvozdenović, Milica 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 a-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 a-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 K-m constant was 1.91 and 1.48 g L-1 for MAG-A and MAG-PANI-A, respectively, while V-m 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 K-m 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 hydrolyzed 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 hydrolyze 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 a-amylase adsorbed onto MAG-PANI.",
publisher = "Savez hemijskih inženjera, Beograd",
journal = "Hemijska industrija",
title = "Polyaniline stabilization of magnetic particles and immobilization of alpha-amylase",
pages = "12-1",
number = "1",
volume = "72",
doi = "10.2298/HEMIND161213016R"
}
Radovanović, M. N., Nikolić, M. P., Đurović, V. M., Jugović, B., Gvozdenović, M., Grgur, B.,& Knežević-Jugović, Z.. (2018). Polyaniline stabilization of magnetic particles and immobilization of alpha-amylase. in Hemijska industrija
Savez hemijskih inženjera, Beograd., 72(1), 1-12.
https://doi.org/10.2298/HEMIND161213016R
Radovanović MN, Nikolić MP, Đurović VM, Jugović B, Gvozdenović M, Grgur B, Knežević-Jugović Z. Polyaniline stabilization of magnetic particles and immobilization of alpha-amylase. in Hemijska industrija. 2018;72(1):1-12.
doi:10.2298/HEMIND161213016R .
Radovanović, Mirjana N., Nikolić, Milan P., Đurović, Vesna M., Jugović, Branimir, Gvozdenović, Milica, Grgur, Branimir, Knežević-Jugović, Zorica, "Polyaniline stabilization of magnetic particles and immobilization of alpha-amylase" in Hemijska industrija, 72, no. 1 (2018):1-12,
https://doi.org/10.2298/HEMIND161213016R . .

Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline

Radovanović, Mirjana N.; Jugović, Branimir; Gvozdenović, Milica; Jokić, Bojan; Grgur, Branimir; Bugarski, Branko; Knežević-Jugović, Zorica

(Wiley-VCH Verlag Gmbh, Weinheim, 2016)

TY  - JOUR
AU  - Radovanović, Mirjana N.
AU  - Jugović, Branimir
AU  - Gvozdenović, Milica
AU  - Jokić, Bojan
AU  - Grgur, Branimir
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2016
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3228
AB  - The immobilization of alpha-amylase via adsorption on magnetic particles coated with polyaniline was studied. The support was characterized by field emission scanning electron microscopy (FESEM). The obtained magnetic particles were agglomerates of nanoparticles with sizes below 100 nm. The effects of various factors on immobilization, including time, the initial enzyme concentration, pH, and temperature, were examined. The optimum pH, temperature, and time for immobilization were established to be 7, 45 degrees C and 75 min, respectively. The maximum amount of adsorbed alpha-amylase of 10/100mg support was determined at the 5 mg/mL enzyme concentration. It appeared that alpha-amylase was stabilized in terms of pH and temperature by adsorption on magnetic particles coated with polyaniline. The good agreement of the equilibrium data with the Langmuir isotherm model confirmed the monolayer coverage of enzyme molecules on the surface of magnetic particles, and the maximum adsorption capacity was found to be 55.6/100mg support at 25 degrees C. The biocatalyst retained 55.5 +/- 1.63% of its initial activity after nine cycles of reuse in starch hydrolysis at 60 degrees C in a batch reactor. The immobilized enzyme also showed very good storage stability.
PB  - Wiley-VCH Verlag Gmbh, Weinheim
T2  - Starch-Starke
T1  - Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline
EP  - 435
IS  - 5-6
SP  - 427
VL  - 68
DO  - 10.1002/star.201500161
ER  - 
@article{
author = "Radovanović, Mirjana N. and Jugović, Branimir and Gvozdenović, Milica and Jokić, Bojan and Grgur, Branimir and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2016",
abstract = "The immobilization of alpha-amylase via adsorption on magnetic particles coated with polyaniline was studied. The support was characterized by field emission scanning electron microscopy (FESEM). The obtained magnetic particles were agglomerates of nanoparticles with sizes below 100 nm. The effects of various factors on immobilization, including time, the initial enzyme concentration, pH, and temperature, were examined. The optimum pH, temperature, and time for immobilization were established to be 7, 45 degrees C and 75 min, respectively. The maximum amount of adsorbed alpha-amylase of 10/100mg support was determined at the 5 mg/mL enzyme concentration. It appeared that alpha-amylase was stabilized in terms of pH and temperature by adsorption on magnetic particles coated with polyaniline. The good agreement of the equilibrium data with the Langmuir isotherm model confirmed the monolayer coverage of enzyme molecules on the surface of magnetic particles, and the maximum adsorption capacity was found to be 55.6/100mg support at 25 degrees C. The biocatalyst retained 55.5 +/- 1.63% of its initial activity after nine cycles of reuse in starch hydrolysis at 60 degrees C in a batch reactor. The immobilized enzyme also showed very good storage stability.",
publisher = "Wiley-VCH Verlag Gmbh, Weinheim",
journal = "Starch-Starke",
title = "Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline",
pages = "435-427",
number = "5-6",
volume = "68",
doi = "10.1002/star.201500161"
}
Radovanović, M. N., Jugović, B., Gvozdenović, M., Jokić, B., Grgur, B., Bugarski, B.,& Knežević-Jugović, Z.. (2016). Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline. in Starch-Starke
Wiley-VCH Verlag Gmbh, Weinheim., 68(5-6), 427-435.
https://doi.org/10.1002/star.201500161
Radovanović MN, Jugović B, Gvozdenović M, Jokić B, Grgur B, Bugarski B, Knežević-Jugović Z. Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline. in Starch-Starke. 2016;68(5-6):427-435.
doi:10.1002/star.201500161 .
Radovanović, Mirjana N., Jugović, Branimir, Gvozdenović, Milica, Jokić, Bojan, Grgur, Branimir, Bugarski, Branko, Knežević-Jugović, Zorica, "Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline" in Starch-Starke, 68, no. 5-6 (2016):427-435,
https://doi.org/10.1002/star.201500161 . .
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