Immobilization of horseradish peroxidase onto kaolin
Authorized Users Only
2016
Authors
Šekuljica, NatašaPrlainović, Nevena
Jovanović, Jelena
Stefanović, Andrea
Đokić, Veljko
Mijin, Dušan
Knežević-Jugović, Zorica
Article (Published version)
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Show full item recordAbstract
Kaolin showed as a very perspective carrier for the enzyme immobilization and it was used for the adsorption of horseradish peroxidase (HRP). The effects of the enzyme concentration and pH on the immobilization efficiency were studied in the reaction with pyrogallol and anthraquinone dye C.I. Acid Violet 109 (AV 109). In addition, Fourier transform infrared spectroscopy, scanning electron microscopy and analysis by Brunauer-EmmettTeller were performed for kaolin, thermally activated kaolin and the immobilized enzyme. It has been shown that 0.1 IU of HRP-kaolin decolorized 87 % of dye solution, under the optimal conditions (pH 5.0, temperature 24 degrees C, dye concentration 40 mg/L and 0.2 mM of H2O2) within 40 min. The immobilized HRP decolorization follows the Ping Pong Bi-Bi mechanism with dead-end inhibition by the dye. The biocatalyst retained 35 +/- 0.9 % of the initial activity after seven cycles of reuse in the decolorization reaction of AV 109 under optimal conditions in a bat...ch reactor. The obtained kinetic parameters and reusability study confirmed improvement in performances of k-HRP compared to free, indicating that k-HRP has a great potential for environmental purposes.
Keywords:
Horseradish peroxidase / Kaolin / Adsorption / Kinetic parameters / Wastewater treatmentSource:
Bioprocess and Biosystems Engineering, 2016, 39, 3, 461-472Publisher:
- Springer, New York
Funding / projects:
- Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness (RS-46010)
- Study of the Synthesis, Structure and Activity of Natural and Synthetic Organic Compounds (RS-172013)
DOI: 10.1007/s00449-015-1529-x
ISSN: 1615-7591
PubMed: 26747440
WoS: 000371071100010
Scopus: 2-s2.0-84960101239
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Tehnološko-metalurški fakultetTY - JOUR AU - Šekuljica, Nataša AU - Prlainović, Nevena AU - Jovanović, Jelena AU - Stefanović, Andrea AU - Đokić, Veljko AU - Mijin, Dušan AU - Knežević-Jugović, Zorica PY - 2016 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3466 AB - Kaolin showed as a very perspective carrier for the enzyme immobilization and it was used for the adsorption of horseradish peroxidase (HRP). The effects of the enzyme concentration and pH on the immobilization efficiency were studied in the reaction with pyrogallol and anthraquinone dye C.I. Acid Violet 109 (AV 109). In addition, Fourier transform infrared spectroscopy, scanning electron microscopy and analysis by Brunauer-EmmettTeller were performed for kaolin, thermally activated kaolin and the immobilized enzyme. It has been shown that 0.1 IU of HRP-kaolin decolorized 87 % of dye solution, under the optimal conditions (pH 5.0, temperature 24 degrees C, dye concentration 40 mg/L and 0.2 mM of H2O2) within 40 min. The immobilized HRP decolorization follows the Ping Pong Bi-Bi mechanism with dead-end inhibition by the dye. The biocatalyst retained 35 +/- 0.9 % of the initial activity after seven cycles of reuse in the decolorization reaction of AV 109 under optimal conditions in a batch reactor. The obtained kinetic parameters and reusability study confirmed improvement in performances of k-HRP compared to free, indicating that k-HRP has a great potential for environmental purposes. PB - Springer, New York T2 - Bioprocess and Biosystems Engineering T1 - Immobilization of horseradish peroxidase onto kaolin EP - 472 IS - 3 SP - 461 VL - 39 DO - 10.1007/s00449-015-1529-x ER -
@article{ author = "Šekuljica, Nataša and Prlainović, Nevena and Jovanović, Jelena and Stefanović, Andrea and Đokić, Veljko and Mijin, Dušan and Knežević-Jugović, Zorica", year = "2016", abstract = "Kaolin showed as a very perspective carrier for the enzyme immobilization and it was used for the adsorption of horseradish peroxidase (HRP). The effects of the enzyme concentration and pH on the immobilization efficiency were studied in the reaction with pyrogallol and anthraquinone dye C.I. Acid Violet 109 (AV 109). In addition, Fourier transform infrared spectroscopy, scanning electron microscopy and analysis by Brunauer-EmmettTeller were performed for kaolin, thermally activated kaolin and the immobilized enzyme. It has been shown that 0.1 IU of HRP-kaolin decolorized 87 % of dye solution, under the optimal conditions (pH 5.0, temperature 24 degrees C, dye concentration 40 mg/L and 0.2 mM of H2O2) within 40 min. The immobilized HRP decolorization follows the Ping Pong Bi-Bi mechanism with dead-end inhibition by the dye. The biocatalyst retained 35 +/- 0.9 % of the initial activity after seven cycles of reuse in the decolorization reaction of AV 109 under optimal conditions in a batch reactor. The obtained kinetic parameters and reusability study confirmed improvement in performances of k-HRP compared to free, indicating that k-HRP has a great potential for environmental purposes.", publisher = "Springer, New York", journal = "Bioprocess and Biosystems Engineering", title = "Immobilization of horseradish peroxidase onto kaolin", pages = "472-461", number = "3", volume = "39", doi = "10.1007/s00449-015-1529-x" }
Šekuljica, N., Prlainović, N., Jovanović, J., Stefanović, A., Đokić, V., Mijin, D.,& Knežević-Jugović, Z.. (2016). Immobilization of horseradish peroxidase onto kaolin. in Bioprocess and Biosystems Engineering Springer, New York., 39(3), 461-472. https://doi.org/10.1007/s00449-015-1529-x
Šekuljica N, Prlainović N, Jovanović J, Stefanović A, Đokić V, Mijin D, Knežević-Jugović Z. Immobilization of horseradish peroxidase onto kaolin. in Bioprocess and Biosystems Engineering. 2016;39(3):461-472. doi:10.1007/s00449-015-1529-x .
Šekuljica, Nataša, Prlainović, Nevena, Jovanović, Jelena, Stefanović, Andrea, Đokić, Veljko, Mijin, Dušan, Knežević-Jugović, Zorica, "Immobilization of horseradish peroxidase onto kaolin" in Bioprocess and Biosystems Engineering, 39, no. 3 (2016):461-472, https://doi.org/10.1007/s00449-015-1529-x . .