Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol
Samo za registrovane korisnike
2022
Autori
Pantić, NevenaSpasojević, Milica
Stojanović, Željko
Veljović, Đorđe
Krstić, Jugoslav
Balaž, Ana Marija
Prodanović, Radivoje
Prodanović, Olivera
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallo...l oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.
Ključne reči:
Dispersion polymerization / Horseradish peroxidase / Macroporous copolymer / Phenol conversionIzvor:
Journal of Polymers and the Environment, 2022Izdavač:
- Springer
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200288 (Inovacioni centar Hemijskog fakulteta u Beogradu doo) (RS-MESTD-inst-2020-200288)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200053 (Univerzitet u Beogradu, Institut za multidisciplinarna istraživanja) (RS-MESTD-inst-2020-200053)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-MESTD-inst-2020-200168)
DOI: 10.1007/s10924-021-02364-3
ISSN: 1566-2543
WoS: 000764963200001
Scopus: 2-s2.0-85125657237
Kolekcije
Institucija/grupa
Inovacioni centarTY - JOUR AU - Pantić, Nevena AU - Spasojević, Milica AU - Stojanović, Željko AU - Veljović, Đorđe AU - Krstić, Jugoslav AU - Balaž, Ana Marija AU - Prodanović, Radivoje AU - Prodanović, Olivera PY - 2022 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5096 AB - Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase. PB - Springer T2 - Journal of Polymers and the Environment T1 - Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol DO - 10.1007/s10924-021-02364-3 ER -
@article{ author = "Pantić, Nevena and Spasojević, Milica and Stojanović, Željko and Veljović, Đorđe and Krstić, Jugoslav and Balaž, Ana Marija and Prodanović, Radivoje and Prodanović, Olivera", year = "2022", abstract = "Novel macroporous copolymers of glycidyl methacrylate and ethylene glycol dimethacrylate with mean pore size diameters ranging from 150 to 310 nm were synthesized by dispersion polymerization and modified with ethylenediamine. The glutaraldehyde and periodate method were employed to immobilize horseradish peroxidase (HRP) onto these carriers. The activity of the immobilized enzyme was greatly affected by the pore size of the carrier. The highest specific activities of 9.65 and 8.94 U/g of dry weight were obtained for HRP immobilized by the periodate-route onto poly(GMA‐co‐EGDMA) carriers with pore size diameters of 234 and 297 nm, respectively. Stability studies showed an improved operational stability of immobilized peroxidase at 65 °C and in an organic solvent. HRP immobilized on a copolymer with a pore size of 234 nm, showing the highest specific activity and good stability, had higher activities at almost all pH values than the native enzyme and the increased Km value for pyrogallol oxidation. Immobilized HRP retained 80% of its original activity after five consecutive cycles of the pyrogallol oxidation and 98% of its initial activity in a storage stability study. Enzyme immobilized onto the macroporous copolymer with the pore size diameter of 234 nm showed a substantial degree of phenol removal achieved by immobilized peroxidase.", publisher = "Springer", journal = "Journal of Polymers and the Environment", title = "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol", doi = "10.1007/s10924-021-02364-3" }
Pantić, N., Spasojević, M., Stojanović, Ž., Veljović, Đ., Krstić, J., Balaž, A. M., Prodanović, R.,& Prodanović, O.. (2022). Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment Springer.. https://doi.org/10.1007/s10924-021-02364-3
Pantić N, Spasojević M, Stojanović Ž, Veljović Đ, Krstić J, Balaž AM, Prodanović R, Prodanović O. Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol. in Journal of Polymers and the Environment. 2022;. doi:10.1007/s10924-021-02364-3 .
Pantić, Nevena, Spasojević, Milica, Stojanović, Željko, Veljović, Đorđe, Krstić, Jugoslav, Balaž, Ana Marija, Prodanović, Radivoje, Prodanović, Olivera, "Immobilization of Horseradish Peroxidase on Macroporous Glycidyl-Based Copolymers with Different Surface Characteristics for the Removal of Phenol" in Journal of Polymers and the Environment (2022), https://doi.org/10.1007/s10924-021-02364-3 . .