Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier
2007
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This paper reports the covalent immobilization of penicillin G acylase from E. coli on Sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes the properties of the immobilized enzyme. Due to its versatility to mediate hydrolysis of penicillins and semi-synthetic B-lactam antibiotics synthesis reactions, the selected enzyme belongs to a class of biocatalysts of great industrial interest. The immobilized enzyme was characterized in its pH and thermal stability and reaction kinetics. The immobilization of penicillin acylase resulted in a slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted the structural and conformational stability to this enzyme. The immobilized enzyme also retained a high catalytic activity and showed the increased thermal stability compared with a free enzyme. By comparison of decimal reduction time values obtained at 50°C, it can be concluded that the immobilized enzyme was appro...ximately 5-fold more stable than a free enzyme. The immobilization procedure developed is quite simple and easily reproduced, and provides a promising solution for the application of penicillin acylase for the purpose of 6-aminopenicillanic acid production.
Ključne reči:
penicillin G acylase / covalent immobilization / epoxy-activated polymethacrylic carrier / sepabeads EC-EP / thermal stabilityIzvor:
Chemical Industry & Chemical Engineering Quarterly, 2007, 13, 4, 205-210Izdavač:
- Association of the Chemical Engineers of Serbia
Finansiranje / projekti:
- Projekat Ministarstva nauke Republike Srbije, br. BTH1008
Institucija/grupa
Tehnološko-metalurški fakultetTY - JOUR AU - Žuža, Milena AU - Šiler-Marinković, Slavica AU - Knežević, Zorica PY - 2007 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1061 AB - This paper reports the covalent immobilization of penicillin G acylase from E. coli on Sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes the properties of the immobilized enzyme. Due to its versatility to mediate hydrolysis of penicillins and semi-synthetic B-lactam antibiotics synthesis reactions, the selected enzyme belongs to a class of biocatalysts of great industrial interest. The immobilized enzyme was characterized in its pH and thermal stability and reaction kinetics. The immobilization of penicillin acylase resulted in a slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted the structural and conformational stability to this enzyme. The immobilized enzyme also retained a high catalytic activity and showed the increased thermal stability compared with a free enzyme. By comparison of decimal reduction time values obtained at 50°C, it can be concluded that the immobilized enzyme was approximately 5-fold more stable than a free enzyme. The immobilization procedure developed is quite simple and easily reproduced, and provides a promising solution for the application of penicillin acylase for the purpose of 6-aminopenicillanic acid production. PB - Association of the Chemical Engineers of Serbia T2 - Chemical Industry & Chemical Engineering Quarterly T1 - Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier EP - 210 IS - 4 SP - 205 VL - 13 DO - 10.2298/CICEQ0704205Z ER -
@article{ author = "Žuža, Milena and Šiler-Marinković, Slavica and Knežević, Zorica", year = "2007", abstract = "This paper reports the covalent immobilization of penicillin G acylase from E. coli on Sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes the properties of the immobilized enzyme. Due to its versatility to mediate hydrolysis of penicillins and semi-synthetic B-lactam antibiotics synthesis reactions, the selected enzyme belongs to a class of biocatalysts of great industrial interest. The immobilized enzyme was characterized in its pH and thermal stability and reaction kinetics. The immobilization of penicillin acylase resulted in a slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted the structural and conformational stability to this enzyme. The immobilized enzyme also retained a high catalytic activity and showed the increased thermal stability compared with a free enzyme. By comparison of decimal reduction time values obtained at 50°C, it can be concluded that the immobilized enzyme was approximately 5-fold more stable than a free enzyme. The immobilization procedure developed is quite simple and easily reproduced, and provides a promising solution for the application of penicillin acylase for the purpose of 6-aminopenicillanic acid production.", publisher = "Association of the Chemical Engineers of Serbia", journal = "Chemical Industry & Chemical Engineering Quarterly", title = "Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier", pages = "210-205", number = "4", volume = "13", doi = "10.2298/CICEQ0704205Z" }
Žuža, M., Šiler-Marinković, S.,& Knežević, Z.. (2007). Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier. in Chemical Industry & Chemical Engineering Quarterly Association of the Chemical Engineers of Serbia., 13(4), 205-210. https://doi.org/10.2298/CICEQ0704205Z
Žuža M, Šiler-Marinković S, Knežević Z. Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier. in Chemical Industry & Chemical Engineering Quarterly. 2007;13(4):205-210. doi:10.2298/CICEQ0704205Z .
Žuža, Milena, Šiler-Marinković, Slavica, Knežević, Zorica, "Preparation and characterization of penicillin acylase immobilized on sepabeads EC-EP carrier" in Chemical Industry & Chemical Engineering Quarterly, 13, no. 4 (2007):205-210, https://doi.org/10.2298/CICEQ0704205Z . .