Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier
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 kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillin and semi-synthetic b-lactam antibiotics synthesis reactions. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems. .
Source:
Zbornik radova Tehnološkog fakulteta, Leskovac, 2007, 16, 33-42Publisher:
- Univerzitet u Nišu - Tehnološki fakultet, Leskovac
Institution/Community
Tehnološko-metalurški fakultetTY - JOUR AU - Žuža, Milena AU - Šiler-Marinković, Slavica AU - Knežević, Zorica PY - 2007 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1195 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 kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillin and semi-synthetic b-lactam antibiotics synthesis reactions. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems. . PB - Univerzitet u Nišu - Tehnološki fakultet, Leskovac T2 - Zbornik radova Tehnološkog fakulteta, Leskovac T1 - Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier EP - 42 IS - 16 SP - 33 UR - https://hdl.handle.net/21.15107/rcub_technorep_1195 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 kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillin and semi-synthetic b-lactam antibiotics synthesis reactions. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems. .", publisher = "Univerzitet u Nišu - Tehnološki fakultet, Leskovac", journal = "Zbornik radova Tehnološkog fakulteta, Leskovac", title = "Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier", pages = "42-33", number = "16", url = "https://hdl.handle.net/21.15107/rcub_technorep_1195" }
Žuža, M., Šiler-Marinković, S.,& Knežević, Z.. (2007). Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier. in Zbornik radova Tehnološkog fakulteta, Leskovac Univerzitet u Nišu - Tehnološki fakultet, Leskovac.(16), 33-42. https://hdl.handle.net/21.15107/rcub_technorep_1195
Žuža M, Šiler-Marinković S, Knežević Z. Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier. in Zbornik radova Tehnološkog fakulteta, Leskovac. 2007;(16):33-42. https://hdl.handle.net/21.15107/rcub_technorep_1195 .
Žuža, Milena, Šiler-Marinković, Slavica, Knežević, Zorica, "Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier" in Zbornik radova Tehnološkog fakulteta, Leskovac, no. 16 (2007):33-42, https://hdl.handle.net/21.15107/rcub_technorep_1195 .