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. .
TY - 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 - conv_767
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 = "conv_767"
}
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.
conv_767
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.
conv_767 .
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,
conv_767 .
