Substrate specificity of immobilized penicillin-G acylase towards penicillin and cephalosporin derivatives was studied. The phenylacetyl moiety can be altered at the α-position with several small substituents. Depending on polarity and size of the substituent, enzyme activity decreases or increases. Insertion or deletion of atoms between the aromatic nucleus of the phenylacetyl group and the center of hydrolysis leads to substrates that are no longer recognized by the enzyme.

1994 ◽  
Vol 4 (2) ◽  
pp. 345-348 ◽  
Author(s):  
Margreet van der Mey ◽  
Erik de Vroom
2012 ◽  
Vol 550-553 ◽  
pp. 1345-1351 ◽  
Author(s):  
Wei Wang ◽  
Zhong Hai Li ◽  
Ji Lie Li ◽  
Yao Hui Wu

Magnetic hydroxyl microspheres were prepared by suspension polymerization and activated by epoxy chloropropane. The magnetic particles were characterized in terms of chemical composition, particle size and electrophoretic mobility. These epoxy-activated magnetic particles were assessed as a new carries for immobilized penicillin G acylase (PGA) by covalent coupling. The oriented PGA immobilization was achieved by employing the interaction electrostatic repulsion between PGA and magnetic supports through adding the phenyl acetic acid (PAA), which resulted in a 1.194-fold increase in the enzyme activity yield as compared to that of untreated PGA. No activity of immobilized PGA was lost after 20 cycles and about 94.28% enzyme activity was retained at the end of the 80th cycle in the batch reaction system.


2000 ◽  
Vol 18 (3) ◽  
pp. 253-258 ◽  
Author(s):  
Gregorio Alvaro ◽  
Josep A. Feliu ◽  
Gloria Caminal ◽  
Josep López-santín ◽  
Pere Clapés

2008 ◽  
Vol 114 (1-3) ◽  
pp. 507-510 ◽  
Author(s):  
Yongjun Lü ◽  
Yanglong Guo ◽  
Yanqin Wang ◽  
Xiaohui Liu ◽  
Yunsong Wang ◽  
...  

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