Covalent immobilization and characterization of penicillin G acylase on magnetic Fe2O3/Fe3O4 heterostructure nanoparticles prepared via a novel solution combustion and gel calcination process

2020 ◽  
Vol 162 ◽  
pp. 1587-1596 ◽  
Author(s):  
Ruijiang Liu ◽  
Wei Huang ◽  
Shuai Pan ◽  
You Li ◽  
Lulu Yu ◽  
...  
Keyword(s):  
Covalent Immobilization ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Solution Combustion ◽  
Calcination Process

Stabilization of heterodimeric enzyme by multipoint covalent immobilization: Penicillin G acylase fromKluyvera citrophila

1993 ◽  
Vol 42 (4) ◽  
pp. 455-464 ◽  
Author(s):  
José M. Guisán ◽  
Gregorio Alvaro ◽  
Roberto Fernandez-Lafuente ◽  
Cristina M. Rosell ◽  
Jose L. Garcia ◽  
...  
Keyword(s):  
Covalent Immobilization ◽  
Penicillin G Acylase ◽  
Penicillin G

Immobilization of modified penicillin G acylase on Sepabeads carriers

2009 ◽  
Vol 63 (2) ◽  
Author(s):  
Milena Žuža ◽  
Nenad Milosavić ◽  
Zorica Knežević-Jugović
Keyword(s):  
Thermal Stability ◽  
Hydrolytic Activity ◽  
Covalent Immobilization ◽  
Stability Study ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Chemically Modified ◽  
Modified Enzyme ◽  
Derivatives Of ◽  
Thermal Stability Study

AbstractAn approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads® carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads® EC EA and Sepabeads® EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5- fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme.

Covalent Immobilization of Penicillin G Acylase onto Fe3O4@Chitosan Magnetic Nanoparticles

2016 ◽  
Vol 26 (5) ◽  
pp. 829-836 ◽  
Author(s):  
Xiao-Min Ling ◽  
Xiang-Yu Wang ◽  
Ping Ma ◽  
Yi Yang ◽  
Jie-Mei Qin ◽  
...  
Keyword(s):  
Magnetic Nanoparticles ◽  
Covalent Immobilization ◽  
Penicillin G Acylase ◽  
Penicillin G

Promotion of multipoint covalent immobilization through different regions of genetically modified penicillin G acylase from E. coli

2010 ◽  
Vol 45 (3) ◽  
pp. 390-398 ◽  
Author(s):  
Valeria Grazú ◽  
Fernando López-Gallego ◽  
Tamara Montes ◽  
Olga Abian ◽  
Ramón González ◽  
...  
Keyword(s):  
Genetically Modified ◽  
Covalent Immobilization ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
E Coli
Sign in / Sign up

Export Citation Format

Share Document