Covalent immobilization of penicillin G acylase onto amine-functionalized PVC membranes for 6-APA production from penicillin hydrolysis process. II. Enzyme immobilization and characterization

2012 ◽  
Vol 125 (5) ◽  
pp. 3820-3828 ◽  
Author(s):  
M. S. Mohy Eldin ◽  
H. A. El Enshasy ◽  
M. E. Hassan ◽  
B. Haroun ◽  
E. A. Hassan
Keyword(s):  
Enzyme Immobilization ◽  
Covalent Immobilization ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Amine Functionalized ◽  
Hydrolysis Process ◽  
Pvc Membranes

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

Covalent Immobilization of Penicillin G Acylase onto Grafted Alginate Beads

2012 ◽  
Vol 1 (2) ◽  
pp. 185-191 ◽  
Author(s):  
MagdyM. M. Elnashar ◽  
AliO. Ali ◽  
MohgaS. Abdallah ◽  
RagaaR. Hamed
Keyword(s):  
Alginate Beads ◽  
Covalent Immobilization ◽  
Penicillin G Acylase ◽  
Penicillin G

scholarly journals High Stabilization of Enzymes Immobilized on Rigid Hydrophobic Glyoxyl-Supports: Generation of Hydrophilic Environments on Support Surfaces

Catalysts ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 676
Author(s):  
Alejandro H. Orrego ◽  
María Romero-Fernández ◽  
María del Carmen Millán-Linares ◽  
Justo Pedroche ◽  
José M. Guisán ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Enzyme Immobilization ◽  
Thermus Thermophilus ◽  
Immobilized Enzymes ◽  
Covalent Immobilization ◽  
Penicillin G ◽  
Support Surface ◽  
Continuous Flow Reactors ◽  
Aldehyde Groups ◽  
Similar Density

Very rigid supports are useful for enzyme immobilization to design continuous flow reactors and/or to work in non-conventional media. Among them, epoxy-methacrylic supports are easily functionalized with glyoxyl groups, which makes them ideal candidates for enzyme stabilization via multipoint covalent immobilization. However, these supports present highly hydrophobic surfaces, which might promote very undesirable effects on enzyme activity and/or stability. The hydrophilization of the support surface after multipoint enzyme immobilization is proposed here as an alternative to reduce these undesirable effects. The remaining aldehyde groups on the support are modified with aminated hydrophilic small molecules (glycine, lysine or aspartic acid) in the presence of 2-picoline borane. The penicillin G acylase from Escherichia coli (PGA) and alcohol dehydrogenase from Thermus thermophilus HB27 (ADH2) were immobilized on glyoxyl-functionalized agarose, Relizyme and Relisorb. Despite the similar density of aldehyde groups displayed by functionalized supports, their stabilization effects on immobilized enzymes were quite different: up to 300-fold lower by hydrophobic supports than by highly hydrophilic glyoxyl-agarose. A dramatic increase in the protein stabilities was shown when a hydrophilization treatment of the hydrophobic support surface was done. The PGA immobilized on the glyoxyl-Relisorb hydrophilized with aspartic acid becomes 280-fold more stable than without any treatment, and it is even more stable than the PGA immobilized on the glyoxyl agarose.

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