Characterization of the activity of penicillin G acylase immobilized onto nylon membranes grafted with different acrylic monomers by means of γ-radiation

2000 ◽  
Vol 8 (4-6) ◽  
pp. 233-244 ◽  
Author(s):  
M.S Mohy Eldin ◽  
U Bencivenga ◽  
S Rossi ◽  
P Canciglia ◽  
F.S Gaeta ◽  
...  
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G ◽  
Γ Radiation ◽  
Acrylic Monomers

Visualized characterization of bacterial penicillin G acylase for the hydrolysis of β-lactams using an activatable NIR fluorescent probe

2020 ◽  
Vol 310 ◽  
pp. 127872 ◽  
Author(s):  
Zhenhao Tian ◽  
Lei Feng ◽  
Lu Li ◽  
Xiangge Tian ◽  
Jingnan Cui ◽  
...  
Keyword(s):  
Fluorescent Probe ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Hydrolysis Of

Immobilization and Characterization of Penicillin G Acylase (PGA) Immobilized on Magnetic Ni0.5Zn0.5Fe2O4 Nanoparticles

2016 ◽  
Vol 16 (1) ◽  
pp. 182-188 ◽  
Author(s):  
Ruijiang Liu ◽  
Jiawen Fan ◽  
Yewang Zhang ◽  
Peng Wang ◽  
Xiangqian Shen
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G

scholarly journals Characterization of the penicillin G acylase from Bacillus megaterium ATCC 14945

2005 ◽  
Vol 48 (spe) ◽  
pp. 105-111 ◽  
Author(s):  
Vanessa Ribeiro de Souza ◽  
Ana C. G. Silva ◽  
Laura Marina Pinotti ◽  
Heloísa Sobreiro Selistre Araújo ◽  
Raquel de Lima Camargo Giordano
Keyword(s):  
Bacillus Megaterium ◽  
Reaction Rate ◽  
Penicillin G Acylase ◽  
Hydrolysis Rate ◽  
Penicillin G ◽  
Average Molecular Mass ◽  
Influence Of Temperature ◽  
Sds Page ◽  
Page Electrophoresis

The purpose of this work was to characterize the enzyme penicillin G acylase (PGA) produced by Bacillus megaterium. Purification of the enzyme by ultra/diafiltration did not allow the detection of the PGA band by SDS-PAGE electrophoresis due to the high content of remaining proteins. However, using the DNA of the microorganism, it was possible to replicate the genes of the two B. megaterium PGA reported in literature, showing that the enzyme consisted of two sub-units, having 245 and 537 amino acids each and an average molecular mass of 26950 and 59070 Da, respectively. The parameters studied were: 1) the influence of temperature in the 25-60(0)C range, 2) pH in the 5-10 range and 3) substrate concentration, this was tested to obtain results on the Penicillin G hydrolysis reaction rate, using the initial velocities approach. The maximum hydrolysis rate was obtained at 37ºC and pH 8.0. The Michaelis-Menten model fitted well, resulting in estimated Km and Vmax parameters values of 1.83 mM and 0.165*10-3 mmol/min/UI, respectively.

Resolution of α/β-amino acids by enantioselective penicillin G acylase from Achromobacter sp .

2015 ◽  
Vol 122 ◽  
pp. 240-247 ◽  
Author(s):  
Michal Grulich ◽  
Jan Brezovský ◽  
Václav ŠtĿpánek ◽  
Andrea Palyzová ◽  
Eva Kyslíková ◽  
...  
Keyword(s):  
Amino Acids ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Achromobacter Sp
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