scholarly journals Gold Nanoparticles for Colorimetric detection of hydrolysis of antibiotics by penicillin G acylase

2010 ◽  
Vol 01 (04) ◽  
pp. 322-329 ◽  
Author(s):  
Neha R. Tiwari ◽  
Ambrish Rathore ◽  
Asmita Prabhune ◽  
Sulabha K. Kulkarni
Keyword(s):  
Gold Nanoparticles ◽  
Colorimetric Detection ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Hydrolysis Of

Hydrolysis of Penicillin G by Penicillin G Acylase Immobilized on Chitosan Microbeads in Different Reactor Systems

2011 ◽  
Vol 34 (10) ◽  
pp. 1706-1714 ◽  
Author(s):  
M. G. Žuža ◽  
B. M. Obradović ◽  
Z. D. Knežević-Jugović
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G ◽  
Hydrolysis Of

Asymmetric hydrolysis of dimethyl phenylmalonate by immobilized penicillin G acylase from E. coli

2007 ◽  
Vol 40 (5) ◽  
pp. 997-1000 ◽  
Author(s):  
Zaida Cabrera ◽  
Fernando Lopez-Gallego ◽  
Gloria Fernandez-Lorente ◽  
Jose M. Palomo ◽  
Tamara Montes ◽  
...  
Keyword(s):  
Penicillin G Acylase ◽  
Penicillin G ◽  
E Coli ◽  
Immobilized Penicillin G Acylase ◽  
Hydrolysis Of

scholarly journals Rapid burst kinetics in the hydrolysis of 4-nitrophenyl acetate by penicillin G acylase from Kluyvera citrophila. Effects of mutation F360V on rate constants for acylation and de-acylation

1996 ◽  
Vol 316 (2) ◽  
pp. 409-412 ◽  
Author(s):  
A Roa ◽  
M L Goble ◽  
J L García ◽  
C Acebal ◽  
R Virden
Keyword(s):  
Rate Constants ◽  
Acetyl Derivative ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Side Chain ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Burst Kinetics ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of release of 4-nitrophenol were followed by stopped-flow spectrophotometry with two 4-nitrophenyl ester substrates of penicillin G acylase from Kluyvera citrophila. With the ester of acetic acid, but not of propionic acid, there was a pre-steady-state exponential phase, the kinetics of which were inhibited by phenylacetic acid (a product of hydrolysis of specific substrates) to the extent predicted from Ki values. This was interpreted as deriving from rapid formation (73 mM-1·s-1) and slow hydrolysis (0.76 s-1) of an acetyl derivative of the side chain of the catalytic-centre residue Ser-290. With the mutant F360V, which differs from the wild-type enzyme in its ability to hydrolyse adipyl-L-leucine and has a kcat for 4-nitrophenyl acetate one-twentieth that of the wild-type enzyme, the corresponding values for the rates of formation and hydrolysis of the acetyl-enzyme were 11.1 mM-1·s-1 and 0.051 s-1 respectively. The ratio of these rate constants was three times that for the wild-type enzyme, suggesting that the mutant is less impaired in the rate of formation of an acetyl-enzyme than in its subsequent hydrolysis.

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

scholarly journals Impact of polybasic alcohols on biocompatibility and selectivity of Penicillin G Acylase for kinetically controlled synthesis

2015 ◽  
Author(s):  
Yi-Feng Shi ◽  
Zhu-An Cao ◽  
Zhong-Yao Shen
Keyword(s):  
Methyl Ester ◽  
Ethylene Glycol ◽  
Butyl Alcohol ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Acyl Donor ◽  
Controlled Synthesis ◽  
Kinetically Controlled ◽  
Hydrolysis Of ◽  
Kinetically Controlled Synthesis

The enzyme catalyzed synthesis of cephalexin (CEX) from 7-amino-3-deacetoxycephalosporanic acid (7-ADCA) and D-a-phenylglycine methyl ester (PGM) by Penicillin G acylase (PGA) is a model for kinetically controlled synthesis. The parallel hydrolysis of PGM, the activated acyl donor, is the principle competing pathway in this reaction, limiting the synthetic yield and reaction efficiency. To improve the performance of PGA catalyzed CEX synthesis, the biocompatibility and selectivity of various co-solvents were investigated. Polybasic alcohols such as ethylene glycol, glycerol and PEG400 did not cause deleterious changes to the enzyme, whereas monobasic alcohols, such as butyl alcohol, disrupted the PGA activity. Compared with the reaction in aqueous medium, the use of ethylene glycol as a co-solvent was found to have good selectivity in order to facilitate CEX synthesis and significantly minimize PGM hydrolysis. The pH of ethylene glycol medium was also optimized. The mechanism of the enhanced effect of polybasic alcohols as co-solvents on both biocompatibility and selectivity of enzymatic kinetically controlled synthesis is suggested.

scholarly journals Impact of polybasic alcohols on biocompatibility and selectivity of Penicillin G Acylase for kinetically controlled synthesis

2015 ◽  
Author(s):  
Yi-Feng Shi ◽  
Zhu-An Cao ◽  
Zhong-Yao Shen
Keyword(s):  
Methyl Ester ◽  
Ethylene Glycol ◽  
Butyl Alcohol ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Acyl Donor ◽  
Controlled Synthesis ◽  
Kinetically Controlled ◽  
Hydrolysis Of ◽  
Kinetically Controlled Synthesis

The enzyme catalyzed synthesis of cephalexin (CEX) from 7-amino-3-deacetoxycephalosporanic acid (7-ADCA) and D-a-phenylglycine methyl ester (PGM) by Penicillin G acylase (PGA) is a model for kinetically controlled synthesis. The parallel hydrolysis of PGM, the activated acyl donor, is the principle competing pathway in this reaction, limiting the synthetic yield and reaction efficiency. To improve the performance of PGA catalyzed CEX synthesis, the biocompatibility and selectivity of various co-solvents were investigated. Polybasic alcohols such as ethylene glycol, glycerol and PEG400 did not cause deleterious changes to the enzyme, whereas monobasic alcohols, such as butyl alcohol, disrupted the PGA activity. Compared with the reaction in aqueous medium, the use of ethylene glycol as a co-solvent was found to have good selectivity in order to facilitate CEX synthesis and significantly minimize PGM hydrolysis. The pH of ethylene glycol medium was also optimized. The mechanism of the enhanced effect of polybasic alcohols as co-solvents on both biocompatibility and selectivity of enzymatic kinetically controlled synthesis is suggested.

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