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Penicillin amidase

About: Penicillin amidase is a research topic. Over the lifetime, 576 publications have been published within this topic receiving 15563 citations. The topic is also known as: penicillin amidohydrolase & ampicillin acylase.


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Journal ArticleDOI
TL;DR: In this article, a recombinant strain Bacillus subtilis WB600 (pMA5) was used to produce Alcaligenes faecalis penicillin G acylase (PGA).

26 citations

Journal ArticleDOI
TL;DR: A new and integrated method for the evaluation of industrial enzymes is proposed and the application of this method to the enzyme penicillin G acylase from Clyvera citrophila shows very interesting industrial propects.
Abstract: We propose a new and integrated method for the evaluation of industrial enzymes. The application of this method to the enzyme penicillin G acylase fromKlyvera citrophila shows very interesting industrial propects. This acylase presents a much better stability agains heat, pH or organic cosovents as compared with the more popular enzyme fromEscherichia coli. In addition, this enzyme is very easy to immobilize through its amine groups and to stabilize through multipoint covalent attachment on activated pre-existing supports.

26 citations

Journal ArticleDOI
TL;DR: Aims: Optimization of 6‐aminopenicillanic acid (6‐APA) production using cross‐linked enzyme aggregates (CLEA) of Bacillus badius penicillin G acylase (PAC).
Abstract: Aims: Optimization of 6-aminopenicillanic acid (6-APA) production using cross-linked enzyme aggregates (CLEA) of Bacillus badius penicillin G acylase (PAC). Methods and Results: CLEA–PAC was prepared using purified/partially purified PAC with phenylacetic acid as active-site blocking agent and glutaraldehyde as cross-linker. Conversion of penicillin G to 6-APA by CLEA–PAC was optimized using response surface methodology (RSM) (central composite rotatable design) consisting of a three-factor–two-level pattern with 20 experimental runs. Conclusion: Nearly, 80% of immobilization yield was obtained when partially purified enzyme was used for the preparation of CLEA–PAC. Quantitative conversion of penicillin G to 6-APA was observed within 60 min and the CLEA–PAC was reusable for 20 repeated cycles with 100% retention of enzyme activity. Significance and Impact of the Study: The faster conversion of penicillin G to 6-APA by CLEA–PAC and efficient reusability holds a strong potential for the industrial application.

26 citations

Journal ArticleDOI
TL;DR: Evidence is presented that the active enzyme is localized in the periplasmic space and maturation of pro-enzyme occurs during transport through the cytoplasmic membrane or rapidly after its entrance in theperiplasm.

25 citations

Journal ArticleDOI
TL;DR: The results indicated good enzyme-binding efficiency of the pre-treated membrane, and an increased stability of the immobilized PGA towards pH and temperature, and the advantage of using non-isothermal bioreactors in biotechnological processes, including pharmaceutical applications, is discussed.
Abstract: A new hydrophobic and catalytic membrane was prepared by immobilizing Penicillin G acylase (PGA, EC.3.5.1.11) from E. coli on a nylon membrane, chemically grafted with butylmethacrylate (BMA). Hexamethylenediamine (HMDA) and glutaraldehyde (Glu) were used as a spacer and coupling agent, respectively. PGA was used for the enzymatic synthesis of cephalexin, using D(-)-phenylglycine methyl ester (PGME) and 7-amino-3-deacetoxycephalosporanic acid (7-ADCA) as substrates. Several factors affecting this reaction, such as pH, temperature, and concentrations of substrates were investigated. The results indicated good enzyme-binding efficiency of the pre-treated membrane, and an increased stability of the immobilized PGA towards pH and temperature. Calculation of the activation energies showed that cephalexin production by the immobilized biocatalyst was limited by diffusion, resulting in a decrease of enzyme activity and substrate affinity. Temperature gradients were employed as a way to reduce the effects of diffusion limitation. Cephalexin was found to linearly increase with the applied temperature gradient. A temperature difference of about 3 degrees C across the catalytic membrane resulted into a cephalexin synthesis increase of 100% with a 50% reduction of the production times. The advantage of using non-isothermal bioreactors in biotechnological processes, including pharmaceutical applications, is also discussed.

25 citations

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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20234
20222
20183
20175
20165
20153