Extraction penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with cetyl-trimethylammoniumbromide

2006 ◽  
Vol 32 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Shiwei Cheng ◽  
Dongzhi Wei ◽  
Qingxun Song
Keyword(s):  
Escherichia Coli ◽  
Alcaligenes Faecalis ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G

scholarly journals Cloning, Overexpression, and Characterization of a Novel Thermostable Penicillin G Acylase from Achromobacter xylosoxidans: Probing the Molecular Basis for Its High Thermostability

2004 ◽  
Vol 70 (5) ◽  
pp. 2764-2770 ◽  
Author(s):  
Gang Cai ◽  
Songcheng Zhu ◽  
Sheng Yang ◽  
Guoping Zhao ◽  
Weihong Jiang
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Molecular Basis ◽  
Alcaligenes Faecalis ◽  
Amino Acid Identity ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Achromobacter Xylosoxidans ◽  
High Thermostability ◽  
Arginine Residues

ABSTRACT The gene encoding a novel penicillin G acylase (PGA), designated pgaW, was cloned from Achromobacter xylosoxidans and overexpressed in Escherichia coli. The pgaW gene contains an open reading frame of 2,586 nucleotides. The deduced protein sequence encoded by pgaW has about 50% amino acid identity to several well-characterized PGAs, including those of Providencia rettgeri, Kluyvera cryocrescens, and Escherichia coli. Biochemical studies showed that the optimal temperature for this novel PGA (PGA650) activity is greater than 60°C and its half-life of inactivation at 55°C is four times longer than that of another previously reported thermostable PGA from Alcaligenes faecalis (R. M. D. Verhaert, A. M. Riemens, J. V. R. Laan, J. V. Duin, and W. J. Quax, Appl. Environ. Microbiol. 63:3412-3418, 1997). To our knowledge, this is the most thermostable PGA ever characterized. To explore the molecular basis of the higher thermostability of PGA650, homology structural modeling and amino acid composition analyses were performed. The results suggested that the increased number of buried ion pair networks, lower N and Q contents, excessive arginine residues, and remarkably high content of proline residues in the structure of PGA650 could contribute to its high thermostability. The unique characteristic of higher thermostability of this novel PGA provides some advantages for its potential application in industry.

Periplasmic penicillin G acylase activity in recombinant Escherichia coli cells permeabilized with organic solvents

2003 ◽  
Vol 39 (3) ◽  
pp. 301-305 ◽  
Author(s):  
A. De León ◽  
B. Garcı́a ◽  
A.P. Barba de la Rosa ◽  
F. Villaseñor ◽  
A. Estrada ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Organic Solvents ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Escherichia Coli Cells

Optimization of the host–plasmid interaction in the recombinant Escherichia coli strains overproducing penicillin G acylase

2004 ◽  
Vol 35 (1) ◽  
pp. 74-80 ◽  
Author(s):  
Renata Valešová ◽  
Lenka Hollerová-Sobotková ◽  
Václav Štěpánek ◽  
Pavel Kyslı́k
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G

Production of penicillin G amidase from Alcaligenes faecalis in a recombinant Escherichia coli

2009 ◽  
Vol 40 (2) ◽  
pp. 233-236 ◽  
Author(s):  
Bin-Quan Gou ◽  
Ju Chu ◽  
Si-Liang Zhang ◽  
Yong-Hong Wang ◽  
Ying-Ping Zhuang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alcaligenes Faecalis ◽  
Recombinant Escherichia Coli ◽  
Penicillin G

Efficient enzymatic synthesis of ampicillin by mutant Alcaligenes faecalis penicillin G acylase

2015 ◽  
Vol 199 ◽  
pp. 62-68 ◽  
Author(s):  
Senwen Deng ◽  
Erzheng Su ◽  
Xiaoqiang Ma ◽  
Shengli Yang ◽  
Dongzhi Wei
Keyword(s):  
Enzymatic Synthesis ◽  
Alcaligenes Faecalis ◽  
Penicillin G Acylase ◽  
Penicillin G
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