High-level production penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with optimization of carbon sources

2007 ◽  
Vol 41 (3) ◽  
pp. 326-330 ◽  
Author(s):  
Shiwei Cheng ◽  
Qingxun Song ◽  
Dongzhi Wei ◽  
Bingxue Gao
Keyword(s):  
Escherichia Coli ◽  
Carbon Sources ◽  
Alcaligenes Faecalis ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
High Level ◽  
Level Production

scholarly journals High level production of tyrosinase in recombinant Escherichia coli

2013 ◽  
Vol 13 (1) ◽  
Author(s):  
Qun Ren ◽  
Bernhard Henes ◽  
Michael Fairhead ◽  
Linda Thöny-Meyer
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
High Level ◽  
Level Production

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.

High level production of human proapo A-I by fed-batch culture of recombinant Escherichia coli

1993 ◽  
Vol 75 (2) ◽  
pp. 155-157 ◽  
Author(s):  
Kunihiko Ohta ◽  
Tatsuro Shibui ◽  
Yuuki Morimoto ◽  
Shinji Iijima ◽  
Takeshi Kobayashi
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
High Level ◽  
Level Production

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
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