Enzymatic Production of Enantiopure Amino Acids from Mono-substituted Hydantoin Substrates

2011 ◽  
pp. 37-54 ◽  
Author(s):  
Gwynneth F. Matcher ◽  
Rosemary A. Dorrington ◽  
Stephanie G. Burton
Keyword(s):  
Amino Acids ◽  
Enzymatic Production

Increased Production of Recombinant O-Phospho-L-Serine Sulfhydrylase from the Hyperthermophilic Archaeon Aeropyrum pernix K1 Using Escherichia coli

2019 ◽  
Vol 8 (1) ◽  
pp. 15-23
Author(s):  
Takashi Nakamura ◽  
Emi Takeda ◽  
Tomoko Kiryu ◽  
Kentaro Mori ◽  
Miyu Ohori ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Industrial Production ◽  
Codon Optimization ◽  
Scale Production ◽  
Enzymatic Production ◽  
Hyperthermophilic Archaeon ◽  
E Coli ◽  
Aeropyrum Pernix ◽  
Natural Amino Acids

Background: O-phospho-L-serine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1 (ApOPSS) is thermostable and tolerant to organic solvents. It can produce nonnatural amino acids in addition to L-cysteine. Objective: We aimed to obtain higher amounts of ApOPSS compared to those reported with previous methods for the convenience of research and for industrial production of L-cysteine and non-natural amino acids. Method: We performed codon optimization of cysO that encodes ApOPSS, for optimal expression in Escherichia coli. We then examined combinations of conditions such as the host strain, plasmid, culture medium, and isopropyl β-D-1-thiogalactopyranoside (IPTG) concentration to improve ApOPSS yield. Results and Discussion: E. coli strain Rosetta (DE3) harboring the expression plasmid pQE-80L with the codon-optimized cysO was cultured in Terrific broth with 0.01 mM IPTG at 37°C for 48 h to yield a 10-times higher amount of purified ApOPSS (650 mg·L-1) compared to that obtained by the conventional method (64 mg·L-1). We found that the optimal culture conditions along with codon optimization were essential for the increased ApOPSS production. The expressed ApOPSS had a 6-histidine tag at the N-terminal, which did not affect its activity. This method may facilitate the industrial production of cysteine and non-natural amino acids using ApOPSS. Conclusion: We conclude that these results could be used in applied research on enzymatic production of L-cysteine in E. coli, large scale production of non-natural amino acids, an enzymatic reaction in organic solvent, and environmental remediation by sulfur removal.

New developments in the chemo-enzymatic production of amino acids

1990 ◽  
pp. 133-186 ◽  
Author(s):  
J. Kamphuis ◽  
W. H. J. Boesten ◽  
Q. B. Broxterman ◽  
H. F. M. Hermes ◽  
J. A. M. van Balken ◽  
...  
Keyword(s):  
Amino Acids ◽  
Enzymatic Production ◽  
New Developments

Optimal Conditions for the Enzymatic Production of l-Aromatic Amino Acids from the Corresponding 5-Substituted Hydantoins

1987 ◽  
Vol 51 (3) ◽  
pp. 729-736
Author(s):  
Kenzo Yokozeki ◽  
Konosuke Sano ◽  
Chikahiko Eguchi ◽  
Hisao Iwagami ◽  
Koji Mitsugi
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Optimal Conditions ◽  
Enzymatic Production

scholarly journals Studies on the Enzymatic Production of L-Amino Acids

1969 ◽  
Vol 22 (8) ◽  
pp. 511-517
Author(s):  
Ichiro Chibata
Keyword(s):  
Amino Acids ◽  
Enzymatic Production

Optimal Conditions for the Enzymatic Production of d-Amino Acids from the Corresponding 5-Substituted Hydantoins

1987 ◽  
Vol 51 (3) ◽  
pp. 715-719
Author(s):  
Kenzo Yokozeki ◽  
Shigeru Nakamori ◽  
Shigeru Yamanaka ◽  
Chikahiko Eguchi ◽  
Koji Mitsugi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Optimal Conditions ◽  
Enzymatic Production

scholarly journals Enzymatic production of D-amino acids from 5-substituted hydantoins. part II Optimal conditions for the enzymatic production of D-amino acids from the corresponding 5-substituted hydantoins.

1987 ◽  
Vol 51 (3) ◽  
pp. 715-719 ◽  
Author(s):  
Kenzo YOKOZEKI ◽  
Shigeru NAKAMORI ◽  
Shigeru YAMANAKA ◽  
Chikahiko EGUCHI ◽  
Koji MITSUGI ◽  
...  
Keyword(s):  
Amino Acids ◽  
Optimal Conditions ◽  
Enzymatic Production
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