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Enhancement of pipecolic acid production by the expression of multiple lysine cyclodeaminase in the Escherichia coli whole-cell system
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  • Yeong-Hoon Han,
  • Tae-Rim Choi,
  • Ye-Lim Park,
  • Jun Young Park,
  • Hun-suk Song,
  • Hyun-Joong Kim,
  • Sun Mi Lee,
  • Sol Lee Park,
  • Hye Soo Lee,
  • Shashi Bhatia,
  • Ranjit Gurav,
  • Yung-Hun Yang
Yeong-Hoon Han
Konkuk University
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Tae-Rim Choi
Konkuk University
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Ye-Lim Park
Konkuk University
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Jun Young Park
Konkuk University
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Hun-suk Song
Konkuk University
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Hyun-Joong Kim
Konkuk University
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Sun Mi Lee
Konkuk University
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Sol Lee Park
Konkuk University
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Hye Soo Lee
Konkuk University
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Shashi Bhatia
Konkuk University
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Ranjit Gurav
Konkuk University
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Yung-Hun Yang
Konkuk University
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Abstract

Pipecolic acid, a non-proteinogenic amino acid, is a metabolite in lysine metabolism and a key chiral precursor in local anesthesia and macrolide antibiotics. To replace the environmentally unfriendly chemical production or preparation procedure of pipecolic acid, many biological synthetic routes have been studied for a long time. Among them, synthesis by lysine cyclodeaminase (LCD), encoded by pipA, has several advantages, including stability of enzyme activity and NAD+ self-regeneration. Thus, we selected this enzyme for pipecolic acid biosynthesis in a whole-cell bioconversion. To construct a robust pipecolic acid production system, we investigated important conditions including expression vector, strain, culture conditions, and other reaction parameters. The most important factors were introduction of multiple pipA genes into the whole-cell system and control of agitation. As a result, we produced 724 mM pipecolic acid (72.4% conversion), and the productivity was 0.78 g/L/h from 1 M L-lysine after 5 days. This is the highest production reported to date.

Peer review status:POSTED

04 Apr 2020Submitted to Biotechnology and Bioengineering
06 Apr 2020Assigned to Editor
06 Apr 2020Submission Checks Completed