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l-Tryptophan Production by Achromobacter liquidum.

T Ujimaru1, T Kakimoto, I Chibata

  • 1Research Laboratory of Applied Biochemistry, Tanabe Seiyaku Co., Ltd., Yodogawa-ku, Osaka 532, Japan.

Applied and Environmental Microbiology
|July 1, 1983
PubMed
Summary

Researchers optimized conditions for producing tryptophanase and synthesizing l-tryptophan using Achromobacter liquidum. This method efficiently converts l-serine and indole to l-tryptophan with high yield.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Production

Background:

  • Tryptophanase is a key enzyme in tryptophan metabolism.
  • Efficient microbial production of tryptophanase and synthesis of l-tryptophan are crucial for various applications.

Purpose of the Study:

  • To determine optimal conditions for tryptophanase production by Achromobacter liquidum.
  • To investigate the efficient conversion of l-serine and indole to l-tryptophan using the enzyme.

Main Methods:

  • Optimized culture media and conditions (temperature, shaking) for enzyme production.
  • Investigated reaction parameters (substrate concentration, cofactor) for l-tryptophan synthesis.
  • Isolated and quantified the synthesized l-tryptophan.

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Main Results:

  • Achieved tryptophanase production of 0.750 U/ml (degradation) and 0.294 U/ml (synthesis).
  • Maximized l-tryptophan synthesis at 37°C with 60 mg/ml l-serine, 60 mg/ml indole, and 0.5 mM pyridoxal phosphate.
  • Obtained 96 mg/ml of l-tryptophan after 3 days, with an 85.4% isolation yield.

Conclusions:

  • Established effective conditions for both tryptophanase production and l-tryptophan synthesis.
  • Demonstrated a high-yield, efficient method for microbial l-tryptophan production.
  • The findings support the use of Achromobacter liquidum for industrial l-tryptophan synthesis.