Original Research Paper

Biotechnology Letters

, Volume 31, Issue 3, pp 443-448

First online:

Enhanced synthesis of l-threo-3,4-dihydroxyphenylserine by high-density whole-cell biocatalyst of recombinant l-threonine aldolase from Streptomyces avelmitilis

  • Sang-Ho BaikAffiliated withDepartment of Food Science and Human Nutrition, Chonbuk National UniversityResearch Institute of Human Ecology, Chonbuk National University Email author 
  • , Hideki YoshiokaAffiliated withNITE Biological Resource Center (NBRC), National Institute of Technology and Evaluation (NITE)

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l-threo-3,4-Dihydroxyphenylserine (DOPS) is a chiral unnatural β-hydroxy amino acid used for the treatment of Parkinson disease. We developed a continuous bioconversion system for DOPS production that uses whole-cell biocatalyst of recombinant Escherichia coli expressing l-threonine aldolase (l-TA) genes cloned from Streptomyces avelmitilis MA-4680. Maximum conversion rates were observed at 2 M glycine, 145 mM 3,4-dihydroxybenzaldehyde, 0.75% Triton-X, 5 g E. coli cells/l, pH 6.5 and 10°C. In the optimized condition, overall productivity was 8 g/l, which represents 40 times the synthesis yield possible with no optimization of conditions.


β-Hydroxy amino acid l-threo-2,3-Dihydroxyphenylserine l-Threonine aldolase Whole-cell conversion