Biotechnology Letters

, Volume 31, Issue 3, pp 443–448 | Cite as

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

Original Research Paper

Abstract

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.

Keywords

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

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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  1. 1.Department of Food Science and Human NutritionChonbuk National UniversityJeonjuSouth Korea
  2. 2.Research Institute of Human EcologyChonbuk National UniversityJeonjuSouth Korea
  3. 3.NITE Biological Resource Center (NBRC)National Institute of Technology and Evaluation (NITE)Kisarazu-shiJapan

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