Biotechnology Letters

, Volume 31, Issue 3, pp 443–448

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

Authors

    • Department of Food Science and Human NutritionChonbuk National University
    • Research Institute of Human EcologyChonbuk National University
  • Hideki Yoshioka
    • NITE Biological Resource Center (NBRC)National Institute of Technology and Evaluation (NITE)
Original Research Paper

DOI: 10.1007/s10529-008-9885-0

Cite this article as:
Baik, S. & Yoshioka, H. Biotechnol Lett (2009) 31: 443. doi:10.1007/s10529-008-9885-0

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 acidl-threo-2,3-Dihydroxyphenylserinel-Threonine aldolaseWhole-cell conversion

Copyright information

© Springer Science+Business Media B.V. 2008