Biotechnology Letters

, Volume 25, Issue 10, pp 809–814 | Cite as

Simultaneous synthesis of enantiomerically pure (R)-1-phenylethanol and (R)-α-methylbenzylamine from racemic α-methylbenzylamine using ω-transaminase/alcohol dehydrogenase/glucose dehydrogenase coupling reaction

  • Hyungdon Yun
  • Yung-Hun Yang
  • Byung-Kwan Cho
  • Bum-Yeol Hwang
  • Byung-Gee Kim

Abstract

A simultaneous synthesis of (R)-1-phenylethanol and (R)-α-methylbenzylamine from racemic α-methylbenzyl- amine was achievied using an ω-transaminase, alcohol dehydrogenase, and glucose dehydrogenase in a coupled reaction. Racemic α-methylbenzylamine (100 mM) was converted to 49 mM (R)-1-phenylethanol (> 99% ee) and 48 mM (R)-α-methylbenzylamine (> 98% ee) in 18 h at 37 °C. This method was also used to overcome product inhibition of ω-TA by the ketone product in the kinetic resolution of racemic amines at high concentration.

alcohol dehydrogenase glucose dehydrogenase kinetic resolution NADPH regeneration ω-transaminase 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Andersson M, Holmberg H, Adlercreutz P (1998) Evaluation of Alcaligenes eutrophus cells as an NADH regenerating catalyst in organic-aqueous two-phase system. Biotechnol. Bioeng. 57: 79–86.Google Scholar
  2. Bradshaw CW, Hummel W, Wong C-H (1992) Lactobacillus kefir ADH: a useful catalyst for synthesis. J. Org. Chem. 57: 1532–1536.Google Scholar
  3. Burdette DS, Zeikus JG (1994) Purification of acetaldehyde dehydrogenase and ADHs from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-ADH (2° ADH) as a bifunctional ADH-acetyl-CoA reductive thioesterase. Biochem. J. 302: 163–170.Google Scholar
  4. Fujita Y, Ramaley R, Freese E (1977) Location and properties GDHin sporulating cells and spores of Bacillus subtilis. J. Bacteriol. 132: 282–293.Google Scholar
  5. Galkin A, Kulakova L, Yoshimura T, Soda K, Esaki N (1997) Synthesis of optically active amino acids from ?-keto acids with Escherichia coli cells expressing heterologous genes. Appl. Environ. Microbiol. 63: 4651–4656.Google Scholar
  6. Hummel W (1999) Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol. 17: 487–492.Google Scholar
  7. Koeller KM, Wong CH (2001) Enzymes for chemical synthesis. Nature 409: 232–240.Google Scholar
  8. Koh JH, Jung HM, Kim M-J, Park J (1999) Enzymatic resolution of secondary alcohols coupled with ruthenium-catalyzed racemization without hydrogen mediator. Tetrahedron Lett. 40: 6281–6284.Google Scholar
  9. Lampel KA, Uratani B, Chaudhry GR, Ramaley RF, Rudikoff S (1986) Characterization of the developmentally regulated Bacillus subtilis. J. Bacteriol. 166: 238–243.Google Scholar
  10. Sambrook J, Fritsch EF, Maniatis T (1989) Molecular Cloning: A Laboratory Manual,2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.Google Scholar
  11. Seelbach K, Kragl U (1997) Nanofiltration membranes for cofactor retention in continuous enzymatic synthesis. Enzyme Microb. Technol. 20: 389–392.Google Scholar
  12. Shin J-S, Kim B-G (1997) Kinetic resolution of ?-methylbenzylamine with ?-TA screened from soil microorganisms: application of a biphasic system to overcome product inhibition. Biotechnol. Bioeng. 55: 348–358.Google Scholar
  13. Shin J-S, Kim B-G (1998) Kinetic modeling of ?-transamination for enzymatic kinetic resolution of ?-methylbenzylamine. Biotechnol. Bioeng. 60: 534–540.Google Scholar
  14. Shin J-S, Kim B-G, Liese A, Wandrey C (2001) Kinetic resolution of chiral amines using enzyme-membrane reactor. Biotechnol. Bioeng. 73: 179–187.Google Scholar

Copyright information

© Kluwer Academic Publishers 2003

Authors and Affiliations

  • Hyungdon Yun
    • 1
  • Yung-Hun Yang
    • 1
  • Byung-Kwan Cho
    • 1
  • Bum-Yeol Hwang
    • 1
  • Byung-Gee Kim
    • 1
  1. 1.School of Chemical Engineering and Institute of Molecular Biology and GeneticsSeoul National UniversitySeoulKorea

Personalised recommendations