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Propioin synthesis using thiamine diphosphate-dependent enzymes.

Renaud J Mikolajek1, Antje C Spiess, Martina Pohl

  • 1Biochemical Engineering, RWTH Aachen University, Worringer Weg 1, Aachen 52056, Germany. mikolajek@biovt.rwth-aachen.de

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|February 19, 2009
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Benzaldehyde lyase (BAL) and benzoylformate decarboxylase (BFD) catalyze asymmetric synthesis of propioin from propanal. BFD shows greater stability and produces (R)-propioin, while BAL yields (S)-propioin.

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Area of Science:

  • Biocatalysis
  • Enzyme kinetics
  • Asymmetric synthesis

Background:

  • Thiamine diphosphate-dependent enzymes, Benzaldehyde lyase (BAL) and benzoylformate decarboxylase (BFD), share structural and catalytic similarities.
  • These enzymes are crucial for C-C bond formation and cleavage reactions.

Purpose of the Study:

  • To investigate the asymmetric synthesis of propioin from propanal using BAL and BFD.
  • To compare the stability, kinetics, and enantioselectivity of BAL and BFD under reaction conditions.

Main Methods:

  • Enzymatic synthesis of propioin in aqueous solution using a batch reactor.
  • Kinetic analysis including Michaelis-Menten kinetics and v/[S]-plots.
  • Determination of enantiomeric excess (ee) of the synthesized propioin.

Main Results:

  • Both BAL and BFD catalyze the asymmetric synthesis of propioin from propanal.
  • BFD exhibits higher stability than BAL under reaction conditions and during storage.
  • BAL produced (S)-propioin with 35% ee, while BFD yielded (R)-propioin with 67% ee.

Conclusions:

  • BFD is a more robust biocatalyst for propioin synthesis compared to BAL.
  • The enzymes demonstrate complementary enantioselectivity, producing opposite propioin enantiomers.
  • Further studies on enzyme engineering could optimize propioin synthesis and enhance enantioselectivity.