Characterization of D-lactate dehydrogenase from Pediococcus acidilactici that converts phenylpyruvic acid into phenyllactic acid

Biotechnol Lett. 2012 May;34(5):907-11. doi: 10.1007/s10529-012-0847-1. Epub 2012 Jan 20.

Abstract

The gene coding for D-lactate dehydrogenase (D-LDH) from Pediococcus acidilactici DSM 20284 was cloned and expressed in E. coli. The recombinant enzyme was purified by nickel-affinity chromatography. It converted phenylpyruvic acid (PPA) to 3-phenyllactic acid maximally at 30°C and pH 5.5 with a specific activity of 140 and 422 U/mg for PPA and pyruvate, respectively. The K(m), turnover number (k(cat)), and catalytic efficiency (k(cat)/K(m)) for PPA were 2.9 mM, 305 s(-1), and 105 mM(-1) s(-1), respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biotransformation
  • Cats
  • Chromatography, Affinity
  • Cloning, Molecular
  • Enzyme Stability
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Gene Expression
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lactate Dehydrogenases / chemistry
  • Lactate Dehydrogenases / genetics*
  • Lactate Dehydrogenases / metabolism*
  • Lactates / metabolism*
  • Pediococcus / enzymology*
  • Pediococcus / genetics*
  • Phenylpyruvic Acids / metabolism*
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Temperature

Substances

  • Lactates
  • Phenylpyruvic Acids
  • Recombinant Proteins
  • 3-phenyllactic acid
  • Lactate Dehydrogenases
  • D-lactate dehydrogenase
  • phenylpyruvic acid