Kinetic resolution of 2-hydroxybutanoate racemic mixtures by NAD-independent L-lactate dehydrogenase

Bioresour Technol. 2011 Apr;102(7):4595-9. doi: 10.1016/j.biortech.2011.01.003. Epub 2011 Jan 7.

Abstract

Optically active D-2-hydroxybutanoate is an important building block intermediate for medicines and biodegradable poly(2-hydroxybutanoate). Kinetic resolution of racemic 2-hydroxybutanoate may be a green and desirable alternative for D-2-hydroxybutanoate production. In this work, D-2-hydroxybutanoate at a high concentration (0.197 M) and a high enantiomeric excess (99.1%) was produced by an NAD-independent L-lactate dehydrogenase (L-iLDH) containing biocatalyst. 2-Oxobutanoate, another important intermediate, was co-produced at a high concentration (0.193 M). Using a simple ion exchange process with the macroporous anion exchange resin D301, D-2-hydroxybutanoate was separated from the biotransformation system with a high recovery of 84.7%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Butyrates / metabolism
  • Catalysis
  • Chemistry, Pharmaceutical / methods*
  • Hydroxybutyrates / metabolism*
  • Ion Exchange Resins
  • Kinetics
  • L-Lactate Dehydrogenase / metabolism*
  • Pseudomonas
  • Tetrazolium Salts
  • Thiazoles

Substances

  • Butyrates
  • Hydroxybutyrates
  • Ion Exchange Resins
  • Tetrazolium Salts
  • Thiazoles
  • alpha-ketobutyric acid
  • L-Lactate Dehydrogenase
  • thiazolyl blue
  • 2-hydroxybutyric acid