Enhancement of L-2-haloacid dehalogenase expression in Pseudomonas stutzeri DEH138 based on the different substrate specificity between dehalogenase-producing bacteria and their dehalogenases

World J Microbiol Biotechnol. 2015 Apr;31(4):669-73. doi: 10.1007/s11274-015-1817-2. Epub 2015 Feb 11.

Abstract

There was no direct correlation in substrate specificity between the metabolism of Pseudomonas stutzeri DEH138 and its corresponding dehalogenase. Dehalogenase substrates that could be dehalogenated might not be degraded by DEH138 or vice versa. Basing on this, different approaches to enhance L-2-haloacid dehalogenase (L-DEX) production in DEH138 via the combination of non-halogenated compounds with different inducers were applied. The optimum approach to obtain more L-DEX from DEH138 was the combination of DL-lactate and DL-2-chlorobutyrate, with 5.7-fold greater production and 11.7-fold greater productivity of the enzyme after optimization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Butyrates / chemistry
  • Butyrates / metabolism
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / metabolism
  • Kinetics
  • Lactic Acid / chemistry
  • Lactic Acid / metabolism
  • Pseudomonas stutzeri / chemistry
  • Pseudomonas stutzeri / enzymology*
  • Pseudomonas stutzeri / genetics
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Butyrates
  • Lactic Acid
  • Hydrolases
  • 2-haloacid dehalogenase