Substrate specificity and product stereochemistry in the dehalogenation of 2-haloacids with the crude enzyme preparation from Pseudomonas putida

Maria Vyazmensky, Shimona Geresh

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Intact cells, disrupted cells (obtained by sonication of the biomass), and crude extracts of Pseudomonas putida strain 109 were shown to have similar dehalogenase activity. An immobilized preparation of dehalogenase on celite retained its activity in polar organic solvents such as dimethyl sulfoxide (DMSO) and dimethylformamide. The nucleophilic substitution of the halogen in 2-bromopropionic acid by water proceeded in the above-mentioned solvents only if at least stoichiometric amounts of water were present in the reaction mixture. The stereochemistry of the product obtained from racemic 2-bromopropionic acid by the action of celite-immobilized disrupted cells of P. putida strain 109 in DMSO differed from that of the enantiomer obtained in an aqueous buffer. The specificity of the enzyme was also tested on other substrates derived from 2-bromopropionic acid.

Original languageEnglish
Pages (from-to)323-328
Number of pages6
JournalEnzyme and Microbial Technology
Volume22
Issue number5
DOIs
StatePublished - 1 Apr 1998

Keywords

  • 2-haloacid dehalogenase
  • Immobilization
  • Organic solvents
  • Stereoselectivity
  • Substrate specificity

Fingerprint

Dive into the research topics of 'Substrate specificity and product stereochemistry in the dehalogenation of 2-haloacids with the crude enzyme preparation from Pseudomonas putida'. Together they form a unique fingerprint.

Cite this