Isolation of enantioselective α-hydroxyacid dehydrogenases based on a high-throughput screening method

Bioprocess Biosyst Eng. 2012 Nov;35(9):1515-22. doi: 10.1007/s00449-012-0741-1. Epub 2012 May 5.

Abstract

To isolate enantioselective α-hydroxyacid dehydrogenases (α-HADHs), a high-throughput screening method was established. 2,4-Dinitrophenylhydrazine solution forms a red-brown complex with ketoacid produced during the α-HADH-mediated oxidation of α-hydroxyacid. The complex can be easily quantified by spectrophotometric measurement at 458 nm. The enantioselectivity of α-HADH in each strain can be measured with this colorimetric method using (R)- and (S)-α-hydroxyacid concurrently as substrates to evaluate the apparent enantioselectivity (E (app)). The E (app) closely matches the value of true enantioselectivity (E (true)) determined by HPLC analysis. With this method, a total of 34 stains harboring enantioselective α-HADHs were selected from 526 potential α-HADH-producing microorganisms. Pseudomonas aeruginosa displayed the highest (S)-enantioselective α-HADH activity. This strain appears promising for potential application in industry to produce (R)-α-hydroxyacids. The method described herein represents a useful tool for the high-throughput isolation of enantioselective α-HADHs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases* / chemistry
  • Alcohol Oxidoreductases* / isolation & purification
  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / isolation & purification
  • Phenylhydrazines / chemistry*
  • Pseudomonas aeruginosa / enzymology*
  • Sinorhizobium / enzymology
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Phenylhydrazines
  • 2,4-dinitrophenylhydrazine
  • Alcohol Oxidoreductases
  • D-2-hydroxyacid dehydrogenase