Enhanced activity and enantioselectivity of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1 by acetone treatment

Appl Biochem Biotechnol. 2011 Oct;165(3-4):795-801. doi: 10.1007/s12010-011-9297-9. Epub 2011 Jun 4.

Abstract

To improve the activity and enantioselectivity of hyperthermophilic archaeon Aeropyrum pernix K1 esterase (APE1547) and its mutants, they were purified by acetone-treated method. It was found that the acetone treatment not only caused APE1547 and its mutants to display higher activity and enantioselectivity but also saved more than 90% of time spent in purifying them by Ni-chelating column. In hydrolysis of p-nitrophenyl caprylate, the acetone-treated APE1547 and mutant A containing the following substitutions R11G, L36P, V225A, I551L, and A564T showed 5.7- and 6.9-fold active increase, respectively. In the resolution of 2-octanol acetate, the acetone-treated mutant A had a 9-fold enantioselective increase relative to that purified by Ni-chelating column. In addition, the impact of pH, temperature, and chemical reagents on activity of APE1547 and mutant A was discussed in this paper.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetone / chemistry*
  • Aeropyrum / chemistry
  • Aeropyrum / enzymology*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism*
  • Biocatalysis
  • Caprylates / metabolism
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Stability
  • Esterases / genetics
  • Esterases / metabolism*
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Industrial Microbiology / methods*
  • Mutation
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Archaeal Proteins
  • Caprylates
  • Recombinant Proteins
  • Acetone
  • 4-nitrophenyloctanoate
  • Esterases