Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant alpha-amylase

Appl Environ Microbiol. 1998 Mar;64(3):1163-5. doi: 10.1128/AEM.64.3.1163-1165.1998.

Abstract

Alpha-Amylase from the antarctic psychrophile Altermonas haloplanktis is synthesized at 0 +/- 2 degrees C by the wild strain. This heat-labile alpha-amylase folds correctly when overexpressed in Escherichia coli, providing the culture temperature is sufficiently low to avoid irreversible denaturation. In the described expression system, a compromise between enzyme stability and E. coli growth rate is reached at 18 degrees C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / genetics
  • Gram-Negative Bacteria / enzymology*
  • Protein Conformation
  • Protein Folding*
  • Recombinant Proteins / chemistry
  • alpha-Amylases / chemistry*
  • alpha-Amylases / genetics
  • alpha-Amylases / isolation & purification

Substances

  • Recombinant Proteins
  • alpha-Amylases