Over-expression and characterization of the recombinant small heat shock protein from Pyrococcus furiosus

Biotechnol Lett. 2006 Jul;28(14):1089-94. doi: 10.1007/s10529-006-9058-y. Epub 2006 Jun 24.

Abstract

The gene encoding a small heat shock protein (sHSP) from Pyrococcus furiosus was redesigned and chemically synthesized by using bacteria-preferred codons. The gene product was over-expressed in Escherichia coli BL21(DE)(3) and purified to homogeneity. In the presence of this protein, the activities of Taq DNA polymerase, DNA restriction endonuclease HindIII and lysozyme were protected at elevated temperature, and also, thermal aggregation of lysozyme was prevented by this purified recombinant sHSP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Activation
  • Enzyme Stability
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Heat-Shock Proteins, Small / chemistry*
  • Heat-Shock Proteins, Small / genetics
  • Heat-Shock Proteins, Small / metabolism*
  • Protein Engineering / methods*
  • Pyrococcus furiosus / enzymology*
  • Pyrococcus furiosus / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Up-Regulation / genetics

Substances

  • Heat-Shock Proteins, Small
  • Recombinant Proteins