Engineering thermolysin-like proteases whose stability is largely independent of calcium

OR Veltman, G Vriend, B vandenBurg, F Hardy, G Venema, VGH Eijsink

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Scopus)

Abstract

Thermal stability of the thermolysin-like protease produced by Bacillus stearothermophilus (TLP-ste) is highly dependent on calcium at concentrations in the millimolar range. We describe the rational design and production of a fully active TLP-ste variant whose stability is only slightly dependent on calcium concentration. (C) 1997 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)241-244
Number of pages4
JournalFEBS Letters
Volume405
Issue number2
Publication statusPublished - 24-Mar-1997

Keywords

  • calcium binding
  • thermal stability
  • thermolysin
  • autolysis
  • unfolding pathway
  • THERMOSTABLE NEUTRAL PROTEASE
  • BACILLUS-STEAROTHERMOPHILUS
  • GENE
  • RESOLUTION
  • SUBTILISIN
  • EXPRESSION
  • CLONING

Cite this