Antifreeze activity enhancement by site directed mutagenesis on an antifreeze protein from the beetle Rhagium mordax.

Dennis Steven Friis, Erlend Kristiansen, Nicolas von Solms, Hans Ramløv

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The ice binding motifs of insect antifreeze proteins (AFPs) mainly consist of repetitive TxT motifs aligned on a flat face of the protein. However, these motifs often contain non-threonines that disrupt the TxT pattern. We substituted two such disruptive amino acids located in the ice binding face of an AFP from Rhagium mordax with threonine. Furthermore, a mutant with an extra ice facing TxT motif was constructed. These mutants showed enhanced antifreeze activity compared to the wild type at low concentrations. However, extrapolating the data indicates that the wild type will become the most active at concentrations above 270μmol.
Original languageEnglish
JournalFEBS Letters
Volume588
Issue number9
Pages (from-to)1767-1772
Number of pages6
ISSN0014-5793
DOIs
Publication statusPublished - 2014

Keywords

  • Antifreeze protein
  • Site directed mutagenesis
  • Thermal hysteresis

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