Psychrophilic enzymes: A thermodynamic challenge

Charles Gerday*, Mohamed Aittaleb, Jean Louis Arpigny, Etienne Baise, Jean Pierre Chessa, Geneviève Garsoux, Ioan Petrescu, Georges Feller

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

275 Citations (Scopus)

Abstract

Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30°C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold α-amylase, β-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost.

Original languageEnglish
Pages (from-to)119-131
Number of pages13
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1342
Issue number2
DOIs
Publication statusPublished - 17 Oct 1997
Externally publishedYes

Keywords

  • Adaptation to cold
  • Antarctic microorganism
  • Psychrophile

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