Hyperthermophilic enzymes - stability, activity and implementation strategies for high temperature applications

L.D. Unsworth, J. van der Oost, S. Koutsopoulos

Research output: Contribution to journalArticleAcademicpeer-review

149 Citations (Scopus)


Current theories agree that there appears to be no unique feature responsible for the remarkable heat stability properties of hyperthermostable proteins. A concerted action of structural, dynamic and other physicochemical attributes are utilized to ensure the delicate balance between stability and functionality of proteins at high temperatures. We have thoroughly screened the literature for hyperthermostable enzymes with optimal temperatures exceeding 100 °C that can potentially be employed in multiple biotechnological and industrial applications and to substitute traditionally used, high-cost engineered mesophilic/thermophilic enzymes that operate at lower temperatures. Furthermore, we discuss general methods of enzyme immobilization and suggest specific strategies to improve thermal stability, activity and durability of hyperthermophilic enzymes.
Original languageEnglish
Pages (from-to)4044-4056
JournalFEBS Journal
Issue number16
Publication statusPublished - 2007


  • archaeon pyrococcus-furiosus
  • extremely thermophilic archaebacteria
  • thermostable dna-polymerase
  • alpha-glucosidase gene
  • sulfolobus-solfataricus
  • escherichia-coli
  • biochemical-characterization
  • thermococcus-litoralis
  • thermotoga-maritima
  • protein stabili

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