Thermozymes: Identifying molecular determinants of protein structural and functional stability

• Published in: Trends in biotechnology (Regular ed.) Vol. 14; no. 6; pp. 183 - 190
• Main Authors: Vieille, Claire, Gregory Zeikus, J.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.06.1996; Elsevier Science
• Subjects: Biological and medical sciences; Biotechnology; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Protein engineering; Molecular structure; Enzyme; Stabilization; Thermostable; Review; Structure function relationship; Comparative study; Mechanism; Thermal stability
• ISSN: 0167-7799; 1879-3096
• DOI: 10.1016/0167-7799(96)10026-3

Thermozymes are thermostable enzymes that function optimally between 60°C and 125°C. These extremozymes are a ‘hot’ research topic because they are remarkable tools for studying protein stability, as well as for developing industrial and specialty biotechnologies. Most protein-stabilization mechanisms (i.e. hydrophobic interactions, packing efficiency, salt-bridges, hydrogen bonds, reduction of conformational strain, reduction of the entropy of unfolding, α-helix stabilization, loop stabilization and resistance to covalent destruction) have been identified by stability studies using mesophilic models. Recent structural comparisons between mesophilic enzymes and thermozymes validate these mechanisms.