THERMOZYMES - IDENTIFYING MOLECULAR DETERMINANTS OF PROTEIN STRUCTURAL AND FUNCTIONAL STABILITY

Citation
C. Vieille et Jg. Zeikus, THERMOZYMES - IDENTIFYING MOLECULAR DETERMINANTS OF PROTEIN STRUCTURAL AND FUNCTIONAL STABILITY, Trends in biotechnology, 14(6), 1996, pp. 183-190
Citations number
63
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
01677799
Volume
14
Issue
6
Year of publication
1996
Pages
183 - 190
Database
ISI
SICI code
0167-7799(1996)14:6<183:T-IMDO>2.0.ZU;2-D
Abstract
Thermozymes are thermostable enzymes that function optimally between 6 0 degrees C and 125 degrees C. These extremozymes are a 'hot' research topic because they are remarkable tools for studying protein stabilit y, 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 confor mational strain, reduction of the entropy of unfolding, alpha-helix st abilization, loop stabilization and resistance to covalent destruction ) have been identified by stability studies using mesophilic models. R ecent structural comparisons between mesophilic enzymes and thermozyme s validate these mechanisms.