C. Vieille et Jg. Zeikus, THERMOZYMES - IDENTIFYING MOLECULAR DETERMINANTS OF PROTEIN STRUCTURAL AND FUNCTIONAL STABILITY, Trends in biotechnology, 14(6), 1996, pp. 183-190
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.