MOLECULAR ADAPTATION TO COLD OF AN ANTARCTIC BACTERIAL LIPASE

Citation
Jl. Arpigny et al., MOLECULAR ADAPTATION TO COLD OF AN ANTARCTIC BACTERIAL LIPASE, Journal of molecular catalysis. B, Enzymatic, 3(1-4), 1997, pp. 29-35
Citations number
18
Categorie Soggetti
Chemistry Physical
ISSN journal
13811177
Volume
3
Issue
1-4
Year of publication
1997
Pages
29 - 35
Database
ISI
SICI code
1381-1177(1997)3:1-4<29:MATCOA>2.0.ZU;2-0
Abstract
The lipase from the Antarctic psychrophilic bacterium Psychrobacter im mobilis B10 shows a very limited thermal stability when compared to th e lipase from a mesophilic strain of Pseudomonas aeruginosa. The therm al dependence of its activity is shifted by at least 30 degrees C towa rds low temperatures and its activation energy is reduced by a factor of 2. The three-dimensional model of the P. immobilis lipase reveals s everal features typical of cold-adapted enzymes: a very low proportion of arginine residues as compared to lysines, a low content in proline residues, a small hydrophobic core, a very small number of salt bridg es and of aromatic-aromatic interactions. All these properties should confer on the enzyme a more flexible structure, in accord with its low activation energy and its low thermal stability.