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
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.