Reference : Did Psychrophilic Enzymes Really Win the Challenge?
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16030
Did Psychrophilic Enzymes Really Win the Challenge?
English
Zecchinon, Laurent mailto [Université de Liège - ULg > Département de morphologie et pathologie > Pathologie spéciale et autopsies >]
Claverie, P. [> > > >]
Collins, T. [> > > >]
D'Amico, Salvino [Université de Liège - ULg > > GIGA-Research >]
Delille, D. [> > > >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
Georlette, D. [> > > >]
Gratia, E. [> > > >]
Hoyoux, A. [> > > >]
Meuwis, Marie-Alice mailto [Université de Liège - ULg > > GIGA-Management : Plate-forme protéomique >]
Sonan, G. [> > > >]
Gerday, Charles mailto [Université de Liège - ULg > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Oct-2001
Extremophiles : Life Under Extreme Conditions
5
5
313-21
Yes (verified by ORBi)
International
1431-0651
[en] Biotechnology ; Biotechnology ; Cold Climate ; Directed Molecular Evolution ; Enzyme Stability ; Enzymes/chemistry/genetics/metabolism ; Kinetics ; Protein Conformation
[en] Organisms living in permanently cold environments, which actually represent the greatest proportion of our planet, display at low temperatures metabolic fluxes comparable to those exhibited by mesophilic organisms at moderate temperatures. They produce cold-evolved enzymes partially able to cope with the reduction in chemical reaction rates and the increased viscosity of the medium induced by low temperatures. In most cases, the adaptation is achieved through a reduction in the activation energy, leading to a high catalytic efficiency, which possibly originates from an increased flexibility of either a selected area of or the overall protein structure. This enhanced plasticity seems in return to be responsible for the weak thermal stability of cold enzymes. These particular properties render cold enzymes particularly useful in investigating the possible relationships existing between stability, flexibility, and specific activity and make them potentially unrivaled for numerous biotechnological tasks. In most cases, however, the adaptation appears to be far from being fully achieved.
http://hdl.handle.net/2268/16030

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