Reference : Some like it cold: biocatalysis at low temperatures
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Some like it cold: biocatalysis at low temperatures
Georlette, D. [> > > >]
Blaise, Vinciane [Université de Liège - ULiège > Département des sciences et gestion de l'environnement > Département des sciences et gestion de l'environnement >]
Collins, T. [> > > >]
D'Amico, Salvino [Université de Liège - ULiège > > GIGA-Research >]
Gratia, E. [> > > >]
Hoyoux, A. [> > > >]
Marx, J. C. [> > > >]
Sonan, G. [> > > >]
Feller, Georges mailto [Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie >]
Gerday, Charles mailto [Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
FEMS Microbiology Reviews
Elsevier Science Bv
Yes (verified by ORBi)
[en] cold-adaptation ; psychrophiles ; extremophiles ; enzyme kinetics ; enzyme activity ; flexibility concept
[en] In the last few years, increased attention has been focused on a class of organisms called psychrophiles. These organisms, hosts of permanently cold habitats, often display metabolic fluxes more or less comparable to those exhibited by mesophilic organisms at moderate temperatures. Psychrophiles have evolved by producing, among other peculiarities, "cold-adapted" enzymes which have the properties to cope with the reduction of chemical reaction rates induced by low temperatures. Thermal compensation in these enzymes is reached, in most cases, through a high catalytic efficiency associated, however, with a low thermal stability. Thanks to recent advances provided by X-ray crystallography, structure modelling, protein engineering and biophysical studies, the adaptation strategies are beginning to be understood. The emerging picture suggests that psychrophilic enzymes are characterized by an improved flexibility of the structural components involved in the catalytic cycle, whereas other protein regions, if not implicated in catalysis, may be even more rigid than their mesophilic counterparts. Due to their attractive properties, i.e., a high specific activity and a low thermal stability, these enzymes constitute a tremendous potential for fundamental research and biotechnological applications. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

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