Psychrophilic Enzymes: A Thermodynamic Challenge

• Published in: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
• Main Authors: Gerday, Charles, Aittaleb, Mohamed, Arpigny, Jean Louis, Baise, Etienne, Chessa, Jean-Pierre, Garsoux, Geneviève, Petrescu, Ioan, Feller, Georges
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier 1997
• Subjects: Life sciences; Biochemistry; biophysics & molecular biology; Sciences du vivant; Biochimie; biophysique & biologie moléculaire; Antarc*; Antarctic
• Online Access: https://orbi.uliege.be/handle/2268/16227; https://doi.org/10.1016/S0167-4838(97)00093-9

peer reviewed Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold alpha-amylase, beta-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost.