Psychrophilic Enzymes: A Thermodynamic Challenge
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...
| Published in: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology |
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| Main Authors: | , , , , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Elsevier
1997
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| Subjects: | |
| Online Access: | https://orbi.uliege.be/handle/2268/16227 https://doi.org/10.1016/S0167-4838(97)00093-9 |
| Summary: | 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. |
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