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Psychrophilic Enzymes : From Folding to Function and Biotechnology
Author
Source
Issue
Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-28, 28 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2013-01-17
Country of Publication
Egypt
No. of Pages
28
Main Subjects
Natural & Life Sciences (Multidisciplinary)
Diseases
Abstract EN
Psychrophiles thriving permanently at near-zero temperatures synthesize cold-active enzymes to sustain their cell cycle.
Genome sequences, proteomic, and transcriptomic studies suggest various adaptive features to maintain adequate translation and proper protein folding under cold conditions.
Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state.
Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold.
In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule.
This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold.
These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate.
Several open questions in the field are also highlighted.
American Psychological Association (APA)
Feller, Georges. 2013. Psychrophilic Enzymes : From Folding to Function and Biotechnology. Scientifica،Vol. 2013, no. 2013, pp.1-28.
https://search.emarefa.net/detail/BIM-477546
Modern Language Association (MLA)
Feller, Georges. Psychrophilic Enzymes : From Folding to Function and Biotechnology. Scientifica No. 2013 (2013), pp.1-28.
https://search.emarefa.net/detail/BIM-477546
American Medical Association (AMA)
Feller, Georges. Psychrophilic Enzymes : From Folding to Function and Biotechnology. Scientifica. 2013. Vol. 2013, no. 2013, pp.1-28.
https://search.emarefa.net/detail/BIM-477546
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-477546