Abstract
Cold-adapted (psychrophilic) enzymes have intrinsically high activities at the expense of low stabilities due to their flexible structures. Their higher thermolability limits their applications under numerous industrial conditions that require the process to be carried out at higher temperatures for efficient catalysis. Therefore, for effective utilization, cold-adapted enzymes need to be improved in such a way that enhances their stability with an increase or retention of their activity. This chapter discusses the thermodynamic aspects of improvement of catalytic properties and presents a unified strategy that aims at simultaneously improving the activity and stability of cold-adapted enzymes by employing not a single but a combination of approaches that include genetic and chemical.
| Original language | English |
|---|---|
| Title of host publication | Psychrophiles |
| Subtitle of host publication | From Biodiversity to Biotechnology: Second Edition |
| Publisher | Springer International Publishing |
| Pages | 477-512 |
| Number of pages | 36 |
| ISBN (Electronic) | 9783319570570 |
| ISBN (Print) | 9783319570563 |
| DOIs | |
| State | Published - 1 Jul 2017 |
ASJC Scopus subject areas
- General Immunology and Microbiology
- General Biochemistry, Genetics and Molecular Biology
- General Physics and Astronomy