Nε-Acetyl L-α Lysine Improves Activity and Stability of α-Amylase at Acidic Conditions: A Comparative Study with other Osmolytes
| Autor: | Masilamani Selladurai, Nidhya Nadarajan Joghee, Gurunathan Jayaraman |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Lysine
Ectoine Biochemistry 03 medical and health sciences chemistry.chemical_compound Betaine Bacterial Proteins Structural Biology Osmotic Pressure Enzyme Stability Bacillus licheniformis Amylase 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry Temperature Amino Acids Diamino General Medicine Hydrogen-Ion Concentration Trehalose Enzyme assay Osmolyte biology.protein Thermodynamics Chemical stability alpha-Amylases |
| Zdroj: | Protein and peptide letters. 27(6) |
| ISSN: | 1875-5305 |
| Popis: | Background: Nε-acetyl L-α lysine is an unusual acetylated di-amino acid synthesized and accumulated by certain halophiles under osmotic stress. Osmolytes are generally known to protect proteins and other cellular components under various stress conditions. Objective: The structural and functional stability imparted by Nε-acetyl L-lysine on proteins were unknown and hence was studied and compared to other commonly known bacterial osmolytes - ectoine, proline, glycine betaine, trehalose and sucrose. Methods: Effects of osmolytes on the temperature and pH profiles, pH stability and thermodynamic stability of the model enzyme, α-amylase were analyzed. Results: At physiological pH, all the osmolytes under study increased the optimal temperature for enzyme activity and improved the thermodynamic stability of the enzyme. At acidic conditions (pH 3.0), Nε-acetyl L-α lysine and ectoine improved both the catalytic and thermodynamic stability of the enzyme; it was reflected in the increase in residual enzyme activity after incubation of the enzyme at pH 3.0 for 15 min by 60% and 63.5% and the midpoint temperature of unfolding transition by 11°C and 10°C respectively. Conclusion: Such significant protective effects on both activity and stability of α-amylase imparted by addition of Nε-acetyl L-α lysine and ectoine at acidic conditions make these osmolytes interesting candidates for biotechnological applications. |
| Databáze: | OpenAIRE |
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