Co-solvent effects on structure and function properties of savinase: solvent-induced thermal stabilization.

Abstract

The industrial utilization of savinase is mainly constrained by its stability limitations. In the present study, the irreversible thermoinactivation of savinase has been evaluated at 70 degrees C, and various possible mechanisms for irreversible thermoinactivation of savinase were examined. The main process seemed to be autodigestion of savinase at higher temperatures. To improve the thermal stability of the enzyme, the effect of two co-solvents (sorbitol and trehalose) on the enzyme's activity and stability was investigated. Both osmolytes prevented the autolysis of savinase at 70 degrees C without inactivating the enzyme; furthermore, the structural and kinetic stabilities of the enzyme increased in the presence of additives.

• Authors: Adak Nasiripourdori, Hossein Naderi-Manesh, Bijan Ranjbar, Khosro Khajeh
• Journal: International journal of biological macromolecules (Int J Biol Macromol) Vol. 44 Issue 4 Pg. 311-5 (May 01 2009) ISSN: 1879-0003 [Electronic] Netherlands
• PMID: 18955077 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amides
• Solvents
• Sorbitol
• Trehalose
• Serine Endopeptidases
• microbial serine proteinases

Topics

• Amides (metabolism)
• Bacillus (enzymology)
• Bacteriolysis (drug effects)
• Enzyme Activation (drug effects)
• Enzyme Stability (drug effects)
• Protein Binding (drug effects)
• Serine Endopeptidases (chemistry, metabolism)
• Solvents (pharmacology)
• Sorbitol (pharmacology)
• Temperature
• Trehalose (pharmacology)