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. Study holds ProTherm entries: 25410, 25411, 25412 Extra Details: Savinase; Thermal stability; Co-solvent; Autolysis; Aggregation
Submission Details
ID: n4EpwK5y3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:55 p.m.
Version: 1
Publication Details
Nasiripourdori A;Naderi-Manesh H;Ranjbar B;Khajeh K,Int. J. Biol. Macromol. (2009) Co-solvent effects on structure and function properties of savinase: solvent-induced thermal stabilization. PMID:18955077Additional Information
Study Summary
| Number of data points | 3 |
| Proteins | Subtilisin Savinase |
| Unique complexes | 1 |
| Assays/Quantities/Protocols | Experimental Assay: Tm |
| Libraries | Mutations for sequence AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATSLGSTNLYGSGLVNAEAATR |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)