On the salt-induced activation of lyophilized enzymes in organic solvents: Effect of salt kosmotropicity on enzyme activity

Michael T. Ru, Scott Y. Hirokane, Andy S. Lo, Jonathan S. Dordick, Jeffrey A. Reimer, Douglas S. Clark

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

The dramatic activation of enzymes in nonaqueous media upon co-lyophilization with simple inorganic salts has been investigated as a function of the Jones - Dole B coefficient, a thermodynamic parameter for characterizing the salt's affinity for water and its chaotropic (water-structure breaking) or kosmotropic (water-structure making) character. In general, the water content, active-site content, and transesterification activity of freeze-dried subtilisin Carlsberg preparations containing >96% w/w salt increased with increasing kosmotropicity of the activating salt. Degrees of activation relative to the salt-free enzyme ranged from 33-fold for chaotropic sodium iodide to 2480-fold for kosmotropic sodium acetate. Exceptions to the general trend can be explained by the mechanical properties and freezing characteristics of the salts undergoing lyophilization. The profound activating effect can thus be attributed in part to the stabilizing (salting-out) effect of kosmotropic salts and the phenomenon of preferential hydration.

Original languageEnglish
Pages (from-to)X
JournalJournal of the American Chemical Society
Volume122
Issue number8
StatePublished - 1 Mar 2000
Externally publishedYes

Fingerprint

Dive into the research topics of 'On the salt-induced activation of lyophilized enzymes in organic solvents: Effect of salt kosmotropicity on enzyme activity'. Together they form a unique fingerprint.

Cite this