Organic solvents strip water off enzymes

Lu Ann S. Gorman, Jonathan S. Dordick

Research output: Contribution to journalArticlepeer-review

346 Scopus citations


Exchange of enzyme‐bound H2O with T2O in aqueous solution followed by freeze drying provided tritiated water bound to chymotrypsin, subtilisin Carlsberg, and horseradish peroxidase. The desorption of T2O from these enzymes suspended in various organic solvents showed that all three enzymes lost enzyme‐bound water with peroxidase losing the most T2O of the three in solvents of moderate to high polarity. Polar solvent resulted in the highest degree of T2O desorption (e.g., methanol desorbed from 56%‐62% of the bound T2O), while nonpolar solvents resulted in the lowest degree of desorption (e.g., hexane desorbed from 0.4%–2% of the bound T2O). Desorption is nearly immediate with most of the desorbable T2O being released from the enzymes within the first 5 min. Both solvent dielectric and a measure of the saturated molar solubility of water in a given solvent provide accurate correlations between the properties of the organic solvents and the extent of T2O desorption. This investigation shows that water stripping from an enzyme into a nonaqueous medium does occur and can be significant in polar solvents.

Original languageEnglish
Pages (from-to)392-397
Number of pages6
JournalBiotechnology and Bioengineering
Issue number4
StatePublished - 20 Feb 1992
Externally publishedYes


  • TO desorption
  • enzymes
  • organic solvents
  • water stripping


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