The addition of simple inorganic salts to aqueous enzyme solutions prior to lyophilization results in a dramatic activation of the dried powder in organic media relative to enzyme with no added salt. Activation of both the serine protease subtilisin Carlsberg and lipase from Mucor javanicus resultin
Selection of salt hydrate pairs for use in water control in enzyme catalysis in organic solvents
โ Scribed by E. Zacharis; I. C. Omar; J. Partridge; D. A. Robb; P. J. Halling
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 230 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0006-3592
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โฆ Synopsis
The water activities (a w ) of 13 salt hydrate pairs equilibration to occur through the gas phase. However, were determined from vapor pressure measurements; a w keeping a w constant during longer term reactions in values for a subset were also estimated from a study of which water is a reactant or product is a challenge which water transfer to isopropylether. The application of salt can be accomplished, theoretically at least, by adding hydrates as water buffers was investigated in two models: salt hydrate pairs directly to the mixture to act as water (i) effect of hydration on the initial rate of subtilisincatalyzed transesterification of the nitrophenol ester of buffers. Just as a pH buffer relies on an acid base mixture CBZ-alanine with butanol; and (ii) effect of hydrates on to function, a water buffer utilizes a salt mixture of, e.g., the equilibrium concentrations of reactants in the esterithe hydrated salt and the anhydrous salt. This approach fication of dodecanol and decanoic acid, catalyzed by has been utilized by several investigators (Berglund et lipase. Transfer of ions from salt to enzyme particles was
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