Investigation of the conformation, solubility, structure and selectivity of alkaline proteases in anhydrous alcohols.

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Abstract

The solubility of two alkaline protease, alcalase and subtilisin Carlsberg, in absolute alcohol are determined. The global conformation as well as the local conformation of the active sites (S-1 and S-2 subsites) of both enzymes in alcohol and in aqueous solution are similar. The enantio- and diastereo-selectivity of both enzymes in anhydrous alcohol are also similar to those in aqueous solution.

The solubility of two alkaline protease, alcalase and subtilisin Carlsberg, in absolute alcohol are determined. The global conformation as well as the local conformation of the active site (S-1 and S-2 subsites) of both enzymes in alcohol and in adqueous solution are similar. The enantio- and diastereo-selectivity of both enzymes in anhydrous alcohol are also similar to those in aqueous solution.

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