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Conformational studies on alkaline protease from Bacillus mesentericus.

The alkaline protease from Bacillus mesentericus (E-30-III) is soluble in acidic media up to pH 4. Below this pH the protein precipitates. The difference ultraviolet spectra showed that in the pH-range from 6.0 to 4.1 gradual changes in the environment of the aromatic chromophores in E-30-III take place which depend on pH. 
 
 
 
On the basis of photooxidation kinetics the following subdivision of the methionyl and tryptophyl residues in E-30-III was made: at pH 6.85 two methionyl residues were “slowly reactive”, one tryptophyl residue was “reactive”, and four methionyl and two tryptophyl residues were “unreactive”. At pH 4.10 all six methionyl and one tryptophyl residues were “slowly reactive” and two tryptophyl residues were “reactive”. The comparison between subtilisin BPN‘, subtilisin Carlsberg and protease E-30-III showed some differences in the state of methionyl and tryptophyl residues. 
 
 
 
Circular dichroism spectra showed that E-30-III possesses about 26% α-helix structure at pH 6.85. At pH 4.10 the protein preserved about 11% α-helix content. 
 
 
 
Gradual but not complete unfolding of the protein molecule occurred when the pH was lowered from 6.0 to 4.1.