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Thermitase is a thermostable member of the subtilisin protease family. It was found that this enzyme binds very strongly one calcium ion. This metal ion cannot be removed without denaturation by any known method. A second binding site for calcium ions can be depleted partially by gel filtration, similar to the strong binding site of subtilisin Carlsberg. In both enzymes the calcium ion bound to this site can be removed completely using Ca 2+ chelating reagent. In thermitase and subtilisin Carlsberg, depleting calcium ions from any binding site results in a significant decrease of stability against autolysis.
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Briedigkeit et al. (1989) studied this question.
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