Abstract
The crude fraction extracted at pH 6.0 from sprouting potato tubers (pH 6.0 fraction) hydrolyzed casein and BANA at pH 6.0. This pH 6.0 fraction contained not only caseinase activity but also gelatinase activity, detected by active staining of PAGE-gel with gelatin, as endopeptidases, and both activities increased during sprouting of tubers. This endopeptidase, also active on Azocolase, had an optimum pH at pH 6.0, whereas the crude fraction extracted at pH 6.0 from fresh potato tubers contained little endopeptidase activities in the whole pH range. Inhibition by monoiodoacetate or antipain indicated this endopeptidase to be a cysteine protease.