Proteolytic enzyme (s) was partially purified from a crude extract of acetone-dried powder of ginger rhizome. The purified preparation gave a single main protein band of approximately 30, 000 Da. on SDS-polyacrylamide gel electrophoresis and hydrolyzed casein (proteinase activity) and type 1 collagen from bovine achilles tendon (collagenase activity). The collagenase activity of ginger was not affected by addition of EDTA, which it is known to be a potent inhibitor of collagenases from other sources, but was inhibited by HgCl₂. The proteinase and collagenase activities of the ginger preparation decreased at a similar rate during heat-treatment. These results are interpreted to indicate that ginger rhizome contains a single enzyme which has both proteinase and collagenase activities.