Isolation and characterization of a novel mung bean protease inhibitor with antipathogenic and anti-proliferative activities.

A novel protease inhibitor, designated mungoin, with both antifungal and antibacterial activities, and exhibiting a molecular mass of 10kDa in SDS-polyacrylamide gel electrophoresis, was isolated from mung bean (Phaseolus mungo) seeds. The isolation procedure involved a combination of extraction, ammonium sulfate precipitation, ion exchange chromatography on CM-Sephadex, and high-performance liquid chromatography (HPLC) on SP-Toyopearl. Its isoelectric point was estimated to be 9.8 by isoelectric focusing. Its N-terminal amino acid sequence was determined to be EMPGKPACLDTDDFCYKP, demonstrating some resemblance to the C-terminal sequences of other protease inhibitors and inhibitor precursors from leguminous plants. It exerted a potent inhibitory action toward a variety of fungal species including Physalospora piricola, Mycosphaerella arachidicola, Botrytis cinerea, Pythium aphanidermatum, Sclerotium rolfsii and Fusarium oxysporum, as well as an antibacterial action against Staphylococcus aureus. In addition, this novel plant protease inhibitor displayed anti-proliferative activity toward tumor cells.