An endopeptidase in powdered yam was purified using a combination of anion-exchange and gel-filtration chromatographies. The preparation gave 9.2-fold purification with yield of 19% against the crude extract. The endopeptidase was classified as a serine endopeptidase with inhibitory spectrum, with an optimum temperature and pH of approximately 60°C and 7.1, respectively. It also had high heat stability and high salt resistance.
