A　novel　peroxidase　with　antifungal　activity　was　isolated　from　the　large　lima　bean　(Phaseolus　limensis)　seeds.　The　procedure　entailed　extraction,　ammonium　sulfate　precipitation,　affinity　chromatography　on　Affi-gel　blue　gel,　ion　exchange　chromatography　on　SP-Toyopearl,　and　gel　filtration　on　Sephadex　G-75.　The　enzyme　was　adsorbed　on　Affi-gel　blue　gel　and　SP-Toyopearl,　and　possessed　a　molecular　weight　of　34　kDa　in　SDS-polyacrylamide　gel　electrophoresis　under　both　reducing　and　nonreducing　conditions.　There　was　an　almost　110-fold　increase　in　specific　activity　of　the　purified　peroxidase　compared　with　that　of　the　crude　extract.　The　enzyme　exhibited　a　pI　of　8.6　by　isoelectric　focusing　electrophoresis,　indicating　that　it　is　a　basic　protein.　The　optimum　pH　and　the　optimum　temperature　were　5.5　and　30　°C,　respectively.　The　enzyme　was　stable　up　to　55　°C.　It　potently　suppressed　mycelial　growth　in　Fusarium　solani,　Mycosphaerella　arachidicola,　and　Pythium　aphanidermatum　with　an　IC50　of　76,　103,　and　119　μM,　respectively.　©　2009　Institute　of　Food　Technologists®.