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　degrees　C,　respectively.　The　enzyme　was　stable　up　to　55　degrees　C.　It　potently　suppressed　mycelial　growth　in　Fusarium　solani,　Mycosphaerella　arachidicola,　and　Pythium　aphanidermatum　with　an　IC50　of　76,　103,　and　119　mu　M,　respectively.