A　28.6-kDa　chitinase　with　chitin-binding　activity　was　isolated　from　the　large　lima　bean　(Phaseolus　limensis)　seeds.　The　procedure　entailed　extraction,　ammonium　sulfate　precipitation,　affinity　chromatography　on　blue　gel,　and　high-performance　liquid　chromatography　(HPLC)　on　SP-Toyopearl.　There　was　an　almost　108-Affi-gel　fold　increase　in　specific　activity　of　the　purified　chitinase　compared　with　that　of　the　crude　extract.　The　enzyme　exhibited　a　pI　of　7.8　by　isoelectric　focusing　electrophoresis.　The　optimum　pH　and　the　optimum　temperature　for　activity　toward　N-acetyld-glucosamine　were　5.4　and　40　to　50　degrees　C,　respectively.　The　enzyme　was　stable　up　to　55　degrees　C.　It　exerted　a　potent　inhibitory　action　toward　fungal　species,　including　Fusarium　solani,　Pythium　aphanidermatum,　and　Sclerotium　rolfsii.