A　novel　lysozyme　was　isolated　from　the　Canadian　cranberry　beans　(Phaseolus　vulgaris)　and　its　enzymatic　properties,　antifungal　and　antibacterial　activities　were　investigated.　The　isolation　procedure　involved　aqueous　extraction,　ammonium　sulfate　precipitation,　and　chromatography　purification　including　affinity　chromatography　on　Affi-gel　blue　gel,　ion　exchange　chromatography　on　CM-Sephadex,　and　high　performance　liquid　chromatography　(HPLC)　on　Mono　S.　The　enzyme　exhibited　a　molecular　mass　of　15.6　kDa　in　SDS-polyacrylamide　gel　electrophoresis　both　under　reducing　and　non-reducing　conditions,　indicating　that　it　was　a　monomeric　protein.　The　15　N-terminal　amino　acid　sequences　were　determined　to　be　KVDMPGRFA-LAMQSH,　showing　some　homology　to　hen　egg　white　lysozyme.　The　pl　was　determined　to　be　9.6　by　isoelectric　focusing　electrophoresis.　The　specific　activity　of　the　lysozyme　was　652　U/mg　at　pH　5.5　and　40　degrees　C.　The　lysozyme　exhibited　a　pH　optimum　at　pH　5.5　and　a　temperature　optimum　at　50　degrees　C.　It　exerted　a　potent　inhibitory　action　toward　fungal　species　including　Alternaria　alternata(Fr.)　Keissl,　Pythium　aphanidermatum,　Fusarium　oxysporum　and　Botrytis　cinerea,　in　addition　to　an　antibacterial　action　against　Staphylococcus　aureus.　However,　it　showed　no　effect　on　Gram-negative　bacteria.　The　enzyme　was　thermostable　below　58　degrees　C　in　both　enzymatic　reaction　and　antifungal　activity.　The　present　findings　further　the　research　on　leguminous　lysozyme　with　potentially　exploitable　significance.　(C)　2011　Elsevier　Ltd.　All　rights　reserved.