A　novel　trypsin　inhibitor　with　thermal　and　pH　stability,　designated　Merrtine,　was　isolated　from　Glycine　max　L.　merr.　The　procedure　involved　ammonium　sulfate　precipitation,　ion-exchange　chromatography　on　CM-Sephadex　C-50,　and　affinity　chromatography　on　Affi-gel　blue　gel.　The　20N-terminal　amino　acid　sequences　were　determined　to　be　DEYSKPCCDLCMCTRRCPPQ,　demonstrating　high　homology　with　the　sequence　of　Bowman-Birk　type　trypsin　inhibitors.　The　molecular　mass　and　isoelectric　point　of　the　inhibitor　were　estimated　by　sodium　dodecyl　sulfate　polyacrylamide　gel　electrophoresis　(SDS-PAGE)　and　isoelectric　focusing　to　be　20.0　kD　and　5.8,　respectively.　Trypsin　could　be　completely　inhibited　by　Merrtine　when　the　molar　ratio　was　8.1.　The　inhibitory　activity　of　Merrtine　was　unaffected　after　exposure　to　temperatures　up　to　85　degrees　C,　as　well　as　within　the　pH　range　2-12.　Besides　inhibiting　trypsin-chymotrypsin,　the　inhibitor　demonstrated　additional　antifungal　activity　against　the　species　of　Alternaria　alternate,　Fusarium　oxysporum,　Pythium　aphanidermatum,　Physalospora　piricola,　Botrytis　cinerea,　and　Fusarium　solani.　We　herein　report　not　only　the　trypsin　inhibitor＇s　extraction　and　isolation　for　the　first　time,　but　also　its　physiochemical　and　antifungal　properties.