Dioscorin, the tuber storage protein of yam (
Dioscorea alata cv. Tainong No. 1), was purified tohomogeneity by DE-52 ion-exchange chromatography. This purified dioscorin was shown byspectrophotometric methods to inhibit angiotensin converting enzyme (ACE) in a dose-dependentmanner (12.5-750
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g, respectively, 20.83-62.5% inhibitions) using
N-[3-(2-
furyl)
acryloyl]-
Phe-
Gly-
Gly (FAPGG) as substrates. The 50% inhibition (IC
50) of ACE activity was 6.404
![](/images/entities/mgr.gif)
M dioscorin (250
![](/images/entities/mgr.gif)
g corresponding to 7.81 nmol) compared to that of 0.00781
![](/images/entities/mgr.gif)
M (0.0095 nmol) for captopril. Thecommercial bovine serum albumin
and casein (bovine milk) showed less ACE inhibitory activity. Theuse of qualitative TLC also showed dioscorin as ACE inhibitors. Dioscorin showed mixed noncompetitive inhibitions against ACE; when 31.25
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g of dioscorin (0.8
![](/images/entities/mgr.gif)
M) was added, the apparent inhibitionconstant (
Ki) was 2.738
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M. Pepsin was used for dioscorin hydrolysis at 37
![](/images/entities/deg.gif)
C for different times. Itwas found that the ACE inhibitory activity was increased from 51.32% to about 75% during 32 hhydrolysis. The smaller peptides were increased with increasing pepsin hydrolytic times. Dioscorin
and its hydrolysates might be a potential for hypertension control when people consume yam tuber.Keywords: Angiotensin converting enzyme (ACE); dioscorin;
N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly(FAPGG); mixed-type inhibition; pepsin; yam