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Journal of Biological Sciences

Year: 2012 | Volume: 12 | Issue: 7 | Page No.: 393-399
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Authors

L.B.G. Viernes

R.N. Garcia

M.A.O. Torio

M.R.N. Angelia

Keywords

Research Article

Antihypertensive Peptides from Vicilin, the Major Storage Protein of Mung Bean (Vigna radiata (L.) R. Wilczek)

L.B.G. Viernes, R.N. Garcia, M.A.O. Torio and M.R.N. Angelia
Hypertension is among the leading diseases afflicting humans and the search for cheap and alternative modes of treatment is of primary importance. This study investigated the potential of vicilin, the major storage protein of mung bean, to generate antihypertensive peptides. The total soluble proteins of mung bean var. Pag-asa 7 were extracted using 35 mM potassium phosphate buffer (pH 7.0) containing 0.40 M NaCl. Vicilin (8S globulin) was purified by a combination of ammonium sulfate fractionation, selective precipitation and gel filtration chromatography. Trypsin and chymotrypsin digests of vicilin, for a 24 h period, yielded Angiotensin Converting Enzyme (ACE) inhibitory activities of 83.95 and 93.68%, respectively. Both digests were further purified using reversed phase-high performance liquid chromatography (RP-HPLC). RP-HPLC fractions obtained from trypsin digests have IC50 values of 1.325, 1.151 and 1.367 mg mL-1 for T1, T2 and T3, respectively. Meanwhile, RP-HPLC fractions of chymotrypsin digests have IC50 values of 0.826, 0.203, 0.286 and 0.852 mg mL-1 for C1, C2, C3 and C4, respectively. Chymotrypsin was better in releasing more potent ACE inhibitory peptides than trypsin. Therefore, vicilin contains antihypertensive peptides that exhibit angiotensin converting enzyme inhibitory activities.
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