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| Antihypertensive Peptides from Vicilin, the Major Storage Protein of Mung Bean (Vigna radiata (L.) R. Wilczek) |
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L.B.G. Viernes,
R.N. Garcia,
M.A.O. Torio and M.R.N. Angelia |
Abstract:
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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How to cite this article:
L.B.G. Viernes, R.N. Garcia, M.A.O. Torio and M.R.N. Angelia, 2012. Antihypertensive Peptides from Vicilin, the Major Storage Protein of Mung Bean (Vigna radiata (L.) R. Wilczek). Journal of Biological Sciences, 12: 393-399.
DOI: 10.3923/jbs.2012.393.399
URL: https://scialert.net/abstract/?doi=jbs.2012.393.399
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