Antihypertensive peptides from vicilin, the major storage protein of mung bean (vigna radiata (l.) r. wilczek)

Issue Date

7-2012

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 beanvar. 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 Tl, 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 CI, 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. © 2012 Asisn Network for Scientific Information.

Source or Periodical Title

Journal of Biological Sciences

ISSN

1727-3048

Volume

12

Issue

7

Document Type

Article

Language

English

Subject

Ace inhibitor, Antihypertensive, Mung bean, Storage protein, Vicilin

Identifier

doi:10.3923/jbs.2012.393.399.

Digital Copy

yes

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