Isolation and partial purification of the major storage protein (Vicilin) in cowpea (Vigna unguiculata) seeds with bioactive peptides exhibiting angiotensin converting enzyme inhibitory activity.

Date

10-2011

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Mary Ann O Torio

Co-adviser

Roberta Garcia

Committee Member

Mark Rickard Angelia

Abstract

The major storage protein was extracted using 50 mM sodium borate buffer pH 8.0. The average protein content of the crude protein isolate was found to be 5 21 mg/mL using the method described by Bradford SDS-PAGE profile of the crude protein showed that the major protein has an approximate molecular weight of 66 KDa In addition, densitrometric analysis revealed that the major protein band of the crude isolate is 32 41% of the total protein. Purification methods such as ammonium sulfate precipitation and fractionation, dialysis, gel filtration chromatography in Sephadex G-200 and hydrophobic interaction chromatography revealed that the major protein is 13-viginin which contains two subunits with molecular weights of approximately 55 KDa and 60 KDa Digestion using pepsin was carried out and showed that lowest remaining protein (11 98% and 50.38% for the two peaks, respectively) occurred after 24 hours digestion time Spectrophotometric assay of the peptic hydrolysates revealed that at increasing digestion time, inhibitory activity also increases. Highest inhibitory activity (90.07%) and lowest 1050 activity (0.029 mg/ml) was observed in 24-hour peptic hydrolysates. Thus, cowpea's major storage protein contains bioactive peptides exhibiting anti-hypertensive activities

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2011 C4 H53

Document Type

Thesis

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