Isolation and purification of the major storage protein from string bean (Phaseolus vulgaris) with bioactive peptides exhibiting ace 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

Abstract

In silico analysis was done using the sequence of phaseolin obtained from the NCBI database. Different dipeptides (VK, MY, KA, GP, AA, AR, GA and RR) exhibiting ACE inhibitory activity and anti-hypertensive activity was observed to be present in the sequence. The crude protein of Phaseolus vulgaris was extracted using 0.5 M NaCl with 0.25 M ascorbic acid. The crude extract had a protein concentration of 2.494 mg/mL using Bradford method. The major storage protein of the sample, phaseolin was purified using ammonium sulfate precipitation, dialysis and gel chromatography. The purified protein extract was estimated to contain 1.434 mg/mL. The molecular weight was estimated to be 51163 Da on SDS-PAGE. The purified protein was digested using pepsin in 1:1 protein-enzyme ratio. The digestion time used was one hour and 24 hours and was then compared to the undigested protein through SDS-PAGE. The percent ACE inhibitory activity of the hydrolysates obtained after one and 24 hours of enzymatic digestion was determined to be 66.23 and 87.86, respectively. The undigested purified protein also exhibited 27.97% inhibition.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2011 C42 /G37

Document Type

Thesis

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