Bioactive peptides exhibiting angiotensin I-converting enzyme inhibitory activity from the total globulins and total albumins from mungbean [Vigna radiata (L.) R. Wilczek]

Date

10-2010

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Mark Rickard N Angelia

Co-adviser

Roberta N. Garcia

Abstract

SISON, AYANA GRACE TALLAFER. University of the Philippines at Los Banos, October 2010. Bioactive Peptides Exhibiting Angiotensin I-Converting Enzyme Inhibitory Activity from the Total Globulins and Total Albumins from Mungbean [Vigna radiata (L.) R. Wilczek].

Adviser: Prof. Mark Rickard N. Angelia

Co-adviser: Dr. Roberta N. Garcia

Advisory Committee Member: Dr. Mary Ann 0. Torio

In silico analysis was done to determine the presence of bioactive peptides exhibiting anti-angiotensin I-converting enzyme activity using amino acid sequences of mungbean globulins and albumins obtained from the NCBI protein database. ACE-inhibiting peptides consisting of 2-4 amino acid residues were found to be present within the parent sequences of mungbean globulins and albumins.

The total proteins from mungbean, Vigna radiata var. Pag-asa 7, were extracted using 35 mM phosphate buffer, pH 7.0, with 0.40 M sodium chloride. The crude protein extract contains 12.2 mg/mL of proteins using Bradford method. The total globulins were then precipitated and separated from the total albumins through dialysis. Purification of the protein fractions was monitored by SDS-PAGE. The protein content of the globulin and albumin fractions was found to be 7.3 and 1.8 mg/mL, respectively.

The partially purified protein fractions were digested using trypsin and chymotrypsin in a 1:1 protein-to-enzyme ratio. 200 µL of the sample was used and mixed with the same volume of a 1-mg/mL solution of the enzyme. The ACE inhibitory activity (in units) of the hydrolysates obtained after 24 hours of enzymatic digestion was determined to be 1.32x10-3, 2.11x10-3, 1.05x10"3 and 1.96x10' units for the trypsin-globulin, chymotrypsin-globulin, trypsin-albumin and chymotrypsin-albumin digests, respectively. These values for inhibitory activity correspond to percentages of ACE inhibition of 58.68, 93.55, 46.53 and 86.85%, respectively.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

Thesis

Document Type

Thesis

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