Isolation and partial purification of the crude protein from cashew nut (Anacardium occidentale), peanut (Arachis hypogaea L. ), and pili nut (Canarium ovatum Engl.) exhibiting angiotensin converting enzyme inhibitory activity.

Date

10-2010

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Mary Ann O Torio

Co-adviser

Mark Rickard N. Angelia

Committee Member

Roberta N. Garcia

Abstract

The crude proteins of peanut, cashew nut and pili nut were isolated using different extraction buffers. For peanut and cashew nut, protein extraction buffer containing 0.02 M Tris-HCI with pH 8.11 and 8.2 were used. For pili nut, 0.5 M NaCI was used. The protein content was determined using Bradford method. The protein content of peanut, cashew nut and pili nut were found to be 22.77 mg/mL, 17.66 mg/mL and 12.64 mg/mL, respectively. Partial purification of the crude proteins of three samples was done by ammonium sulfate fractionation and dialysis. In vitro digestibility of the crude proteins by proteases was carried out using trypsin, chymotrypsin, and pepsin. Enzyme hydrolysates of pepsin, trypsin and chymotrypsin after 24 hours digestion were subjected to angiotensin 1-converting enzyme (ACE) inhibitory activity assay. Pepsin hydrolysate front peanut and cashew nut resulted to 2.93 x 10' and 2.06 x 10-3 inhibitory activity units, respectively. Pepsin, trypsin, and chymotrypsin hydrolysates of pili nut resulted to 3.13 x 104, 3.30 x le, and 3.26 x 104 inhibitory activity units, respectively. Thus, peanut. cashew nut and pili nut contain bioactive peptides with anti-ACE (angiotensin (-converting enzyme) activity.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2010 C4 I83

Document Type

Thesis

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