Extraction and characterization of bioactive peptides from total soluble protein hydrolysates of pistachio nuts (Pistacia vera L.)

Date

10-2013

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Mark Richard N. Angelia

Restrictions

Restricted: Not available to the general public. Access is available only after consultation with author/thesis adviser and only to those bound by the confidentiality agreement.

Abstract

The total soluble proteins of pistachio nuts (Pistacia vera L.) was evaluated for the presence of ACE-inhibitor, antibacterial and antioxidative peptides. Enzymatic hydrolysis of TSPPN at 24-hr digestion time exhibits highest ACE-inhibition activity of 76.67% and 70.83% for chymotrypsin and trypsin digestion, respectively. Purification and fractionation of bioactive peptides from both digests using RP-HPLC revealed peaks with relatively high ACE-inhibition with IC50 values of 147.7 μg/mL chymotrypsin digest and 236.4 and 148.7 μg/mL for the peaks observed in trypsin digestion. The 24-hr digest of TSPPN were subjected for antioxidative activity against DPPH and hydroxyl radicals. Chymotrypsin and trypsin digestion of TSPPN showed 83.7 (EC50: 356.5 μg/mL) and 80.4% (EC50: 402.7 μg/mL) DPPH radical scavenging activity, respectively. The TSPPN hydrolysates scavenge hydroxyl radical at 22.8 and 16.6% for chymotrypsin and trypsin digestion, respectively. No antibacterial activity against Escherichia coli and Staphylococcus aureus was observed in the 24-hr TSPPN hydrolysates. Therefore, bioactive peptides encoding for ACE inhibition, antioxidative and antibacterial activities are effectively released using chymotrypsin at nearly complete digestion (24-hr) than trypsin digestion. It can also be concluded that consumption of pistachio nuts may help reduce the risk of hypertension and oxidative stress.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2013 C42 /D86

Document Type

Thesis

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