Extraction And Characterization of Bioactive Peptides Derived from the Hydrolysates of Total Soluble Proteins of Pistachio Nuts (Pistacia vera L.)

Authors

  • Nico G. Dumandan Institute of Chemistry, College of Arts and Sciences, University of the Philippines Los Baños, College, Laguna 4031
  • Mark Rickard N. Angelica Institute of Chemistry, College of Arts and Sciences, University of the Philippines Los Baños, College, Laguna 4031
  • Ma. Desiree Belina-Aldemita Institute of Chemistry, College of Arts and Sciences, University of the Philippines Los Baños, College, Laguna 4031
  • Mary Ann O. Torio Institute of Chemistry, College of Arts and Sciences, University of the Philippines Los Baños, College, Laguna 4031

DOI:

https://doi.org/10.26534/kimika.v25i1.1-10

Keywords:

Pistachio, antioxidative, antibacterial, angiotensin-converting, bioactive peptides

Abstract

This study explored the potential of pistachio nut (Pistacia vera L.) total soluble proteins to release bioactive peptides exhibiting angiotensin-converting enzyme (ACE) inhibition, antioxidative, and antibacterial activities. The total soluble proteins were extracted from the ground, defatted nut using 0.010 M phosphate buffered saline, pH 6.8. The extracted proteins were hydrolyzed at different time intervals using trypsin and chymotrypsin. Hydrolysates of the total soluble proteins at 24 h digestion time exhibited the highest ACE-inhibition activity of 76.67 ± 0.10% and 70.83 ± 0.00% for chymotrypsin and trypsin digestion, respectively. The 24 h enzymatic hydrolysates were further fractionated in RP-HPLC using a C18 Vydac column. The C1 fraction from the 24 h chymotryptic hydrolysates and T2 from the 24 h tryptic hydrolysates exhibited the highest ACE-inhibition activities with an IC50 value of 147.7 ± 0.8 and 148.7 ± 0.6 μg/mL, respectively. The 24 h chymotryptic and tryptic hydrolysates also exhibited a DPPH radical scavenging activity of 83.7 ± 1.1% (EC50 = 356.5 ± 1.0 μg/mL) and 80.4 ± 0.2% (EC50 = 402.7 ± 1.1 μg/mL), respectively. The hydroxyl radical scavenging activities of the 24 h chymotryptic and tryptic hydrolysates were found to be 22.8 ± 1.0 and 16.6 ± 3.7%, respectively. However, the 24 h tryptic and chymotryptic hydrolysates did not exhibit any antibacterial activity against the gram-negative Escherichia coli and gram-positive Staphylococcus aureus. Therefore, the total soluble proteins of pistachio nuts were found to contain peptides exhibiting ACE-inhibition and antioxidative activities upon hydrolysis with trypsin and chymotrypsin.

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Published

2014-06-17

How to Cite

Dumandan, N. G., Angelica, M. R. N., Belina-Aldemita, M. D., & Torio, M. A. O. (2014). Extraction And Characterization of Bioactive Peptides Derived from the Hydrolysates of Total Soluble Proteins of Pistachio Nuts (Pistacia vera L.). KIMIKA, 25(1), 1–10. https://doi.org/10.26534/kimika.v25i1.1-10

Issue

Vol. 25 No. 1 (2014)

Section

Research Articles

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