Current Analytical Chemistry

Samuel Achilefu
Washington University
St. Louis, MO


Isolation and Identification of an Angiotensin-I Converting Enzyme Inhibitory Peptide from Yeast (Saccharomyces cerevisiae)

Author(s): He Ni, Lin Li, Sha-Sha Guo, Hai-Hang Li, Rui Jiang, Song-Qing Hu.


Angiotensin-I converting enzyme (ACE) has an important function in blood pressure regulation. ACEinhibitory peptides can lower blood pressure by inhibiting ACE activity. In this investigation, water-soluble proteins were extracted from yeast (Saccharomyces cerevisiae) and hydrolyzed by yeast protein extraction enzyme to isolate ACEinhibitory peptides. Peptides with ACE-inhibitory activity were further separated and purified by ultrafiltration and fast protein liquid chromatography (FPLC). A hexapeptide, Thr-Pro-Thr-Gln-Gln-Ser, with a calculated molecular weight of 660Da, was purified and identified by MALDI-TOF-MS. The hexapeptide showed remarkable ACE-inhibitory activity, with an IC50 of 73.25 μg/mL. The level of ACE-inhibitory activity of the hexapeptide indicated that it is a good candidate for development of a hypotension drug or functional food.

Keywords: Angiotensin-I converting enzyme, Bioactive peptide, Inhibitory peptide, Yeast protein, Fast protein liquid chromatography (FPLC), High performance liquid chromatography, Mass spectrometry, MALDI-TOF-MS, Ultrafiltration, Water-soluble proteins

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Article Details

Year: 2012
Page: [180 - 185]
Pages: 6
DOI: 10.2174/157341112798472224