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Current Analytical Chemistry


ISSN (Print): 1573-4110
ISSN (Online): 1875-6727

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 and Song-Qing Hu

Volume 8 , Issue 1 , 2012

Page: [180 - 185] Pages: 6

DOI: 10.2174/157341112798472224

Price: $58


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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