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

Abstract

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 IC 50 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.

Inhibition Mechanism and Model of an Angiotensin I-Converting Enzyme (ACE)-Inhibitory Hexapeptide from Yeast (Saccharomyces cerevisiae)

“…TPTQQS has been shown to be an effective ACE-inhibitory peptide that was isolated from hydrolyzed yeast protein in our previous study [16] . However, the amino acid sequence of this peptide is not in accordance with the results of structure-activity correlation studies on ACE-inhibitory peptides [11] .…”

“…The active cleft divides tACE into two structural subdomains: subdomain I and subdomain II. The peptide was adjacent to subdomain I, far from the active site, which includes the important positions S1′ and S2′, especially [16] .…”

“…In a previous study [16] , we purified a highly active ACE-inhibitory hexapeptide from yeast, Thr-Pro-Thr-Gln-Gln-Ser (TPTQQS); however, this peptide does not have the characteristics of the highly active ACE-inhibitory peptides that have been previous characterized [11] . In this study, we investigated the inhibition mechanism of the hexapeptide on the basis of its sequence to provide a reference for the design of drugs that target such enzymes as ACE.…”

Preparation and Properties of Bioactive Peptides from Yeast Protein

“…The method was referred to Ni(2012) with some modifications, the method was conducted as follows: yeast powder (1:15 w/V) was added to distilled water, then adjusted to pH 7.7, incubated at 60°C for 30 minutes after that. In the next step, the solutions were treated with yeast protein extraction enzyme (3.5% w/w), and the protein was extracted with shaking for 6 hours.…”

Purification and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from abalone (Haliotis discus hannai Ino) gonads

“…Because of their confirmed or suspected association with side effects such as taste disturbances, cough and skin rashes, the tendency for aCE inhibitorrelated research is going progressively toward the development of non-toxic and natural substitutions. During the last decade, studies have focused on the production and isolation of peptides with potent aCE inhibitory activity from various sources, including lysozyme [7], casein [8], soya milk [9], collagen and gelatin [10], bovine brisket [11], fish [12,13] and production by fermentation [14,15]. Studies suggested that natural peptides consisting of two or three amino acids have higher affinities with tissues, becoming absorbed and assimilated more easily, than the recognized inhibitor such as captopril [16,17].…”