Keywords

Spirulina Platensis, Angiotensin-Converting Enzyme, Ace, Inhibitory Peptide, Purification, Identification

Abstract

Angiotensin-converting enzyme (ACE) inhibitors play an important role in slowing down and suppressing hypertension by affecting the renin-angiotensin system. In this study, an angiotensin-converting enzyme (ACE) inhibitory peptide was isolated and purified from the papain hydrolyzate of Spirulina platensis through ultrafiltration, gel filtration chromatography, reversed-phase high-performance liquid chromatography, and other methods, and used Matrix-assisted laser desorption ionization-time of flight mass spectrometry (maldi-tof-ms) and amino acid sequencing were used to identify the purified peptides. In addition, its inhibition type and stability in simulated digestive environment in vitro were also studied. The results showed that the enzymatic hydrolyzate with a molecular mass ranging from 0 to 3000ku had the highest ace inhibitory activity, with an ic50 value of (1.03¡À0.04)g/l. This part of the enzymatic hydrolyzate was purified to obtain ace inhibitory peptide. The ic50 value was (0.0094¡À0.0002) g/l, which is equivalent to (27.36¡À0.14) ¦Ìmol/l. The sequence was identified as val-glu-pro. The lineweaver-burk plot and dixon plot show that the ace inhibitory peptide is a non-competitive inhibitor, with a ki value of (23.59¡À0.54) ¦Ìmol/l. In vitro stability experiments show that the inhibitory peptide can maintain good inhibitory activity under digestion by gastrointestinal proteases such as pepsin, chymotrypsin, and trypsin, indicating that the Spirulina-derived ace inhibitory peptide can be used in hypotensive functional foods and pharmaceuticals In terms of development, it has good development prospects.

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Original research done by Lu Jun, Ren Difeng, Wang Jianzhong, Tian Zhicangyu

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