A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate
2009; Elsevier BV; Volume: 30; Issue: 6 Linguagem: Inglês
10.1016/j.peptides.2009.03.002
ISSN1873-5169
AutoresYuanhui Zhao, Bafang Li, Shiyuan Dong, Zunying Liu, Xue Qiang Zhao, Jingfeng Wang, Mingyong Zeng,
Tópico(s)Biochemical effects in animals
ResumoBody wall protein from the sea cucumber (Acaudina molpadioidea) was hydrolyzed sequentially with bromelain and alcalase. The hydrolysate was fractionated into two ranges of molecular weight (PH-I, >2 kDa; PH-II, <2 kDa) using an ultrafiltration membrane bioreactor system. The PH-II brought about a high angiotensin I-converting enzyme (ACE) inhibitory activity. An ACE inhibitory peptide was isolated from the PH-II, using the chromatographic methods including gel filtration, ion-exchange chromatography and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide was a novel peptide, showing very low similarity to other ACE inhibitory peptide sequences, and was sequenced as MEGAQEAQGD. It was found that the inhibitory activity of the peptide was intensified by 3.5 times from IC50 15.9 to IC50 4.5 μM after incubation with gastrointestinal proteases. The ACE inhibitory peptide from A. molpadioidea showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR), at a dosage of 3 μM/kg.
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