Details

Autor(en) / Beteiligte

• Pan, Saikun
• Wang, Shujun
• Jing, Lingling
• Yao, Dongrui

Titel

Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein

Ist Teil von

• Food chemistry, 2016-11, Vol.211, p.423-430

Ort / Verlag

England: Elsevier Ltd

Erscheinungsjahr

2016

Quelle

MEDLINE

Beschreibungen/Notizen

• •The sequence of the peptide is Pro-Ala-Phe-Gly.•The inhibitory kinetic mechanism of the peptide is non-competitive.•The peptide effectively inhibits gastrointestinal proteases. Hydrolysates containing angiotensin-I converting enzyme (ACE)-inhibitory peptide were prepared from Enteromorpha clathrata protein using alcalase. The hydrolysates were fractionated into two molecular-weight ranges (below and above 10kDa) by ultrafiltration. The below-10kDa fraction showed higher ACE-inhibitory activity and was subsequently purified by Sephadex G-15 gel filtration chromatography. The structure of active peptide was identified as Pro-Ala-Phe-Gly by HPLC-Q-TOF-MS and its IC50 value was 35.9μM. The yield of this peptide from E. clathrata protein was 0.82%. Lineweaver–Burk plots demonstrated that the inhibitory kinetic mechanism of this peptide was non-competitive. Stability study revealed that the purified peptide showed resistance against gastrointestinal proteases. Thus, E. clathrata protein hydrolysate treated with alcalase is a beneficial ingredient of nutraceuticals and pharmaceuticals against hypertension and related diseases.