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首页> 外文期刊>Fisheries and Aquatic Sciences >ACE-lnhibitory Properties of Proteolytic Hydrolysates from Giant Jellyfish Nemopilema nomurai
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ACE-lnhibitory Properties of Proteolytic Hydrolysates from Giant Jellyfish Nemopilema nomurai

机译：野水母Nemopilema nomurai蛋白水解产物的ACE抑制特性。

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摘要

This study aimed to determine the degree of hydrolysis and angiotensin-I-converting enzyme (ACE)-inhibitory activity of Giant Jellyfish Nemopilema nomurai (jellyfish) hydrolysates. The degree of hydrolysis using six proteolytic enzymes (Alcalase, Flavo-zyme, Neutrase, papain, Protamex, and trypsin) ranged from 13.1-36.8% and the inhibitory activities from 20.46-79.58%. Using papain hydrolysate, we newly isolated and characterized ACE-inhibitory peptides with a molecular weight of 3,000-5,000 Da thatoriginated from jellyfish collagen. The purified peptide (Fll-b) was predicted to be produced from an alpha-2 fragment of the type IV collagen of jellyfish. The N-terminal sequence of Fll-b was Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly- and showed 87% identityto the collagen type IV alpha-2 fragment of Rattus norvegicus and a predicted protein from Nematostella vectensis, indicating that the ACE-inhibitory peptide originated from the collagen hydrolysate and had an IC_(50) value of 3.8 ug/mL. The primary structure of the fragment is now being studied; this peptide represents an interesting new type of ACE inhibitor and will provide knowledge of the potential applications of jellyfish components as therapies for hypertension.
机译：本研究旨在确定巨型水母Nemopilema nomurai（水母）水解产物的水解程度和血管紧张素-I转换酶（ACE）抑制活性。使用六种蛋白水解酶（Alcalase，Flavo-zyme，Neutrase，木瓜蛋白酶，Protamex和胰蛋白酶）的水解度范围为13.1-36.8％，抑制活性为20.46-79.58％。使用木瓜蛋白酶水解产物，我们新分离并鉴定了由水母胶原蛋白产生的分子量为3,000-5,000 Da的ACE抑制肽。预计纯化的肽（Fll-b）由水母IV型胶原的alpha-2片段产生。 Fll-b的N端序列是Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly-，与褐家鼠的IV型胶原α-2片段和线虫的预测蛋白具有87％的同一性vectensis，表明ACE抑制肽起源于胶原蛋白水解产物，IC_（50）值为3.8 ug / mL。片段的主要结构正在研究中。这种肽代表了一种有趣的新型ACE抑制剂，将提供有关水母成分作为高血压疗法的潜在应用的知识。

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