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首页> 外文期刊>Fisheries and Aquatic Sciences >The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate
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The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

机译：虹鳟鱼肌肉水解产物中的新型血管紧张素I转化酶抑制肽

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The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The IC_(50) value of purified ACE inhibitory peptide was 63.9 uM. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.
机译：这项研究的目的是纯化和表征从虹鳟鱼Onmyhynchus mykiss肌肉的酶解产物中纯化的血管紧张素I转化酶（ACE）抑制肽。去除脂质后，虹鳟鱼的近似组成分析显示蛋白质，脂质和水分分别为24.4％，1.7％和68.3％。在六种水解物中，消化性水解物表现出最高的ACE抑制活性。我们尝试使用ODS色谱柱上的高效液相色谱法从消化性水解物中纯化ACE抑制肽。纯化的ACE抑制肽的IC_（50）值为63.9uM。该肽的氨基酸序列鉴定为Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn，分子量为1,220 Da，Lineweaver-Burk图表明它们可作为ACE的竞争性抑制剂。我们的研究表明，从虹鳟鱼肌肉蛋白中纯化出的新型ACE抑制肽作为功能性食品中的抗高血压化合物可能是有益的。

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