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首页> 外文期刊>African Journal of Biotechnology >Purification and characterization of angiotensin-1 converting enzyme (ACE)-inhibitory peptide from the jellyfish, Nemopilema nomurai
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Purification and characterization of angiotensin-1 converting enzyme (ACE)-inhibitory peptide from the jellyfish, Nemopilema nomurai

机译：海noNemopilema nomurai的血管紧张素-1转换酶（ACE）抑制肽的纯化和鉴定

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The?Nemopilema nomurai?hydrolysate was produced by the reaction of papain, and an angiotensin-Ι converting enzyme (ACE)-inhibitory peptide was purified by using the molecular cut-offs membrane filter, the gel filtration chromatography with Sephadex LH-20 and the reverse phase chromatographic method using C18and C12?columns. Purification yield of the active peptide was estimated to be 0.2 ± 0.1%, starting from the lyophilized jellyfish. The infrared (IR), proton nuclear magnetic resonance spectroscopy (1H NMR), carbon nuclear magnetic resonance (13C NMR) and mass spectrometry (MS) spectrometer analyses elucidated that the structure of the purified peptide is tyrosine-isoleucine (Tyr-Ile). The inhibitory concentration at 50% (IC50) and?Ki?values were calculated to be 2.0 ± 0.3 μg/ml and 3.3 ± 0.3 μM, respectively, which acts as a competitive inhibitor to ACE.
机译：通过木瓜蛋白酶的反应产生Nemopilemanomuraiβ水解产物，并通过使用分子截止膜过滤器，Sephadex LH-20的凝胶过滤色谱法和NaCl-脱氧核糖核酸纯化纯化血管紧张素-1转化酶（ACE）-抑制性肽。 C18和C12？色谱柱的反相色谱方法。从冻干的水母开始，活性肽的纯化产率估计为0.2±0.1％。红外（IR），质子核磁共振波谱（1H NMR），碳核磁共振波谱（13C NMR）和质谱（MS）光谱仪分析表明，纯化的肽的结构是酪氨酸-异亮氨酸（Tyr-Ile）。计算出50％的抑制浓度（IC50）和？Ki？值分别为2.0±0.3μg/ ml和3.3±0.3μM，它们是ACE的竞争性抑制剂。

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