从海蜇性腺水解物中分离和鉴定具有抗氧化和血管紧张素转化酶抑制活性的肽。
Separation and Characterization of Antioxidative and Angiotensin Converting Enzyme Inhibitory Peptide from Jellyfish Gonad Hydrolysate.
机构信息
School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.
National Engineering Research Center of Seafood, Dalian 116034, China.
出版信息
Molecules. 2018 Jan 5;23(1):94. doi: 10.3390/molecules23010094.
The gonad of jellyfish (), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE.
水母性腺（）含有高蛋白含量和丰富的氨基酸组成，适合制备生物活性肽。用中性蛋白酶水解水母性腺得到水母性腺蛋白水解物（JGPH），然后通过超滤、凝胶过滤色谱和反相高效液相色谱（RP-HPLC）顺序进行纯化。采用 HPLC-MS/MS 对肽进行表征。鉴定并合成了一种具有氨基酸序列 Ser-Tyr (SY) 的肽，该肽具有良好的 ACE 抑制和抗氧化活性。该肽对 DPPH、·OH、超氧阴离子清除活性和 ACE 抑制活性的 IC 分别为 84.623 μM、1177.632 μM、456.663 μM 和 1164.179 μM。通过分子模拟获得了 SY 和 ACE C 结构域（ACE-C）结合位点中的锚。结果表明，从水母性腺蛋白水解物中纯化的二肽可用作功能性食品材料，有助于研究抗氧化和 ACE 抑制。
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