蚕蛹源ACE抑制肽的分离纯化与结构研究

Separation, Purification and Structural Analysis of Angiotensin-converting Enzyme (ACE) Inhibitory Peptides from Hydrolysate of Silkworm Pupae Protein

目的：研究蚕蛹蛋白血管紧张素转换酶（ACE）抑制肽的结构特征。方法：采用超滤、DEAE-52离子交换色谱和Sephadex G-50凝胶色谱对蚕蛹蛋白酶解产物进行分离纯化,并利用液质联用对蚕蛹蛋白ACE抑制肽的结构特征进行初步分析。结果：分离得到的组分2（IC500.072mg/mL）对ACE抑制活性较高,是分离纯化前的2.95倍,为蚕蛹蛋白ACE抑制肽的主要组分。结论：组分2中ACE抑制肽的分子质量为226.34-983.61u,主要由2-8肽组成。

Objective： In order to investigate the structural characteristics of angiotensin-converting enzyme （ACE） inhibitory peptides from silkworm pupae protein. Methods： The ACE-inhibitory peptides from hydrolysate of silkworm pupae protein were separated and purified by ultrafiltration, DEAE-52 ion exchange chromatography and Sephadex G-50 gel filtration chromatography. Then, the structural characteristics of purified ACE-inhibitory peptides were analyzed by liquid chromatography-mass spectrometry （LC-MS）. Results： Fraction 2 （IC50 0.072 mg/mL） with higher ACE-inhibitory activity was obtained from silkwoma pupae protein hydrolysate. This fraction was the major component of ACE-inhibitory peptides, and its ACE-inhibitory activity was increased by 2.95 times over that of silkworm pupae protein hydrolysate. Conclusion： In fraction 2, ACE-inhibitory peptides were mainly composed of the peptide fragments from dipeptide to octapeptide, and their relative molecular weights were 226.34 to 983.61 u.