食品科学 ›› 2013, Vol. 34 ›› Issue (23): 118-122.doi: 10.7506/spkx1002-6630-201323025

• 基础研究 • 上一篇    下一篇

蚕蛹源ACE抑制肽的分离纯化与结构研究

吴琼英1,杜金娟1,徐金玲1,贾俊强2,颜 辉1,桂仲争2   

  1. 1.江苏科技大学生物与化学工程学院,江苏 镇江 212018;2.中国农业科学院蚕业研究所,江苏科技大学,江苏 镇江 212018
  • 收稿日期:2012-11-23 修回日期:2013-10-28 出版日期:2013-12-15 发布日期:2014-01-03
  • 通讯作者: 吴琼英 E-mail:wuqy1@163.com
  • 基金资助:

    江苏省自然科学基金面上项目(BK2012693);江苏省科技支撑计划项目(BE2011389);
    江苏科技大学青年骨干教师支持计划项目(37210901)

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

WU Qiong-ying1,DU Jin-juan1,XU Jin-ling1,JIA Jun-qiang2,YAN Hui1,GUI Zhong-zheng2   

  1. 1. School of Biotechnology and Chemical Engineering, Jiangsu University of Science and Technology, Zhenjiang 212018, China;
    2. Sericultural Research Institute, Chinese Academy of Agricultural Sciences, Jiangsu University of Science and Technology,
    Zhenjiang 212018, China
  • Received:2012-11-23 Revised:2013-10-28 Online:2013-12-15 Published:2014-01-03
  • Contact: WU Qiong-ying E-mail:wuqy1@163.com

摘要:

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(IC50 0.072mg/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。

关键词: 蚕蛹蛋白, ACE抑制肽, 分离纯化, 液质联用

Abstract:

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 silkworm 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.

Key words: silkworm pupae protein, angiotensin-converting enzyme (ACE) inhibitory peptide, separation and purification, liquid chromatography-mass spectrometry

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