蚕蛹源ACE抑制肽的分离纯化与结构研究

doi:10.7506/spkx1002-6630-201323025

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

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.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. 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/Abstract

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

中图分类号:

TS201. 1

吴琼英1，杜金娟1，徐金玲1，贾俊强2，颜辉1，桂仲争2. 蚕蛹源ACE抑制肽的分离纯化与结构研究[J]. 食品科学, 2013, 34(23): 118-122.

WU Qiong-ying1，DU Jin-juan1，XU Jin-ling1，JIA Jun-qiang2，YAN Hui1，GUI Zhong-zheng2. Separation, Purification and Structural Analysis of Angiotensin-converting Enzyme (ACE) Inhibitory Peptides from Hydrolysate of Silkworm Pupae Protein[J]. FOOD SCIENCE, 2013, 34(23): 118-122.

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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

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