碱性蛋白酶酶解鸡腿骨蛋白制备血管紧张素转化酶抑制肽的研究

Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalase.

机构信息

Department of Hospitality Management, Toko University, Chiayi City, Taiwan.

出版信息

Anim Sci J. 2009 Feb;80(1):91-7. doi: 10.1111/j.1740-0929.2008.00601.x.

DOI:10.1111/j.1740-0929.2008.00601.x

PMID:20163474

Abstract

This study aims to identify peptides with angiotensin-I converting enzyme (ACE) inhibitory activity in hydrolysate from chicken leg bone protein hydrolyzed with alcalase for 4 h (A4H). The hydrolysate has demonstrated potent in vitro ACE inhibitory activity, and has been shown to attenuate the development of hypertension and cardiovascular hypertrophy in spontaneously hypertensive rats (SHR). A4H is competitive for ACE and was separated using high-performance liquid chromatography (HPLC) with a gel filtration column (Superdex Peptide HR 10/30). The results show that A4H is a mixed non-competitive inhibitor. Eighteen fractions were detected after separation of A4H, and most of them showed ACE inhibitory activity. Five fractions with strong ACE inhibitory activities (above 50%) were labeled from A to E. In addition, there were 10 peptides, consisting of 5-10 amino acid residues that were identified from fraction D that exhibited the strongest ACE inhibitory activity. Three of the identified peptides corresponded to peptides derived from collagen type I and chicken muscular protein. It is revealed that A4H has several peptides that possess ACE inhibitory activities.

摘要

本研究旨在鉴定碱性蛋白酶水解鸡腿骨蛋白 4 小时（A4H）得到的水解产物中具有血管紧张素转化酶（ACE）抑制活性的肽。该水解产物具有很强的体外 ACE 抑制活性，并已被证明可减轻自发性高血压大鼠（SHR）高血压和心血管肥大的发展。A4H 是 ACE 的竞争性抑制剂，并用高效液相色谱（HPLC）和凝胶过滤柱（Superdex Peptide HR 10/30）进行分离。结果表明，A4H 是一种混合非竞争性抑制剂。A4H 分离后检测到 18 个馏分，其中大多数表现出 ACE 抑制活性。从 A 到 E 标记出 5 个具有强 ACE 抑制活性（超过 50%）的馏分。此外，从具有最强 ACE 抑制活性的馏分 D 中鉴定出由 5-10 个氨基酸残基组成的 10 个肽。鉴定出的 3 个肽对应于来源于 I 型胶原和鸡肌肉蛋白的肽。结果表明，A4H 含有几种具有 ACE 抑制活性的肽。