Preparation of an ACE-inhibitory peptide from Perinereis aibuhitensis protein
Preparation of an ACE-inhibitory peptide from Perinereis aibuhitensis protein
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DOI：
10.1080/13102818.2017.1370983
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发表时间：
2017-08
影响因子：
1.4
通讯作者：
Li Chen;Shujun Wang
中科院分区：
文献类型：
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作者：
Li Chen;Shujun Wang
摘要以双齿围沙蚕蛋白为原料，采用中性蛋白酶水解法制备了具有血管紧张素转换酶（ACE）抑制活性的多肽，并对多肽的ACE抑制率进行了测定。优化的水解条件为：反应时间5 h，温度50 °C，pH 7，酶用量0.5%。在最佳水解条件下，PAP肽的ACE抑制率可达83.61%。通过超滤将水解产物分成两个分子量范围（低于和高于10 kDa）。随后通过Sephadex G-15凝胶过滤层析纯化具有较高ACE抑制的低于10-kDa的组分。经高效液相色谱-四极杆飞行时间质谱联用技术（HPLC-Q-TOF-MS）鉴定，其结构为Gly-Ala-Phe。因此，PAP经中性蛋白酶水解制备的肽可能是抗高血压保健品和药物的有益成分。
ABSTRACT The peptides with angiotensin-I converting enzyme (ACE)-inhibition activity were prepared from Perinereis aibuhitensis protein (PAP) by hydrolysis with neutral protease, in which the ACE-inhibition rate of peptides derived from PAP was monitored. The hydrolysis conditions were optimised as follows: reaction time 5 h, temperature 50 °C, pH 7 and enzyme amount 0.5%. Under the optimum hydrolysis conditions, the ACE-inhibition rate of peptides of PAP reached up to 83.61%. The hydrolysates were fractionated into two molecular-weight ranges (below and above 10 kDa) by ultrafiltration. The below-10-kDa fraction with higher ACE-inhibitory was subsequently purified by Sephadex G-15 gel filtration chromatography. The structure of the active peptide was identified as Gly-Ala-Phe by high performance liquid chromatography (HPLC) coupled with quadrupole (Q) time-of-flight (TOF) mass spectrometry (HPLC-Q-TOF-MS). Thus, the peptide prepared from PAP by hydrolysis with neutral protease could be a beneficial ingredient of nutraceuticals and pharmaceuticals against hypertension.