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新型血管紧张素转化酶抑制肽的筛选研究 来源于红藻 Acrochaetium sp.

First Report of Screening of Novel Angiotensin-I Converting Enzyme Inhibitory Peptides Derived from the Red Alga Acrochaetium sp.

机构信息

Department of Aquaculture, Faculty of Fisheries and Marine Science, Universitas Diponegoro, Semarang, 50275, Indonesia.

Department of Biological Science and Technology, National Pingtung University of Science and Technology, Pingtung, 91201, Taiwan.

出版信息

Mar Biotechnol (NY). 2022 Oct;24(5):882-894. doi: 10.1007/s10126-022-10152-w. Epub 2022 Sep 8.

DOI:10.1007/s10126-022-10152-w
PMID:36074309
Abstract

ACE inhibitors generated from food proteins have recently become the most well-known subclass of bioactive peptides, and their bio-functionality can be a potential alternative to natural bioactive food components and synthetic drugs. The bioactivities of Acrochaetium sp., the red alga used in this investigation, have never been reported before. Screening of bioactive peptides from Acrochaetium sp. as ACE inhibitors were hydrolyzed with various proteolytic enzymes. Protein hydrolysates were fractionated separately using reversed phased (RP) and strong cation exchange (SCX) chromatography and identified as VGGSDLQAL (VL-9) using α-chymotrypsin. It comes from Phycoerythrin (PE), an abundant protein in a primarily red alga. The peptide VL-9 shows the ACE inhibitory activity with IC value 433.1 ± 1.08 µM. The inhibition pattern showed VL-9 as a non-competitive inhibitor. Molecular docking simulation proved that VL-9 was non-competitive inhibition due to the interaction peptide and ACE was not in the catalytic site. Moreover, VL-9 derived from Acrochaetium sp. is a natural bioactive peptide that is safer and available for food protein; also, the ACE inhibitory peptide derived from Acrochaetium sp. could be the one alternative resource to develop functional food for combating hypertension.

摘要

ACE 抑制剂来源于食物蛋白,最近已成为最知名的生物活性肽亚类,其生物功能可能是天然生物活性食物成分和合成药物的潜在替代品。本研究中使用的红藻 Acrochaetium sp. 的生物活性以前从未报道过。用各种蛋白酶水解 Acrochaetium sp. 作为 ACE 抑制剂的生物活性肽。使用 α-糜蛋白酶将蛋白质水解物分别用反相(RP)和强阳离子交换(SCX)色谱法进行分离,并鉴定为 VGGSDLQAL(VL-9)。它来自藻红蛋白(PE),一种主要的红藻中的丰富蛋白质。肽 VL-9 表现出 ACE 抑制活性,IC 值为 433.1 ± 1.08 μM。抑制模式表明 VL-9 是非竞争性抑制剂。分子对接模拟证明 VL-9 是由于与 ACE 的相互作用,而不是在催化部位,因此是非竞争性抑制。此外,来源于 Acrochaetium sp. 的 VL-9 是一种天然的生物活性肽,更安全,可用于食品蛋白;此外,来源于 Acrochaetium sp. 的 ACE 抑制肽可能是开发用于治疗高血压的功能性食品的替代资源之一。

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