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Angiotensin I-Converting Enzyme (ACE-I) Inhibition and Antioxidant Peptide from a Squilla Species
Protein & Peptide Letters ( IF 1.6 ) Pub Date : 2021-10-31 , DOI: 10.2174/0929866528666210616122835
Ila Joshi 1 , Nazeer Rasool Abdul 1
Affiliation  

Background: Oratosquilla woodmasoni is one of the marine squilla species, which is found in the entire Asia-Pacific region. This current study assesses the species as the main basis of both ACEi and antioxidant peptide.

Objective: To isolate the ACEi peptide derived from O. woodmasoni and examine its ACE inhibition along with antioxidant potential.

Materials and Methods: The squilla muscle protein was hydrolysed using alcalase and trypsin enzymes for 12 hours and tested for DH. The hydrolysates were examined for their ACEi activity and then the best hydrolysate was sequentially purified in various chromatographical methods. The purified peptide was studied for anti-oxidant and functional properties, followed by amino acid sequencing. The purified peptide was also evaluated for its toxicity by in vitro cell viability assay.

Results: The DH% was found to be 47.13 ± 0.72% and 89.43 ± 2.06% for alcalase and trypsin, respectively. The alcalase 5th-hour hydrolysate was detected with potent activity (65.97 ± 0.56%) using ACEi assay and was primarily fractionated using ultrafiltration; the maximum inhibitory activity was found with 77.04 ± 0.52% in 3-10 kDa fraction. Subsequently, the fraction was purified using IEC and GFC, in which the AC1-A2 fraction had higher antihypertensive activity (70.85 ± 0.78%). The non-toxic fraction showed hexapeptide HVGGCG with molecular weight 529 Da with great potential of antioxidant activity along with functional property.

Conclusion: This peptide could be developed as a potential ACE-inhibitory and antioxidant agent.



中文翻译:

来自 Squilla 物种的血管紧张素 I 转换酶 (ACE-I) 抑制和抗氧化肽

背景:Oratosquilla woodmasoni 是一种海洋松鼠,分布于整个亚太地区。目前的这项研究评估了作为 ACEi 和抗氧化肽的主要基础的物种。

目的:分离来自木松果的 ACEi 肽,并检测其 ACE 抑制作用和抗氧化潜力。

材料和方法:使用碱性酶和胰蛋白酶水解海松鼠肌肉蛋白 12 小时并测试 DH。检查水解产物的 ACEi 活性,然后用各种色谱方法依次纯化最好的水解产物。研究了纯化肽的抗氧化和功能特性,然后进行氨基酸测序。还通过体外细胞活力测定评估了纯化肽的毒性。

结果:发现碱性蛋白酶和胰蛋白酶的 DH% 分别为 47.13 ± 0.72% 和 89.43 ± 2.06%。使用 ACEi 测定法检测到 Alcalase 第 5 小时水解产物具有有效活性 (65.97 ± 0.56%),并使用超滤进行初步分级;在 3-10 kDa 级分中发现最大抑制活性为 77.04 ± 0.52%。随后,使用IEC和GFC对该级分进行纯化,其中AC1-A2级分具有更高的抗高血压活性(70.85±0.78%)。无毒部分显示出分子量为529 Da的六肽HVGGCG,具有巨大的抗氧化活性和功能特性。

结论:该肽可开发为潜在的 ACE 抑制剂和抗氧化剂。

更新日期:2021-12-24
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