红毛藻血管紧张素转化酶抑制肽的筛选及其稳定性评价

doi:10.7506/spkx1002-6630-20230710-123

食品科学 ›› 2024, Vol. 45 ›› Issue (2): 188-194.doi: 10.7506/spkx1002-6630-20230710-123

红毛藻血管紧张素转化酶抑制肽的筛选及其稳定性评价

吴靖娜，洪乔茜，廖榕榕，蔡水淋，陈晓婷，苏海燕，苏筱，许莉，潘南，卓诗晴

（1.厦门医学院海洋生物医药资源福建省高校工程研究中心，福建厦门 361023；2.厦门医学院厦门市海洋药用天然产物资源重点实验室，福建厦门 361023；3.福建省水产研究所，福建厦门 361013）

出版日期:2024-01-25 发布日期:2024-02-05
基金资助:
厦门市海洋与渔业发展专项资金青年科技创新项目（23YYST079QCA12）；福建省大学生创新创业训练计划项目（202312631032）

Screening and Stability Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides from Bangia fusco-purpurea

WU Jingna, HONG Qiaoxi, LIAO Rongrong, CAI Shuilin, CHEN Xiaoting, SU Haiyan, SU Xiao, XU Li, PAN Nan, ZHUO Shiqing

(1. Fujian Universities and Colleges Engineering Research Center of Marine Biopharmaceutical Resources, Xiamen Medical College, Xiamen 361023, China; 2. Xiamen Key Laboratory of Marine Medicinal Natural Products Resources, Xiamen Medical College, Xiamen 361023, China; 3. Fisheries Research Institute of Fujian, Xiamen 361013, China)

Online:2024-01-25 Published:2024-02-05

摘要/Abstract

摘要： 本实验以红毛藻为原料，利用酶解法及超滤分级制备获得不同分子质量的肽组分，经高效液相色谱法测定体外血管紧张素转化酶（angiotensin-converting enzyme，ACE）抑制活性发现F2组分（800～2 000 Da）的ACE抑制率最高；采用液相色谱-串联质谱技术和PEAKS Studio软件的de novo从头测序对F2组分进行氨基酸序列鉴定，并结合分子对接筛选出与ACE稳定结合的6 个ACE抑制肽。利用固相合成法制备预测肽并经体外ACE抑制活性验证，发现L1（LVLLFLFGE）的ACE抑制活性最高，半抑制浓度（half maximal inhibitory concentration，IC50）为14.22 μg/mL。分子对接结果表明，L1对ACE的抑制主要归因于其能够与ACE的活性口袋形成氢键相互作用。最后，探讨温度、pH值、金属离子、光照类型和模拟胃肠道酶系消化对L1稳定性的影响，结果表明L1具有较好的热稳定性和离子强度稳定性，pH＞2时抑制活性逐步减弱，紫外光处理会影响其抑制活性，体外模拟胃肠液处理后L1的ACE抑制率虽然显著降低，但仍具有较高ACE抑制活性。

关键词: 红毛藻；de novo从头测序；虚拟筛选；血管紧张素转化酶抑制肽；稳定性

Abstract: In this study, peptide fractions (F1-F4) with different molecular masses were obtained from Bangia fusco-purpurea through enzymatic hydrolysis and ultrafiltration. F2, with molecular masses of 800–2 000 Da, exhibited the highest in vitro angiotensin-converting enzyme (ACE) inhibitory activity as determined by high performance liquid chromatography (HPLC). The amino acid sequence of F2 was identified through liquid chromatography-tandem mass spectrometry (LC-MS/MS) and de novo sequencing using PEAKS Studio software. Six ACE inhibitory peptides that stably bind to ACE were selected through molecular docking. The predicted peptides were synthesized by solid-phase synthesis and their in vitro ACE inhibitory activity was verified. Among them, L1 (LVLLFLFGE) showed the highest ACE inhibitory activity with a half maximal inhibitory concentration (IC50) value of 14.22 μg/mL. Molecular docking results indicated that the inhibition of ACE by L1 was mainly attributed to its ability to form hydrogen bond interactions with the active site of ACE. Finally, the effects of temperature, pH, metal ions, light exposure, and simulated gastrointestinal digestion on the stability of L1 were investigated. The results revealed that L1 was highly stable to heat and ionic strength. However, its activity gradually decreased at pH > 2, and was affected by ultraviolet treatment. The ACE inhibitory activity of L1 decreased after simulated gastric and intestinal digestion, but was still significant.

Key words: Bangia fusco-purpurea; de novo sequencing; virtual screening; angiotensin-converting enzyme inhibitory peptides; stability

中图分类号:

TS201.4

吴靖娜，洪乔茜，廖榕榕，蔡水淋，陈晓婷，苏海燕，苏筱，许莉，潘南，卓诗晴. 红毛藻血管紧张素转化酶抑制肽的筛选及其稳定性评价[J]. 食品科学, 2024, 45(2): 188-194.

WU Jingna, HONG Qiaoxi, LIAO Rongrong, CAI Shuilin, CHEN Xiaoting, SU Haiyan, SU Xiao, XU Li, PAN Nan, ZHUO Shiqing. Screening and Stability Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides from Bangia fusco-purpurea[J]. FOOD SCIENCE, 2024, 45(2): 188-194.

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红毛藻血管紧张素转化酶抑制肽的筛选及其稳定性评价

Screening and Stability Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides from Bangia fusco-purpurea

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