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

doi:10.7506/spkx1002-6630-20230710-123

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

• Bioengineering • Previous Articles Next Articles

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

Abstract

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

CLC Number:

TS201.4

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

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