Purification and identification of peptides with high angiotensin-I converting enzyme (ACE) inhibitory activity from honeybee pupae (Apis mellifera) hydrolysates with in silico gastrointestinal digestion
Autor: | Huaigao Liu, Yuqi Zhang, Yongkang Luo, Kangni Chen, Xiaoxue Yang |
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Rok vydání: | 2019 |
Předmět: |
Proteases
030309 nutrition & dietetics Biochemistry High-performance liquid chromatography Industrial and Manufacturing Engineering Hydrolysate 03 medical and health sciences chemistry.chemical_compound 0404 agricultural biotechnology Pepsin medicine 0303 health sciences Chymotrypsin biology Molecular mass 04 agricultural and veterinary sciences General Chemistry Trypsin 040401 food science Papain chemistry biology.protein Food Science Biotechnology medicine.drug |
Zdroj: | European Food Research and Technology. 245:535-544 |
ISSN: | 1438-2385 1438-2377 |
Popis: | The objective was to identify peptides with ACE inhibitory activity generated from honeybee pupae hydrolysates. In addition, we simulated gastrointestinal digestion and predicted the potential cleavage sites of the identified peptides. Peptides derived from honeybee pupae were cleaved in silico by pepsin, trypsin, and chymotrypsin using the PeptideCutter tool of ExPASy. Honeybee pupae were hydrolyzed using four different proteases (Alcalase, neutrase, trypsin, and papain), and their ACE inhibitory activity and distribution of molecular weights were determined. The neutrase hydrolysates showed the highest ACE inhibitory activity. Then, the hydrolysates were isolated and purified using ultrafiltration, gel filtration chromatography, and reversed-phased high performance liquid chromatography. Three novel ACE inhibitory peptides were identified by LC–MS/MS, AVFPSIVGR, PPVLVFV, and PGKVHIT, which exhibited the most potent ACE inhibitory activity, with IC50 values of 6.64, 47.7859, and 223.869 µM, respectively. In simulated in silico gastrointestinal digestion, peptides AVPFSIVGR and PGKVHIT had the position of cleavage sites by pepsin, chymotrypsin and trypsin, and PPVLVFV was cleaved by pepsin and chymotrypsin. We hope these results support the application of honeybee pupa hydrolysates as functional ingredients in foods and pharmaceuticals. |
Databáze: | OpenAIRE |
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