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- Title
Investigation of Chlorella pyrenoidosa Protein as a Source of Novel Angiotensin I-Converting Enzyme (ACE) and Dipeptidyl Peptidase-IV (DPP-IV) Inhibitory Peptides.
- Authors
Li, Yuchen; Aiello, Gilda; Fassi, Enrico Mario Alessandro; Boschin, Giovanna; Bartolomei, Martina; Bollati, Carlotta; Roda, Gabriella; Arnoldi, Anna; Grazioso, Giovanni; Lammi, Carmen; Nagaoka, Satoshi
- Abstract
Chlorella pyrenoidosa (C. pyrenoidosa) is a microalgae species with a remarkably high protein content that may potentially become a source of hypotensive and hypoglycemic peptides. In this study, C. pyrenoidosa proteins were extracted and hydrolyzed overnight with pepsin and trypsin with final degrees of hydrolysis of 18.7% and 35.5%, respectively. By LC-MS/MS, 47 valid peptides were identified in the peptic hydrolysate (CP) and 66 in the tryptic one (CT). At the concentration of 1.0 mg/mL, CP and CT hydrolysates inhibit in vitro the angiotensin-converting enzyme (ACE) activity by 84.2 ± 0.37% and 78.6 ± 1.7%, respectively, whereas, tested at cellular level at the concentration of 5.0 mg/mL, they reduce the ACE activity by 61.5 ± 7.7% and 69.9 ± 0.8%, respectively. At the concentration of 5.0 mg/mL, they decrease in vitro the DPP-IV activity by 63.7% and 69.6% and in Caco-2 cells by 38.4% and 42.5%, respectively. Short peptides (≤10 amino acids) were selected for investigating the potential interaction with ACE and DPP-IV by using molecular modeling approaches and four peptides were predicted to block both enzymes. Finally, the stability of these peptides was investigated against gastrointestinal digestion.
- Subjects
PROTEIN analysis; PROTEIN metabolism; PROTEINS; PHYSICAL &; theoretical chemistry; TRYPSIN; IN vitro studies; PEPSIN; LIQUID chromatography; PROTEOLYTIC enzymes; MASS spectrometry; DESCRIPTIVE statistics; ALGAE; CELL lines; MOLECULAR docking; ANGIOTENSIN converting enzyme
- Publication
Nutrients, 2021, Vol 13, Issue 5, p1624
- ISSN
2072-6643
- Publication type
Article
- DOI
10.3390/nu13051624