Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme -Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel IGigantidas vrijenhoeki/I

Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme -Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel IGigantidas vrijenhoeki/I

The objective of this study was to prepare an angiotensin I-converting enzyme (ACE)-inhibitory peptide from the hydrothermal vent mussel, Gigantidas vrijenhoeki. The G. vrijenhoeki protein was hydrolyzed by various hydrolytic enzymes. The peptic hydrolysate exhibited the highest ACE-inhibitory activ...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Marine drugs 2023-08, Vol.21 (8)
Hauptverfasser: Heo, Seong-Yeong, Kang, Nalae, Kim, Eun-A, Kim, Junseong, Lee, Seung-Hong, Ahn, Ginnae, Oh, Je Hyeok, Shin, A Young, Kim, Dongsung, Heo, Soo-Jin
Format: Artikel
Sprache:eng
Schlagworte:
ACE inhibitors
Antihypertensive drugs
Chemical properties
Health aspects
Molecules
Mussels
Peptides
Pharmaceutical research
Production processes
Protein hydrolysates
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The objective of this study was to prepare an angiotensin I-converting enzyme (ACE)-inhibitory peptide from the hydrothermal vent mussel, Gigantidas vrijenhoeki. The G. vrijenhoeki protein was hydrolyzed by various hydrolytic enzymes. The peptic hydrolysate exhibited the highest ACE-inhibitory activity and was fractionated into four molecular weight ranges by ultrafiltration. The
ISSN:1660-3397
1660-3397
DOI:10.3390/md21080458