Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki

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...

Full description

Saved in:
Bibliographic Details
Published in:Marine drugs 2023-08, Vol.21 (8), p.458
Main Authors: 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: Article
Language:English
Subjects:
Amino acids
Angiotensin
Angiotensin I
angiotensin I-converting enzyme
bioactive peptide
Blood pressure
Conversion
Deep sea
Deep water
Enzymes
Gigantidas vrijenhoeki
Hydrogen bonding
Hydrogen bonds
Hydrolysates
hydrothermal vent mussel
Hydrothermal vents
Hypertension
Molecular docking
Molecular weight
Mollusks
Peptides
Peptidyl-dipeptidase A
Proteins
Ultrafiltration
Water purification
Zinc
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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