Antihypertensive effect of surimi prepared from olive flounder (Paralichthys olivaceus) by angiotensin-I converting enzyme (ACE) inhibitory activity and characterization of ACE inhibitory peptides SCIE SCOPUS

DC Field Value Language
dc.contributor.author Oh, Jae-Young -
dc.contributor.author Kim, Eun-A -
dc.contributor.author Lee, Hyogeun -
dc.contributor.author Kim, Hyun-Soo -
dc.contributor.author Lee, Jung-Suck -
dc.contributor.author Jeon, You-Jin -
dc.date.accessioned 2020-12-10T08:00:35Z -
dc.date.available 2020-12-10T08:00:35Z -
dc.date.created 2020-05-27 -
dc.date.issued 2019-05 -
dc.identifier.issn 1359-5113 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/38862 -
dc.description.abstract In this study, we investigated the physicochemical characteristics of flounder surimi (FS) and surimi gel (FSG). We analyzed the proximate composition, heavy metal content, and amino acid composition of FS and the gel strength and whiteness of FSG. In spontaneously hypertensive rats, the oral administration of FS significantly decreased systolic blood pressure. We further evaluated the antihypertensive activity of an FS digest (FSD) using an in vitro gastric model. FSD had significant ACE inhibitory activity and increased nitric oxide (NO) levels in human umbilical vein endothelial cells. We purified and identified three peptides from FSD by gel filtration chromatography and quadrupole time of flight electrospray ionization mass spectrometry. We predicted the tertiary structure of ACE for docking simulation. The bioactive peptides from FS showed successful binding to ACE (PDB ID: 1086) with negative binding energy and negative CDOCKER interaction energy in an in silica docking analysis. These results showed that FSD functions as an antihypertensive agent and FS could be a beneficial ingredient in the nutraceutical, pharmaceutical, and functional food industries. -
dc.description.uri 1 -
dc.language English -
dc.publisher ELSEVIER SCI LTD -
dc.title Antihypertensive effect of surimi prepared from olive flounder (Paralichthys olivaceus) by angiotensin-I converting enzyme (ACE) inhibitory activity and characterization of ACE inhibitory peptides -
dc.type Article -
dc.citation.endPage 170 -
dc.citation.startPage 164 -
dc.citation.title PROCESS BIOCHEMISTRY -
dc.citation.volume 80 -
dc.contributor.alternativeName 김은아 -
dc.identifier.bibliographicCitation PROCESS BIOCHEMISTRY, v.80, pp.164 - 170 -
dc.identifier.doi 10.1016/j.procbio.2019.01.016 -
dc.identifier.scopusid 2-s2.0-85061632585 -
dc.identifier.wosid 000466616800021 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.subject.keywordPlus FRAME PROTEIN -
dc.subject.keywordPlus NITRIC-OXIDE -
dc.subject.keywordPlus GEL PROPERTIES -
dc.subject.keywordPlus HYDROLYSATE -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus MUSCLE -
dc.subject.keywordPlus GROWTH -
dc.subject.keywordAuthor Antihypertensive -
dc.subject.keywordAuthor Olive flounder -
dc.subject.keywordAuthor Surimi -
dc.subject.keywordAuthor Angiotensin-I-converting enzyme -
dc.subject.keywordAuthor Peptide -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology -
dc.relation.journalWebOfScienceCategory Biotechnology & Applied Microbiology -
dc.relation.journalWebOfScienceCategory Engineering, Chemical -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Biochemistry & Molecular Biology -
dc.relation.journalResearchArea Biotechnology & Applied Microbiology -
dc.relation.journalResearchArea Engineering -
Appears in Collections:
Jeju Research Institute > Jeju Bio Research Center > 1. Journal Articles
Files in This Item:
There are no files associated with this item.

qrcode

Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse