Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni 2
Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish ( ) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated fr...
Gespeichert in:
| Veröffentlicht in: | Marine drugs 2017-02, Vol.15 (2) |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 2 |
| container_start_page | |
| container_title | Marine drugs |
| container_volume | 15 |
| creator | Sun, Lixia Wu, Shanguang Zhou, Liqin Wang, Feng Lan, Xiongdiao Sun, Jianhua Tong, Zhangfa Liao, Dankui |
| description | Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (
) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC
Ni
). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC
of 0.116 mg·mL
) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC
value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate. |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed</sourceid><recordid>TN_cdi_pubmed_primary_28212269</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>28212269</sourcerecordid><originalsourceid>FETCH-pubmed_primary_282122693</originalsourceid><addsrcrecordid>eNqFj81Kw0AUhQdBbP15BblLXQTSicZmGUKkWSiFui8T5ya9ktwJd6bC9Dl84Basa1eH83H44Fyo-SLP0yTLipeZuvb-K02z52XxdKVmeqkXWufFXP1scDJiAjkGwxaq3al9BhQ6_ELXQck9uYDsiaGByvE3SiDuoeZDHBEeyqp-hIZ31FJwEmGNUyCLHjpxI2zMXsgawMFxb4KBtZxsxB5W0YobojcBoY3QvJVV8k6gb9VlZwaPd-e8Ufev9Ue1SqZ9O6LdTkKjkbj9u5H9OzgCiQFUVA</addsrcrecordid><sourcetype>Index Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni 2</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>PubMed Central Open Access</source><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Sun, Lixia ; Wu, Shanguang ; Zhou, Liqin ; Wang, Feng ; Lan, Xiongdiao ; Sun, Jianhua ; Tong, Zhangfa ; Liao, Dankui</creator><creatorcontrib>Sun, Lixia ; Wu, Shanguang ; Zhou, Liqin ; Wang, Feng ; Lan, Xiongdiao ; Sun, Jianhua ; Tong, Zhangfa ; Liao, Dankui</creatorcontrib><description>Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (
) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC
Ni
). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC
of 0.116 mg·mL
) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC
value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate.</description><identifier>EISSN: 1660-3397</identifier><identifier>PMID: 28212269</identifier><language>eng</language><publisher>Switzerland</publisher><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry ; Angiotensin-Converting Enzyme Inhibitors - isolation & purification ; Animals ; Chemical Fractionation ; Chromatography, Affinity - methods ; Chromatography, Reverse-Phase ; Fish Proteins - chemistry ; Fish Proteins - isolation & purification ; Fishes ; Oligopeptides - isolation & purification ; Protein Hydrolysates - chemistry ; Ultrafiltration</subject><ispartof>Marine drugs, 2017-02, Vol.15 (2)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28212269$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sun, Lixia</creatorcontrib><creatorcontrib>Wu, Shanguang</creatorcontrib><creatorcontrib>Zhou, Liqin</creatorcontrib><creatorcontrib>Wang, Feng</creatorcontrib><creatorcontrib>Lan, Xiongdiao</creatorcontrib><creatorcontrib>Sun, Jianhua</creatorcontrib><creatorcontrib>Tong, Zhangfa</creatorcontrib><creatorcontrib>Liao, Dankui</creatorcontrib><title>Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni 2</title><title>Marine drugs</title><addtitle>Mar Drugs</addtitle><description>Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (
) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC
Ni
). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC
of 0.116 mg·mL
) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC
value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate.</description><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</subject><subject>Animals</subject><subject>Chemical Fractionation</subject><subject>Chromatography, Affinity - methods</subject><subject>Chromatography, Reverse-Phase</subject><subject>Fish Proteins - chemistry</subject><subject>Fish Proteins - isolation & purification</subject><subject>Fishes</subject><subject>Oligopeptides - isolation & purification</subject><subject>Protein Hydrolysates - chemistry</subject><subject>Ultrafiltration</subject><issn>1660-3397</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFj81Kw0AUhQdBbP15BblLXQTSicZmGUKkWSiFui8T5ya9ktwJd6bC9Dl84Basa1eH83H44Fyo-SLP0yTLipeZuvb-K02z52XxdKVmeqkXWufFXP1scDJiAjkGwxaq3al9BhQ6_ELXQck9uYDsiaGByvE3SiDuoeZDHBEeyqp-hIZ31FJwEmGNUyCLHjpxI2zMXsgawMFxb4KBtZxsxB5W0YobojcBoY3QvJVV8k6gb9VlZwaPd-e8Ufev9Ue1SqZ9O6LdTkKjkbj9u5H9OzgCiQFUVA</recordid><startdate>20170215</startdate><enddate>20170215</enddate><creator>Sun, Lixia</creator><creator>Wu, Shanguang</creator><creator>Zhou, Liqin</creator><creator>Wang, Feng</creator><creator>Lan, Xiongdiao</creator><creator>Sun, Jianhua</creator><creator>Tong, Zhangfa</creator><creator>Liao, Dankui</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20170215</creationdate><title>Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni 2</title><author>Sun, Lixia ; Wu, Shanguang ; Zhou, Liqin ; Wang, Feng ; Lan, Xiongdiao ; Sun, Jianhua ; Tong, Zhangfa ; Liao, Dankui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmed_primary_282122693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Angiotensin-Converting Enzyme Inhibitors - chemistry</topic><topic>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</topic><topic>Animals</topic><topic>Chemical Fractionation</topic><topic>Chromatography, Affinity - methods</topic><topic>Chromatography, Reverse-Phase</topic><topic>Fish Proteins - chemistry</topic><topic>Fish Proteins - isolation & purification</topic><topic>Fishes</topic><topic>Oligopeptides - isolation & purification</topic><topic>Protein Hydrolysates - chemistry</topic><topic>Ultrafiltration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sun, Lixia</creatorcontrib><creatorcontrib>Wu, Shanguang</creatorcontrib><creatorcontrib>Zhou, Liqin</creatorcontrib><creatorcontrib>Wang, Feng</creatorcontrib><creatorcontrib>Lan, Xiongdiao</creatorcontrib><creatorcontrib>Sun, Jianhua</creatorcontrib><creatorcontrib>Tong, Zhangfa</creatorcontrib><creatorcontrib>Liao, Dankui</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Marine drugs</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sun, Lixia</au><au>Wu, Shanguang</au><au>Zhou, Liqin</au><au>Wang, Feng</au><au>Lan, Xiongdiao</au><au>Sun, Jianhua</au><au>Tong, Zhangfa</au><au>Liao, Dankui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni 2</atitle><jtitle>Marine drugs</jtitle><addtitle>Mar Drugs</addtitle><date>2017-02-15</date><risdate>2017</risdate><volume>15</volume><issue>2</issue><eissn>1660-3397</eissn><abstract>Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (
) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC
Ni
). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC
of 0.116 mg·mL
) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC
value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate.</abstract><cop>Switzerland</cop><pmid>28212269</pmid></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 1660-3397 |
| ispartof | Marine drugs, 2017-02, Vol.15 (2) |
| issn | 1660-3397 |
| language | eng |
| recordid | cdi_pubmed_primary_28212269 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; PubMed Central Open Access; MDPI - Multidisciplinary Digital Publishing Institute; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals Chemical Fractionation Chromatography, Affinity - methods Chromatography, Reverse-Phase Fish Proteins - chemistry Fish Proteins - isolation & purification Fishes Oligopeptides - isolation & purification Protein Hydrolysates - chemistry Ultrafiltration |
| title | Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni 2 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T15%3A48%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Separation%20and%20Characterization%20of%20Angiotensin%20I%20Converting%20Enzyme%20(ACE)%20Inhibitory%20Peptides%20from%20Saurida%20elongata%20Proteins%20Hydrolysate%20by%20IMAC-Ni%202&rft.jtitle=Marine%20drugs&rft.au=Sun,%20Lixia&rft.date=2017-02-15&rft.volume=15&rft.issue=2&rft.eissn=1660-3397&rft_id=info:doi/&rft_dat=%3Cpubmed%3E28212269%3C/pubmed%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/28212269&rfr_iscdi=true |