Extraction of antioxidant and ACE inhibitory peptides from Thai traditional fermented shrimp pastes
•Thai fermented shrimp pastes exhibited antioxidant and ACE inhibitory activity.•IEX and SPE were used to fractionate the peptides.•Novel antioxidant peptides (Trp-Pro and Ser-Val) were identified.•Ser-Val was identified as a novel ACE inhibitory peptide. Antioxidant and angiotensin converting enzym...
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Veröffentlicht in: | Food chemistry 2015-06, Vol.176, p.441-447 |
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creator | Kleekayai, Thanyaporn Harnedy, Pádraigín A. O’Keeffe, Martina B. Poyarkov, Alexey A. CunhaNeves, Adriana Suntornsuk, Worapot FitzGerald, Richard J. |
description | •Thai fermented shrimp pastes exhibited antioxidant and ACE inhibitory activity.•IEX and SPE were used to fractionate the peptides.•Novel antioxidant peptides (Trp-Pro and Ser-Val) were identified.•Ser-Val was identified as a novel ACE inhibitory peptide.
Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were extracted and isolated from two different types of Thai traditional fermented shrimp pastes, Kapi Ta Dam (Kp-B6) and Kapi Ta Deang (Kp-R6). Compounds with masses less than 500Da were found to be predominantly presented in both extracts. Following fractionation with sequential anion exchange chromatography and solid phase extraction (C18 matrix), three dipeptides were identified. Ser-Val and Ile-Phe were shown to exhibit ACE inhibitory activity with IC50 values of 60.68±1.06 and 70.03±1.45μM, respectively. Trp-Pro was shown to have high 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) radical scavenging activity (EC50 17.52±0.46μM). These results indicate that Thai traditional fermented shrimp pastes are potential sources of bioactive peptides possessing ACE inhibitory and antioxidant activities. |
doi_str_mv | 10.1016/j.foodchem.2014.12.026 |
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Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were extracted and isolated from two different types of Thai traditional fermented shrimp pastes, Kapi Ta Dam (Kp-B6) and Kapi Ta Deang (Kp-R6). Compounds with masses less than 500Da were found to be predominantly presented in both extracts. Following fractionation with sequential anion exchange chromatography and solid phase extraction (C18 matrix), three dipeptides were identified. Ser-Val and Ile-Phe were shown to exhibit ACE inhibitory activity with IC50 values of 60.68±1.06 and 70.03±1.45μM, respectively. Trp-Pro was shown to have high 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) radical scavenging activity (EC50 17.52±0.46μM). These results indicate that Thai traditional fermented shrimp pastes are potential sources of bioactive peptides possessing ACE inhibitory and antioxidant activities.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2014.12.026</identifier><identifier>PMID: 25624254</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>ACE inhibitor ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Animals ; Antioxidant ; Antioxidants - chemistry ; Asian Continental Ancestry Group ; Biofunctional peptides ; Decapoda ; Fermentation ; Fermented shrimp paste ; Humans ; Penaeidae - drug effects ; Peptides - chemistry ; Peptidyl-Dipeptidase A ; Shellfish - analysis</subject><ispartof>Food chemistry, 2015-06, Vol.176, p.441-447</ispartof><rights>2014 Elsevier Ltd</rights><rights>Copyright © 2014 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-73b3f9a9574141a22c4965e62fb805004e421e952eaaef130a49f48f431627633</citedby><cites>FETCH-LOGICAL-c401t-73b3f9a9574141a22c4965e62fb805004e421e952eaaef130a49f48f431627633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2014.12.026$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25624254$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kleekayai, Thanyaporn</creatorcontrib><creatorcontrib>Harnedy, Pádraigín A.</creatorcontrib><creatorcontrib>O’Keeffe, Martina B.</creatorcontrib><creatorcontrib>Poyarkov, Alexey A.</creatorcontrib><creatorcontrib>CunhaNeves, Adriana</creatorcontrib><creatorcontrib>Suntornsuk, Worapot</creatorcontrib><creatorcontrib>FitzGerald, Richard J.</creatorcontrib><title>Extraction of antioxidant and ACE inhibitory peptides from Thai traditional fermented shrimp pastes</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Thai fermented shrimp pastes exhibited antioxidant and ACE inhibitory activity.•IEX and SPE were used to fractionate the peptides.•Novel antioxidant peptides (Trp-Pro and Ser-Val) were identified.•Ser-Val was identified as a novel ACE inhibitory peptide.
Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were extracted and isolated from two different types of Thai traditional fermented shrimp pastes, Kapi Ta Dam (Kp-B6) and Kapi Ta Deang (Kp-R6). Compounds with masses less than 500Da were found to be predominantly presented in both extracts. Following fractionation with sequential anion exchange chromatography and solid phase extraction (C18 matrix), three dipeptides were identified. Ser-Val and Ile-Phe were shown to exhibit ACE inhibitory activity with IC50 values of 60.68±1.06 and 70.03±1.45μM, respectively. Trp-Pro was shown to have high 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) radical scavenging activity (EC50 17.52±0.46μM). These results indicate that Thai traditional fermented shrimp pastes are potential sources of bioactive peptides possessing ACE inhibitory and antioxidant activities.</description><subject>ACE inhibitor</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Animals</subject><subject>Antioxidant</subject><subject>Antioxidants - chemistry</subject><subject>Asian Continental Ancestry Group</subject><subject>Biofunctional peptides</subject><subject>Decapoda</subject><subject>Fermentation</subject><subject>Fermented shrimp paste</subject><subject>Humans</subject><subject>Penaeidae - drug effects</subject><subject>Peptides - chemistry</subject><subject>Peptidyl-Dipeptidase A</subject><subject>Shellfish - analysis</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9vGyEQxVGUqnHSfoWIYy-7GVgWdm-NLPePFKmX9IwwDDKWd9kArpJvXywnvTanN4ffm6eZR8gtg5YBk3f71sfo7A6nlgMTLeMtcHlBVmxQXaNA8Uuygg6GZmBCXpHrnPcAUNnhI7niveSC92JF7Oa5JGNLiDONnpq5Ts_BVa2zo_frDQ3zLmxDiemFLriU4DBTn-JEH3cm0Op24WQ3B-oxTTgXdDTvUpgWuphcMH8iH7w5ZPz8qjfk97fN4_pH8_Dr-8_1_UNjBbDSqG7b-dGMvRJMMMO5FaPsUXK_HaAHECg4w7HnaAx61oERoxeDFx2TXMmuuyFfznuXFJ-OmIueQrZ4OJgZ4zFrJgcl1TCq8R1ozwUoIXlF5Rm1Keac0Oul3mbSi2agT13ovX7rQp-60Izr2kU13r5mHLcTun-2t-dX4OsZwPqUPwGTzjbgbNGFhLZoF8P_Mv4C1lmdnQ</recordid><startdate>20150601</startdate><enddate>20150601</enddate><creator>Kleekayai, Thanyaporn</creator><creator>Harnedy, Pádraigín A.</creator><creator>O’Keeffe, Martina B.</creator><creator>Poyarkov, Alexey A.</creator><creator>CunhaNeves, Adriana</creator><creator>Suntornsuk, Worapot</creator><creator>FitzGerald, Richard J.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>20150601</creationdate><title>Extraction of antioxidant and ACE inhibitory peptides from Thai traditional fermented shrimp pastes</title><author>Kleekayai, Thanyaporn ; Harnedy, Pádraigín A. ; O’Keeffe, Martina B. ; Poyarkov, Alexey A. ; CunhaNeves, Adriana ; Suntornsuk, Worapot ; FitzGerald, Richard J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-73b3f9a9574141a22c4965e62fb805004e421e952eaaef130a49f48f431627633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>ACE inhibitor</topic><topic>Angiotensin-Converting Enzyme Inhibitors - chemistry</topic><topic>Animals</topic><topic>Antioxidant</topic><topic>Antioxidants - chemistry</topic><topic>Asian Continental Ancestry Group</topic><topic>Biofunctional peptides</topic><topic>Decapoda</topic><topic>Fermentation</topic><topic>Fermented shrimp paste</topic><topic>Humans</topic><topic>Penaeidae - drug effects</topic><topic>Peptides - chemistry</topic><topic>Peptidyl-Dipeptidase A</topic><topic>Shellfish - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kleekayai, Thanyaporn</creatorcontrib><creatorcontrib>Harnedy, Pádraigín A.</creatorcontrib><creatorcontrib>O’Keeffe, Martina B.</creatorcontrib><creatorcontrib>Poyarkov, Alexey A.</creatorcontrib><creatorcontrib>CunhaNeves, Adriana</creatorcontrib><creatorcontrib>Suntornsuk, Worapot</creatorcontrib><creatorcontrib>FitzGerald, Richard J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kleekayai, Thanyaporn</au><au>Harnedy, Pádraigín A.</au><au>O’Keeffe, Martina B.</au><au>Poyarkov, Alexey A.</au><au>CunhaNeves, Adriana</au><au>Suntornsuk, Worapot</au><au>FitzGerald, Richard J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Extraction of antioxidant and ACE inhibitory peptides from Thai traditional fermented shrimp pastes</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2015-06-01</date><risdate>2015</risdate><volume>176</volume><spage>441</spage><epage>447</epage><pages>441-447</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•Thai fermented shrimp pastes exhibited antioxidant and ACE inhibitory activity.•IEX and SPE were used to fractionate the peptides.•Novel antioxidant peptides (Trp-Pro and Ser-Val) were identified.•Ser-Val was identified as a novel ACE inhibitory peptide.
Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were extracted and isolated from two different types of Thai traditional fermented shrimp pastes, Kapi Ta Dam (Kp-B6) and Kapi Ta Deang (Kp-R6). Compounds with masses less than 500Da were found to be predominantly presented in both extracts. Following fractionation with sequential anion exchange chromatography and solid phase extraction (C18 matrix), three dipeptides were identified. Ser-Val and Ile-Phe were shown to exhibit ACE inhibitory activity with IC50 values of 60.68±1.06 and 70.03±1.45μM, respectively. Trp-Pro was shown to have high 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) radical scavenging activity (EC50 17.52±0.46μM). These results indicate that Thai traditional fermented shrimp pastes are potential sources of bioactive peptides possessing ACE inhibitory and antioxidant activities.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>25624254</pmid><doi>10.1016/j.foodchem.2014.12.026</doi><tpages>7</tpages></addata></record> |
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subjects | ACE inhibitor Angiotensin-Converting Enzyme Inhibitors - chemistry Animals Antioxidant Antioxidants - chemistry Asian Continental Ancestry Group Biofunctional peptides Decapoda Fermentation Fermented shrimp paste Humans Penaeidae - drug effects Peptides - chemistry Peptidyl-Dipeptidase A Shellfish - analysis |
title | Extraction of antioxidant and ACE inhibitory peptides from Thai traditional fermented shrimp pastes |
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