ACE-inhibitory activity of tilapia protein hydrolysates
Fish processing wastes can be used for preparing bioactive peptides with various functionalities. Our objective was to evaluate the in vitro angiotensin converting enzyme (ACE) inhibitory activity of tilapia protein hydrolysates and its corresponding fractionates. Tilapia protein was alkali-solubili...
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| Veröffentlicht in: | Food chemistry 2009-12, Vol.117 (4), p.582-588 |
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| container_title | Food chemistry |
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| creator | Raghavan, Sivakumar Kristinsson, Hordur G. |
| description | Fish processing wastes can be used for preparing bioactive peptides with various functionalities. Our objective was to evaluate the in vitro angiotensin converting enzyme (ACE) inhibitory activity of tilapia protein hydrolysates and its corresponding fractionates. Tilapia protein was alkali-solubilised at pH 11.0 and recovered at pH 5.5 to obtain a stable substrate. This substrate was hydrolysed using two enzymes, Cryotin-F or Flavourzyme, to 7.5% and 25% degree of hydrolysis (DH). The hydrolysates were ultra-filtered into three fractions: >30
kDa fraction, 10–30
kDa fraction, and |
| doi_str_mv | 10.1016/j.foodchem.2009.04.058 |
| format | Article |
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kDa fraction, 10–30
kDa fraction, and <10
kDa fractions. Both hydrolysates and fractionates were tested for ACE inhibition. Results showed that both Cryotin and Flavourzyme hydrolysates with 25% DH gave maximum ACE inhibitory activity. Low MW peptides showed higher ACE inhibition than high MW peptides. The inhibitory activity of fractionates was lower than that of the corresponding hydrolysates, possibly due to separation and removal of synergistic peptides by ultrafiltration. Amongst fractionates, all the 7.5% DH Cryotin fractions and 25% DH Flavourzyme fractions exhibited optimum % ACE inhibition. The results of this research could be used for optimising enzyme parameters to obtain peptides from tilapia with optimum in vitro ACE inhibitory activity.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2009.04.058</identifier><identifier>CODEN: FOCHDJ</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Angiotensin converting enzyme inhibition ; Biological and medical sciences ; Cryotin ; enzyme activity ; enzyme inhibition ; Flavourzyme ; Food industries ; food processing wastes ; fractionation ; Fundamental and applied biological sciences. Psychology ; peptidyl-dipeptidase A ; protein hydrolysates ; separation ; Tilapia ; tilapia (common name) ; Ultrafiltration</subject><ispartof>Food chemistry, 2009-12, Vol.117 (4), p.582-588</ispartof><rights>2009 Elsevier Ltd</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-43fa1736de2af613b2df4a22a6d8ea74b986fea626ce59e919594e1e7890dc453</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2009.04.058$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21748539$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Raghavan, Sivakumar</creatorcontrib><creatorcontrib>Kristinsson, Hordur G.</creatorcontrib><title>ACE-inhibitory activity of tilapia protein hydrolysates</title><title>Food chemistry</title><description>Fish processing wastes can be used for preparing bioactive peptides with various functionalities. Our objective was to evaluate the in vitro angiotensin converting enzyme (ACE) inhibitory activity of tilapia protein hydrolysates and its corresponding fractionates. Tilapia protein was alkali-solubilised at pH 11.0 and recovered at pH 5.5 to obtain a stable substrate. This substrate was hydrolysed using two enzymes, Cryotin-F or Flavourzyme, to 7.5% and 25% degree of hydrolysis (DH). The hydrolysates were ultra-filtered into three fractions: >30
kDa fraction, 10–30
kDa fraction, and <10
kDa fractions. Both hydrolysates and fractionates were tested for ACE inhibition. Results showed that both Cryotin and Flavourzyme hydrolysates with 25% DH gave maximum ACE inhibitory activity. Low MW peptides showed higher ACE inhibition than high MW peptides. The inhibitory activity of fractionates was lower than that of the corresponding hydrolysates, possibly due to separation and removal of synergistic peptides by ultrafiltration. Amongst fractionates, all the 7.5% DH Cryotin fractions and 25% DH Flavourzyme fractions exhibited optimum % ACE inhibition. The results of this research could be used for optimising enzyme parameters to obtain peptides from tilapia with optimum in vitro ACE inhibitory activity.</description><subject>Angiotensin converting enzyme inhibition</subject><subject>Biological and medical sciences</subject><subject>Cryotin</subject><subject>enzyme activity</subject><subject>enzyme inhibition</subject><subject>Flavourzyme</subject><subject>Food industries</subject><subject>food processing wastes</subject><subject>fractionation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>peptidyl-dipeptidase A</subject><subject>protein hydrolysates</subject><subject>separation</subject><subject>Tilapia</subject><subject>tilapia (common name)</subject><subject>Ultrafiltration</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFkE1P3DAURa2KSh0of6HNBnZJ_RXH3oFGQCshdVFYW2-c545HmXhqG6T8e4wGumX1Nufed3UI-cZoxyhTP3adj3F0W9x3nFLTUdnRXn8iK6YH0Q504CdkRQXVrWZSfSGnOe8opZwyvSLD9fqmDfM2bEKJaWnAlfAcytJE35QwwSFAc0ixYJib7TKmOC0ZCuav5LOHKeP52z0jj7c3D-uf7f3vu1_r6_vWSSVKK4UHNgg1IgevmNjw0UvgHNSoEQa5MVp5BMWVw96gYaY3EhkO2tDRyV6ckctjbx3x7wlzsfuQHU4TzBifsuVUmV4pUUF1BF2KOSf09pDCHtJiGbWvnuzOvnuyr54slbZ6qsGLtw-QHUw-wexC_p_mbJC6F6Zy34-ch2jhb6rM458qUdTunmutKnF1JLAKeQ6YbHYBZ4djSOiKHWP4aMwLoWuK3Q</recordid><startdate>20091215</startdate><enddate>20091215</enddate><creator>Raghavan, Sivakumar</creator><creator>Kristinsson, Hordur G.</creator><general>Elsevier Ltd</general><general>[Amsterdam]: Elsevier Science</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>20091215</creationdate><title>ACE-inhibitory activity of tilapia protein hydrolysates</title><author>Raghavan, Sivakumar ; Kristinsson, Hordur G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-43fa1736de2af613b2df4a22a6d8ea74b986fea626ce59e919594e1e7890dc453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Angiotensin converting enzyme inhibition</topic><topic>Biological and medical sciences</topic><topic>Cryotin</topic><topic>enzyme activity</topic><topic>enzyme inhibition</topic><topic>Flavourzyme</topic><topic>Food industries</topic><topic>food processing wastes</topic><topic>fractionation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>peptidyl-dipeptidase A</topic><topic>protein hydrolysates</topic><topic>separation</topic><topic>Tilapia</topic><topic>tilapia (common name)</topic><topic>Ultrafiltration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Raghavan, Sivakumar</creatorcontrib><creatorcontrib>Kristinsson, Hordur G.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</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>Raghavan, Sivakumar</au><au>Kristinsson, Hordur G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ACE-inhibitory activity of tilapia protein hydrolysates</atitle><jtitle>Food chemistry</jtitle><date>2009-12-15</date><risdate>2009</risdate><volume>117</volume><issue>4</issue><spage>582</spage><epage>588</epage><pages>582-588</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><coden>FOCHDJ</coden><abstract>Fish processing wastes can be used for preparing bioactive peptides with various functionalities. Our objective was to evaluate the in vitro angiotensin converting enzyme (ACE) inhibitory activity of tilapia protein hydrolysates and its corresponding fractionates. Tilapia protein was alkali-solubilised at pH 11.0 and recovered at pH 5.5 to obtain a stable substrate. This substrate was hydrolysed using two enzymes, Cryotin-F or Flavourzyme, to 7.5% and 25% degree of hydrolysis (DH). The hydrolysates were ultra-filtered into three fractions: >30
kDa fraction, 10–30
kDa fraction, and <10
kDa fractions. Both hydrolysates and fractionates were tested for ACE inhibition. Results showed that both Cryotin and Flavourzyme hydrolysates with 25% DH gave maximum ACE inhibitory activity. Low MW peptides showed higher ACE inhibition than high MW peptides. The inhibitory activity of fractionates was lower than that of the corresponding hydrolysates, possibly due to separation and removal of synergistic peptides by ultrafiltration. Amongst fractionates, all the 7.5% DH Cryotin fractions and 25% DH Flavourzyme fractions exhibited optimum % ACE inhibition. The results of this research could be used for optimising enzyme parameters to obtain peptides from tilapia with optimum in vitro ACE inhibitory activity.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><doi>10.1016/j.foodchem.2009.04.058</doi><tpages>7</tpages></addata></record> |
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| ispartof | Food chemistry, 2009-12, Vol.117 (4), p.582-588 |
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| language | eng |
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| source | ScienceDirect Journals (5 years ago - present) |
| subjects | Angiotensin converting enzyme inhibition Biological and medical sciences Cryotin enzyme activity enzyme inhibition Flavourzyme Food industries food processing wastes fractionation Fundamental and applied biological sciences. Psychology peptidyl-dipeptidase A protein hydrolysates separation Tilapia tilapia (common name) Ultrafiltration |
| title | ACE-inhibitory activity of tilapia protein hydrolysates |
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