An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides
•Protein by-product can be valorize by enzymatic hydrolysis.•SWVE and DILN appeared essential for ACE inhibitory activity.•Peptides: SWV, SWVE and NSWVE are non-competitive inhibitors. The aim of this study was to (i) examine how enzymatic hydrolysis with a non-commercially available proteinase of f...
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| Veröffentlicht in: | Food chemistry 2014-05, Vol.151, p.500-505 |
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| creator | Pokora, M. Zambrowicz, A. Dąbrowska, A. Eckert, E. Setner, B. Szołtysik, M. Szewczuk, Z. Zabłocka, A. Polanowski, A. Trziszka, T. Chrzanowska, J. |
| description | •Protein by-product can be valorize by enzymatic hydrolysis.•SWVE and DILN appeared essential for ACE inhibitory activity.•Peptides: SWV, SWVE and NSWVE are non-competitive inhibitors.
The aim of this study was to (i) examine how enzymatic hydrolysis with a non-commercially available proteinase of fig-leaf gourd fruit (Cucurbita ficifolia) increased the use value of egg white protein preparations, generated as byproducts in the industrial process of lysozyme and cystatin isolation from egg white, and (ii) evaluate the inhibition of angiotensin I-converting enzyme (ACE) by the obtained hydrolysates. Purification procedures including membrane filtration, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) led to the production of several peptide fractions. Two novel ovalbumin-derived tetrapeptides: SWVE (f 148–151) and DILN (f 86–89) with ACE inhibitory activity were obtained. Study of their inhibitory kinetics revealed a non-competitive binding mode, with an IC50 value against ACE of 33.88 and 73.44μg for SWVE and DILN, respectively. Synthetic peptides which were designed on the basis of peptide SWVE were examined. A tripeptide sequence of SWV revealed the strongest ACE-inhibitory activity. |
| doi_str_mv | 10.1016/j.foodchem.2013.11.111 |
| format | Article |
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The aim of this study was to (i) examine how enzymatic hydrolysis with a non-commercially available proteinase of fig-leaf gourd fruit (Cucurbita ficifolia) increased the use value of egg white protein preparations, generated as byproducts in the industrial process of lysozyme and cystatin isolation from egg white, and (ii) evaluate the inhibition of angiotensin I-converting enzyme (ACE) by the obtained hydrolysates. Purification procedures including membrane filtration, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) led to the production of several peptide fractions. Two novel ovalbumin-derived tetrapeptides: SWVE (f 148–151) and DILN (f 86–89) with ACE inhibitory activity were obtained. Study of their inhibitory kinetics revealed a non-competitive binding mode, with an IC50 value against ACE of 33.88 and 73.44μg for SWVE and DILN, respectively. Synthetic peptides which were designed on the basis of peptide SWVE were examined. A tripeptide sequence of SWV revealed the strongest ACE-inhibitory activity.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2013.11.111</identifier><identifier>PMID: 24423562</identifier><identifier>CODEN: FOCHDJ</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Angiotensin I-converting enzyme inhibitory activity ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Antihypertensive Agents - therapeutic use ; Bioactive peptides ; Biological and medical sciences ; Cucurbita ficifolia ; egg albumen ; Egg Proteins - chemistry ; enzymatic hydrolysis ; filtration ; Food toxicology ; hydrolysates ; Hydrolysis ; industrial byproducts ; Medical sciences ; Peptides - chemistry ; peptidyl-dipeptidase A ; Protein by-product ; Proteinase of Cucurbita ficifolia ; proteinases ; reversed-phase high performance liquid chromatography ; size exclusion chromatography ; synthetic peptides ; Toxicology</subject><ispartof>Food chemistry, 2014-05, Vol.151, p.500-505</ispartof><rights>2013 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2013 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-57ebc524fa225f2b17ead2ff9d3772ba6d4526f507de5b78144627cbe99d7b673</citedby><cites>FETCH-LOGICAL-c422t-57ebc524fa225f2b17ead2ff9d3772ba6d4526f507de5b78144627cbe99d7b673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0308814613017998$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28376641$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24423562$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pokora, M.</creatorcontrib><creatorcontrib>Zambrowicz, A.</creatorcontrib><creatorcontrib>Dąbrowska, A.</creatorcontrib><creatorcontrib>Eckert, E.</creatorcontrib><creatorcontrib>Setner, B.</creatorcontrib><creatorcontrib>Szołtysik, M.</creatorcontrib><creatorcontrib>Szewczuk, Z.</creatorcontrib><creatorcontrib>Zabłocka, A.</creatorcontrib><creatorcontrib>Polanowski, A.</creatorcontrib><creatorcontrib>Trziszka, T.</creatorcontrib><creatorcontrib>Chrzanowska, J.</creatorcontrib><title>An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Protein by-product can be valorize by enzymatic hydrolysis.•SWVE and DILN appeared essential for ACE inhibitory activity.•Peptides: SWV, SWVE and NSWVE are non-competitive inhibitors.
The aim of this study was to (i) examine how enzymatic hydrolysis with a non-commercially available proteinase of fig-leaf gourd fruit (Cucurbita ficifolia) increased the use value of egg white protein preparations, generated as byproducts in the industrial process of lysozyme and cystatin isolation from egg white, and (ii) evaluate the inhibition of angiotensin I-converting enzyme (ACE) by the obtained hydrolysates. Purification procedures including membrane filtration, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) led to the production of several peptide fractions. Two novel ovalbumin-derived tetrapeptides: SWVE (f 148–151) and DILN (f 86–89) with ACE inhibitory activity were obtained. Study of their inhibitory kinetics revealed a non-competitive binding mode, with an IC50 value against ACE of 33.88 and 73.44μg for SWVE and DILN, respectively. Synthetic peptides which were designed on the basis of peptide SWVE were examined. A tripeptide sequence of SWV revealed the strongest ACE-inhibitory activity.</description><subject>Angiotensin I-converting enzyme inhibitory activity</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Antihypertensive Agents - therapeutic use</subject><subject>Bioactive peptides</subject><subject>Biological and medical sciences</subject><subject>Cucurbita ficifolia</subject><subject>egg albumen</subject><subject>Egg Proteins - chemistry</subject><subject>enzymatic hydrolysis</subject><subject>filtration</subject><subject>Food toxicology</subject><subject>hydrolysates</subject><subject>Hydrolysis</subject><subject>industrial byproducts</subject><subject>Medical sciences</subject><subject>Peptides - chemistry</subject><subject>peptidyl-dipeptidase A</subject><subject>Protein by-product</subject><subject>Proteinase of Cucurbita ficifolia</subject><subject>proteinases</subject><subject>reversed-phase high performance liquid chromatography</subject><subject>size exclusion chromatography</subject><subject>synthetic peptides</subject><subject>Toxicology</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE9v3CAQxVHVqtmm_Qopl0q9eAsYg31rFKV_pEg9tDkjDIOXlde4wG60375Y3rTHSoMYpN97MzyEbijZUkLFp_3WhWDNDg5bRmi9pbQUfYE2tJV1JYlkL9GG1KStWsrFFXqT0p4QUtj2NbpinLO6EWyDhtsJ65yjNtmfAD_pMw4OwzDgp53PgOcYMvgJ9-eqtPZoMj4mwC5EvL79NCyKKZxgxHrKvtqdZ4gZprQYzjBnbyG9Ra-cHhO8u9zX6PHL_a-7b9XDj6_f724fKsMZy1UjoTcN404z1jjWUwnaMuc6W0vJei0sb5hwDZEWml6Wv3HBpOmh66zshayv0cfVt2z3-wgpq4NPBsZRTxCOSVHeEdG1vBYFFStqYkgpglNz9Acdz4oStYSs9uo5ZLWErCgtRYvw5jLj2B_A_pU9p1qADxdAJ6NHF_VkfPrHtbUUgi9G71fO6aD0EAvz-LNMakg5vOu6QnxeCSiZnTxElYyHyYD1EUxWNvj_bfsHQV-ocA</recordid><startdate>20140515</startdate><enddate>20140515</enddate><creator>Pokora, M.</creator><creator>Zambrowicz, A.</creator><creator>Dąbrowska, A.</creator><creator>Eckert, E.</creator><creator>Setner, B.</creator><creator>Szołtysik, M.</creator><creator>Szewczuk, Z.</creator><creator>Zabłocka, A.</creator><creator>Polanowski, A.</creator><creator>Trziszka, T.</creator><creator>Chrzanowska, J.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><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></search><sort><creationdate>20140515</creationdate><title>An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides</title><author>Pokora, M. ; Zambrowicz, A. ; Dąbrowska, A. ; Eckert, E. ; Setner, B. ; Szołtysik, M. ; Szewczuk, Z. ; Zabłocka, A. ; Polanowski, A. ; Trziszka, T. ; Chrzanowska, J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-57ebc524fa225f2b17ead2ff9d3772ba6d4526f507de5b78144627cbe99d7b673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Angiotensin I-converting enzyme inhibitory activity</topic><topic>Angiotensin-Converting Enzyme Inhibitors - chemistry</topic><topic>Antihypertensive Agents - therapeutic use</topic><topic>Bioactive peptides</topic><topic>Biological and medical sciences</topic><topic>Cucurbita ficifolia</topic><topic>egg albumen</topic><topic>Egg Proteins - chemistry</topic><topic>enzymatic hydrolysis</topic><topic>filtration</topic><topic>Food toxicology</topic><topic>hydrolysates</topic><topic>Hydrolysis</topic><topic>industrial byproducts</topic><topic>Medical sciences</topic><topic>Peptides - chemistry</topic><topic>peptidyl-dipeptidase A</topic><topic>Protein by-product</topic><topic>Proteinase of Cucurbita ficifolia</topic><topic>proteinases</topic><topic>reversed-phase high performance liquid chromatography</topic><topic>size exclusion chromatography</topic><topic>synthetic peptides</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pokora, M.</creatorcontrib><creatorcontrib>Zambrowicz, A.</creatorcontrib><creatorcontrib>Dąbrowska, A.</creatorcontrib><creatorcontrib>Eckert, E.</creatorcontrib><creatorcontrib>Setner, B.</creatorcontrib><creatorcontrib>Szołtysik, M.</creatorcontrib><creatorcontrib>Szewczuk, Z.</creatorcontrib><creatorcontrib>Zabłocka, A.</creatorcontrib><creatorcontrib>Polanowski, A.</creatorcontrib><creatorcontrib>Trziszka, T.</creatorcontrib><creatorcontrib>Chrzanowska, J.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pokora, M.</au><au>Zambrowicz, A.</au><au>Dąbrowska, A.</au><au>Eckert, E.</au><au>Setner, B.</au><au>Szołtysik, M.</au><au>Szewczuk, Z.</au><au>Zabłocka, A.</au><au>Polanowski, A.</au><au>Trziszka, T.</au><au>Chrzanowska, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2014-05-15</date><risdate>2014</risdate><volume>151</volume><spage>500</spage><epage>505</epage><pages>500-505</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><coden>FOCHDJ</coden><abstract>•Protein by-product can be valorize by enzymatic hydrolysis.•SWVE and DILN appeared essential for ACE inhibitory activity.•Peptides: SWV, SWVE and NSWVE are non-competitive inhibitors.
The aim of this study was to (i) examine how enzymatic hydrolysis with a non-commercially available proteinase of fig-leaf gourd fruit (Cucurbita ficifolia) increased the use value of egg white protein preparations, generated as byproducts in the industrial process of lysozyme and cystatin isolation from egg white, and (ii) evaluate the inhibition of angiotensin I-converting enzyme (ACE) by the obtained hydrolysates. Purification procedures including membrane filtration, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) led to the production of several peptide fractions. Two novel ovalbumin-derived tetrapeptides: SWVE (f 148–151) and DILN (f 86–89) with ACE inhibitory activity were obtained. Study of their inhibitory kinetics revealed a non-competitive binding mode, with an IC50 value against ACE of 33.88 and 73.44μg for SWVE and DILN, respectively. Synthetic peptides which were designed on the basis of peptide SWVE were examined. A tripeptide sequence of SWV revealed the strongest ACE-inhibitory activity.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>24423562</pmid><doi>10.1016/j.foodchem.2013.11.111</doi><tpages>6</tpages></addata></record> |
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| subjects | Angiotensin I-converting enzyme inhibitory activity Angiotensin-Converting Enzyme Inhibitors - chemistry Antihypertensive Agents - therapeutic use Bioactive peptides Biological and medical sciences Cucurbita ficifolia egg albumen Egg Proteins - chemistry enzymatic hydrolysis filtration Food toxicology hydrolysates Hydrolysis industrial byproducts Medical sciences Peptides - chemistry peptidyl-dipeptidase A Protein by-product Proteinase of Cucurbita ficifolia proteinases reversed-phase high performance liquid chromatography size exclusion chromatography synthetic peptides Toxicology |
| title | An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides |
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