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Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology
Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of discards, which might...
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Published in: | Marine drugs 2017-10, Vol.15 (10), p.306 |
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description | Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of
discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of
and temperature on the hydrolysis of the
muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The
optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex. |
doi_str_mv | 10.3390/md15100306 |
format | article |
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discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of
and temperature on the hydrolysis of the
muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The
optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.</description><identifier>ISSN: 1660-3397</identifier><identifier>EISSN: 1660-3397</identifier><identifier>DOI: 10.3390/md15100306</identifier><identifier>PMID: 28994711</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Angiotensin ; Angiotensin-Converting Enzyme Inhibitors - metabolism ; Angiotensin-Converting Enzyme Inhibitors - pharmacology ; Animals ; antihypertensive activity ; Antihypertensive Agents - metabolism ; Antihypertensive Agents - pharmacology ; Antihypertensives ; antioxidant activity ; Antioxidants ; Antioxidants - metabolism ; Antioxidants - pharmacology ; Bioactive compounds ; Biological activity ; Biomass ; By products ; Common Fishery Policy ; Discards ; Drugs ; Elasmobranchii - metabolism ; enzyme hydrolysis ; Enzymes ; Enzymolysis ; Fish ; fish discards ; fish protein hydrolysates ; Fisheries ; Fishing ; Gillnets ; Hydrogen-Ion Concentration ; Hydrolysates ; Hydrolysis ; Industrial fisheries ; Lipids ; Longline fishing ; Optimization ; Peptide Hydrolases - metabolism ; Peptides ; Peptidyl-dipeptidase A ; pH effects ; Policies ; Protein Hydrolysates - metabolism ; Protein Hydrolysates - pharmacology ; Proteins ; Response surface methodology ; Scyliorhinus canicula ; Scyliorhinus canicula muscle by-products ; Subtilisin ; Temperature ; Viability ; Waste Products</subject><ispartof>Marine drugs, 2017-10, Vol.15 (10), p.306</ispartof><rights>Copyright MDPI AG 2017</rights><rights>2017 by the authors. 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-12babde7d4842bb8b36681e170e336641528271cf7bb5f529df06122de806a13</citedby><cites>FETCH-LOGICAL-c472t-12babde7d4842bb8b36681e170e336641528271cf7bb5f529df06122de806a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1965593462/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1965593462?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25751,27922,27923,37010,37011,44588,53789,53791,74896</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28994711$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vázquez, José A</creatorcontrib><creatorcontrib>Blanco, Maria</creatorcontrib><creatorcontrib>Massa, Agueda E</creatorcontrib><creatorcontrib>Amado, Isabel Rodríguez</creatorcontrib><creatorcontrib>Pérez-Martín, Ricardo I</creatorcontrib><title>Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology</title><title>Marine drugs</title><addtitle>Mar Drugs</addtitle><description>Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of
discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of
and temperature on the hydrolysis of the
muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The
optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.</description><subject>Angiotensin</subject><subject>Angiotensin-Converting Enzyme Inhibitors - metabolism</subject><subject>Angiotensin-Converting Enzyme Inhibitors - pharmacology</subject><subject>Animals</subject><subject>antihypertensive activity</subject><subject>Antihypertensive Agents - metabolism</subject><subject>Antihypertensive Agents - pharmacology</subject><subject>Antihypertensives</subject><subject>antioxidant activity</subject><subject>Antioxidants</subject><subject>Antioxidants - metabolism</subject><subject>Antioxidants - pharmacology</subject><subject>Bioactive compounds</subject><subject>Biological activity</subject><subject>Biomass</subject><subject>By products</subject><subject>Common Fishery Policy</subject><subject>Discards</subject><subject>Drugs</subject><subject>Elasmobranchii - metabolism</subject><subject>enzyme hydrolysis</subject><subject>Enzymes</subject><subject>Enzymolysis</subject><subject>Fish</subject><subject>fish discards</subject><subject>fish protein hydrolysates</subject><subject>Fisheries</subject><subject>Fishing</subject><subject>Gillnets</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysates</subject><subject>Hydrolysis</subject><subject>Industrial fisheries</subject><subject>Lipids</subject><subject>Longline fishing</subject><subject>Optimization</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Peptides</subject><subject>Peptidyl-dipeptidase A</subject><subject>pH effects</subject><subject>Policies</subject><subject>Protein Hydrolysates - metabolism</subject><subject>Protein Hydrolysates - pharmacology</subject><subject>Proteins</subject><subject>Response surface methodology</subject><subject>Scyliorhinus canicula</subject><subject>Scyliorhinus canicula muscle by-products</subject><subject>Subtilisin</subject><subject>Temperature</subject><subject>Viability</subject><subject>Waste Products</subject><issn>1660-3397</issn><issn>1660-3397</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdks1u1DAUhSMEoqWw4QGQJTao0oB_EifZII1KSyu1KqJlHfnnZuJRYg-2MzR9T94Hz0wZWla2zv187rF9s-wtwR8Zq_GnQZOCYMwwf5YdEs7xLMnl80f7g-xVCMuEFFWdv8wOaFXXeUnIYfb7m3d6VNE4i1yLzkzoUJIiGIvOJ-1dPwURIaDWuwHdqKk3znfGjgEpYY0ae4G-mKCE1wH9MrFDcxtNN63AR7DBrAEJq7eiuzNa2IjmqdvaRJNM5YRO7f00iGjUvp0J2yNXInawrYgeXa-iGcy92Ob8EYxdoO8QVs4GQDejb4UCdAWxc9r1bjG9zl60og_w5mE9ym7PTm9PzmeX118vTuaXM5WXNM4IlUJqKHVe5VTKSjLOKwKkxMDSNicFrWhJVFtKWbQFrXWLOaFUQ4W5IOwou9jZaieWzcqbQfipccI0W8H5RSN8ukAPDeCaKszalhGVC8pkBUqQSkmuFZeqSF6fd16rUQ6gFdjoRf_E9GnFmq5ZuHVT8E3SPBl8eDDw7ucIITZD-hfoe2HBjaEhdV7zOmfFBn3_H7p0o7fppRLFi6JmOaeJOt5RyrsQPLT7MAQ3m8Fr_g1egt89jr9H_04a-wMm39q8</recordid><startdate>20171010</startdate><enddate>20171010</enddate><creator>Vázquez, José A</creator><creator>Blanco, Maria</creator><creator>Massa, Agueda E</creator><creator>Amado, Isabel Rodríguez</creator><creator>Pérez-Martín, Ricardo I</creator><general>MDPI AG</general><general>MDPI</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>3V.</scope><scope>7T7</scope><scope>7TN</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H95</scope><scope>H99</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.F</scope><scope>L.G</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PCBAR</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20171010</creationdate><title>Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology</title><author>Vázquez, José A ; Blanco, Maria ; Massa, Agueda E ; Amado, Isabel Rodríguez ; Pérez-Martín, Ricardo I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c472t-12babde7d4842bb8b36681e170e336641528271cf7bb5f529df06122de806a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Angiotensin</topic><topic>Angiotensin-Converting Enzyme Inhibitors - metabolism</topic><topic>Angiotensin-Converting Enzyme Inhibitors - pharmacology</topic><topic>Animals</topic><topic>antihypertensive activity</topic><topic>Antihypertensive Agents - metabolism</topic><topic>Antihypertensive Agents - pharmacology</topic><topic>Antihypertensives</topic><topic>antioxidant activity</topic><topic>Antioxidants</topic><topic>Antioxidants - metabolism</topic><topic>Antioxidants - pharmacology</topic><topic>Bioactive compounds</topic><topic>Biological activity</topic><topic>Biomass</topic><topic>By products</topic><topic>Common Fishery Policy</topic><topic>Discards</topic><topic>Drugs</topic><topic>Elasmobranchii - metabolism</topic><topic>enzyme hydrolysis</topic><topic>Enzymes</topic><topic>Enzymolysis</topic><topic>Fish</topic><topic>fish discards</topic><topic>fish protein hydrolysates</topic><topic>Fisheries</topic><topic>Fishing</topic><topic>Gillnets</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysates</topic><topic>Hydrolysis</topic><topic>Industrial fisheries</topic><topic>Lipids</topic><topic>Longline fishing</topic><topic>Optimization</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Peptides</topic><topic>Peptidyl-dipeptidase A</topic><topic>pH effects</topic><topic>Policies</topic><topic>Protein Hydrolysates - metabolism</topic><topic>Protein Hydrolysates - pharmacology</topic><topic>Proteins</topic><topic>Response surface methodology</topic><topic>Scyliorhinus canicula</topic><topic>Scyliorhinus canicula muscle by-products</topic><topic>Subtilisin</topic><topic>Temperature</topic><topic>Viability</topic><topic>Waste Products</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vázquez, José A</creatorcontrib><creatorcontrib>Blanco, Maria</creatorcontrib><creatorcontrib>Massa, Agueda E</creatorcontrib><creatorcontrib>Amado, Isabel Rodríguez</creatorcontrib><creatorcontrib>Pérez-Martín, Ricardo I</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Oceanic Abstracts</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Marine drugs</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vázquez, José A</au><au>Blanco, Maria</au><au>Massa, Agueda E</au><au>Amado, Isabel Rodríguez</au><au>Pérez-Martín, Ricardo I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology</atitle><jtitle>Marine drugs</jtitle><addtitle>Mar Drugs</addtitle><date>2017-10-10</date><risdate>2017</risdate><volume>15</volume><issue>10</issue><spage>306</spage><pages>306-</pages><issn>1660-3397</issn><eissn>1660-3397</eissn><abstract>Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of
discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of
and temperature on the hydrolysis of the
muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The
optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>28994711</pmid><doi>10.3390/md15100306</doi><oa>free_for_read</oa></addata></record> |
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subjects | Angiotensin Angiotensin-Converting Enzyme Inhibitors - metabolism Angiotensin-Converting Enzyme Inhibitors - pharmacology Animals antihypertensive activity Antihypertensive Agents - metabolism Antihypertensive Agents - pharmacology Antihypertensives antioxidant activity Antioxidants Antioxidants - metabolism Antioxidants - pharmacology Bioactive compounds Biological activity Biomass By products Common Fishery Policy Discards Drugs Elasmobranchii - metabolism enzyme hydrolysis Enzymes Enzymolysis Fish fish discards fish protein hydrolysates Fisheries Fishing Gillnets Hydrogen-Ion Concentration Hydrolysates Hydrolysis Industrial fisheries Lipids Longline fishing Optimization Peptide Hydrolases - metabolism Peptides Peptidyl-dipeptidase A pH effects Policies Protein Hydrolysates - metabolism Protein Hydrolysates - pharmacology Proteins Response surface methodology Scyliorhinus canicula Scyliorhinus canicula muscle by-products Subtilisin Temperature Viability Waste Products |
title | Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology |
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