Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake
The traditional method to obtain phycocolloids from seaweeds implies successive extraction steps with cold and hot water. The residual cake derived from phycocolloids obtaining process of red seaweed Porphyra columbina is a waste containing 27 % protein and 10.7-mg gallic acid equivalents (100 g)⁻¹....
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Veröffentlicht in: | Journal of applied phycology 2013-08, Vol.25 (4), p.1197-1206 |
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description | The traditional method to obtain phycocolloids from seaweeds implies successive extraction steps with cold and hot water. The residual cake derived from phycocolloids obtaining process of red seaweed Porphyra columbina is a waste containing 27 % protein and 10.7-mg gallic acid equivalents (100 g)⁻¹. Seaweeds contain functional proteins, and the enzymatic hydrolysis of these proteins has been shown to release bioactive peptides. The aims of this study were to extract bioactive peptides and polyphenols after enzymatic hydrolysis of the residual cake and to evaluate their ACE inhibitory and antioxidant capacities (TEAC, DPPH, and copper-chelating activity). Residual cake hydrolysate has low molecular weight peptides containing Asp, Glu, Ala, and Leu. Residual cake hydrolysate had higher protein solubility than residual cake. ACE inhibition (≈45 %) and radical scavenging activity (TEAC and DPPH inhibition) were attributed mainly to low molecular weight peptides (500 Da) and polyphenols compounds released during proteolysis. The 50 % inhibition protein concentration value (IC50) corresponded to residual cake hydrolysate was 1.01 ± 0.02 and 0.91 ± 0.01 g L⁻¹, for ABTS and DPPH, respectively. Also, residual cake hydrolysate had high copper-chelating activity (≈97.5 %). Hydrolysis could be used as a means to obtain ACE inhibitory and antioxidant compounds (peptides and polyphenols) from algae protein waste and add value to the phycocolloids extraction process. |
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The residual cake derived from phycocolloids obtaining process of red seaweed Porphyra columbina is a waste containing 27 % protein and 10.7-mg gallic acid equivalents (100 g)⁻¹. Seaweeds contain functional proteins, and the enzymatic hydrolysis of these proteins has been shown to release bioactive peptides. The aims of this study were to extract bioactive peptides and polyphenols after enzymatic hydrolysis of the residual cake and to evaluate their ACE inhibitory and antioxidant capacities (TEAC, DPPH, and copper-chelating activity). Residual cake hydrolysate has low molecular weight peptides containing Asp, Glu, Ala, and Leu. Residual cake hydrolysate had higher protein solubility than residual cake. ACE inhibition (≈45 %) and radical scavenging activity (TEAC and DPPH inhibition) were attributed mainly to low molecular weight peptides (500 Da) and polyphenols compounds released during proteolysis. The 50 % inhibition protein concentration value (IC50) corresponded to residual cake hydrolysate was 1.01 ± 0.02 and 0.91 ± 0.01 g L⁻¹, for ABTS and DPPH, respectively. Also, residual cake hydrolysate had high copper-chelating activity (≈97.5 %). Hydrolysis could be used as a means to obtain ACE inhibitory and antioxidant compounds (peptides and polyphenols) from algae protein waste and add value to the phycocolloids extraction process.</description><identifier>ISSN: 0921-8971</identifier><identifier>EISSN: 1573-5176</identifier><identifier>DOI: 10.1007/s10811-012-9913-2</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Algae ; antioxidant activity ; Antioxidants ; Biomedical and Life Sciences ; cold ; Copper ; Ecology ; enzymatic hydrolysis ; free radical scavengers ; Freshwater & Marine Ecology ; gallic acid ; Hydrolysis ; Life Sciences ; macroalgae ; molecular weight ; oilseed cakes ; Peptides ; Plant Physiology ; Plant Sciences ; polyphenols ; Porphyra ; Porphyra columbina ; protein solubility ; proteins ; proteolysis ; wastes</subject><ispartof>Journal of applied phycology, 2013-08, Vol.25 (4), p.1197-1206</ispartof><rights>Springer Science+Business Media Dordrecht 2012</rights><rights>Springer Science+Business Media Dordrecht 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-9bd5a4ac88b2cf88b6ba37e58a6b75a163f33d2abfe83e667bec130016daee763</citedby><cites>FETCH-LOGICAL-c397t-9bd5a4ac88b2cf88b6ba37e58a6b75a163f33d2abfe83e667bec130016daee763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10811-012-9913-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10811-012-9913-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Cian, Raúl E</creatorcontrib><creatorcontrib>Alaiz, Manuel</creatorcontrib><creatorcontrib>Vioque, Javier</creatorcontrib><creatorcontrib>Drago, Silvina R</creatorcontrib><title>Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake</title><title>Journal of applied phycology</title><addtitle>J Appl Phycol</addtitle><description>The traditional method to obtain phycocolloids from seaweeds implies successive extraction steps with cold and hot water. The residual cake derived from phycocolloids obtaining process of red seaweed Porphyra columbina is a waste containing 27 % protein and 10.7-mg gallic acid equivalents (100 g)⁻¹. Seaweeds contain functional proteins, and the enzymatic hydrolysis of these proteins has been shown to release bioactive peptides. The aims of this study were to extract bioactive peptides and polyphenols after enzymatic hydrolysis of the residual cake and to evaluate their ACE inhibitory and antioxidant capacities (TEAC, DPPH, and copper-chelating activity). Residual cake hydrolysate has low molecular weight peptides containing Asp, Glu, Ala, and Leu. Residual cake hydrolysate had higher protein solubility than residual cake. ACE inhibition (≈45 %) and radical scavenging activity (TEAC and DPPH inhibition) were attributed mainly to low molecular weight peptides (500 Da) and polyphenols compounds released during proteolysis. The 50 % inhibition protein concentration value (IC50) corresponded to residual cake hydrolysate was 1.01 ± 0.02 and 0.91 ± 0.01 g L⁻¹, for ABTS and DPPH, respectively. Also, residual cake hydrolysate had high copper-chelating activity (≈97.5 %). Hydrolysis could be used as a means to obtain ACE inhibitory and antioxidant compounds (peptides and polyphenols) from algae protein waste and add value to the phycocolloids extraction process.</description><subject>Algae</subject><subject>antioxidant activity</subject><subject>Antioxidants</subject><subject>Biomedical and Life Sciences</subject><subject>cold</subject><subject>Copper</subject><subject>Ecology</subject><subject>enzymatic hydrolysis</subject><subject>free radical scavengers</subject><subject>Freshwater & Marine Ecology</subject><subject>gallic acid</subject><subject>Hydrolysis</subject><subject>Life Sciences</subject><subject>macroalgae</subject><subject>molecular weight</subject><subject>oilseed cakes</subject><subject>Peptides</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>polyphenols</subject><subject>Porphyra</subject><subject>Porphyra columbina</subject><subject>protein solubility</subject><subject>proteins</subject><subject>proteolysis</subject><subject>wastes</subject><issn>0921-8971</issn><issn>1573-5176</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kcFu1TAQRSMEEo_CB7DCEpuyCMzYSZwsq6cHrVSplaBry3EmfS6JHexEavob_WFcwgKx6MKehc-5Gutm2XuEzwggv0SEGjEH5HnToMj5i2yHpRR5ibJ6me2g4ZjXjcTX2ZsY7wCgqbHeZY8H97COxKbgZ_LDGm1k5I7aGeoY3c9Bm9l6x3zPzvYHZt3Rtnb2YWXademkx3vbpcmMHye_uC6y04mm2XYU_zBTSp2O5PwQP7E--JFd-zAd16CTMixja51mgaLtFj0wo3_S2-xVr4dI7_7Ok-zm6-HH_jy_vPp2sT-7zI1o5Jw3bVfqQpu6brnp0121Wkgqa121stRYiV6Ijuu2p1pQVcmWDAoArDpNJCtxkp1uuenzvxaKsxptNDQM2pFfosKCS4CixCKhH_9D7_wSXNpOYSVBYFEDJgo3ygQfY6BeTcGOOqwKQT3VpLaaVKpJPdWkeHL45sTEulsK_yQ_I33YpF57pW-DjermOwcsUq-iEQjPEhxBovgNluSq4A</recordid><startdate>20130801</startdate><enddate>20130801</enddate><creator>Cian, Raúl E</creator><creator>Alaiz, Manuel</creator><creator>Vioque, Javier</creator><creator>Drago, Silvina R</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TN</scope><scope>7X2</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>GNUQQ</scope><scope>H95</scope><scope>HCIFZ</scope><scope>L.G</scope><scope>LK8</scope><scope>M0K</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope></search><sort><creationdate>20130801</creationdate><title>Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake</title><author>Cian, Raúl E ; Alaiz, Manuel ; Vioque, Javier ; Drago, Silvina R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-9bd5a4ac88b2cf88b6ba37e58a6b75a163f33d2abfe83e667bec130016daee763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Algae</topic><topic>antioxidant activity</topic><topic>Antioxidants</topic><topic>Biomedical and Life Sciences</topic><topic>cold</topic><topic>Copper</topic><topic>Ecology</topic><topic>enzymatic hydrolysis</topic><topic>free radical scavengers</topic><topic>Freshwater & Marine Ecology</topic><topic>gallic acid</topic><topic>Hydrolysis</topic><topic>Life Sciences</topic><topic>macroalgae</topic><topic>molecular weight</topic><topic>oilseed cakes</topic><topic>Peptides</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>polyphenols</topic><topic>Porphyra</topic><topic>Porphyra columbina</topic><topic>protein solubility</topic><topic>proteins</topic><topic>proteolysis</topic><topic>wastes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cian, Raúl E</creatorcontrib><creatorcontrib>Alaiz, Manuel</creatorcontrib><creatorcontrib>Vioque, Javier</creatorcontrib><creatorcontrib>Drago, Silvina R</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Oceanic Abstracts</collection><collection>Agricultural Science Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>ProQuest Central Student</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>SciTech Premium Collection</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><jtitle>Journal of applied phycology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cian, Raúl E</au><au>Alaiz, Manuel</au><au>Vioque, Javier</au><au>Drago, Silvina R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake</atitle><jtitle>Journal of applied phycology</jtitle><stitle>J Appl Phycol</stitle><date>2013-08-01</date><risdate>2013</risdate><volume>25</volume><issue>4</issue><spage>1197</spage><epage>1206</epage><pages>1197-1206</pages><issn>0921-8971</issn><eissn>1573-5176</eissn><abstract>The traditional method to obtain phycocolloids from seaweeds implies successive extraction steps with cold and hot water. The residual cake derived from phycocolloids obtaining process of red seaweed Porphyra columbina is a waste containing 27 % protein and 10.7-mg gallic acid equivalents (100 g)⁻¹. Seaweeds contain functional proteins, and the enzymatic hydrolysis of these proteins has been shown to release bioactive peptides. The aims of this study were to extract bioactive peptides and polyphenols after enzymatic hydrolysis of the residual cake and to evaluate their ACE inhibitory and antioxidant capacities (TEAC, DPPH, and copper-chelating activity). Residual cake hydrolysate has low molecular weight peptides containing Asp, Glu, Ala, and Leu. Residual cake hydrolysate had higher protein solubility than residual cake. ACE inhibition (≈45 %) and radical scavenging activity (TEAC and DPPH inhibition) were attributed mainly to low molecular weight peptides (500 Da) and polyphenols compounds released during proteolysis. The 50 % inhibition protein concentration value (IC50) corresponded to residual cake hydrolysate was 1.01 ± 0.02 and 0.91 ± 0.01 g L⁻¹, for ABTS and DPPH, respectively. Also, residual cake hydrolysate had high copper-chelating activity (≈97.5 %). Hydrolysis could be used as a means to obtain ACE inhibitory and antioxidant compounds (peptides and polyphenols) from algae protein waste and add value to the phycocolloids extraction process.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><doi>10.1007/s10811-012-9913-2</doi><tpages>10</tpages></addata></record> |
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subjects | Algae antioxidant activity Antioxidants Biomedical and Life Sciences cold Copper Ecology enzymatic hydrolysis free radical scavengers Freshwater & Marine Ecology gallic acid Hydrolysis Life Sciences macroalgae molecular weight oilseed cakes Peptides Plant Physiology Plant Sciences polyphenols Porphyra Porphyra columbina protein solubility proteins proteolysis wastes |
title | Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake |
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