Erythrina Edulis (Pajuro) Seed Protein: A New Source of Antioxidant Peptides
Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutras...
Gespeichert in:
| Veröffentlicht in: | Natural product communications 2016-06, Vol.11 (6), p.781-786 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext bestellen |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 786 |
|---|---|
| container_issue | 6 |
| container_start_page | 781 |
| container_title | Natural product communications |
| container_volume | 11 |
| creator | Intiquilla, Arturo Jiménez-Aliaga, Karim Zavaleta, Amparo I. Arnao, Inés Peña, Carmen Chavez-Hidalgo, Elizabeth L. Hernández-Ledesma, Blanca |
| description | Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutrase®, Flavourzyme®, and Alcalase® were used to hydrolyze the protein concentrate at different times. By SDS-PAGE, the lower resistance of proteins to Alcalase® action was observed, providing hydrolyzates with higher radical scavenging activity. The 120 min-hydrolyzate showed ORAC and TEAC values of 2.51 and 0.91 μmol Trolox equivalents/mg of protein, respectively. A fraction lower than 3 kDa and rich in hydrophobic and aromatic amino acids was demonstrated to be mainly responsible for the observed activity. E. edulis could be a new alternative in the formulation of functional foods not only for its high protein content but also for the potential biological properties of its hydrolyzates. |
| doi_str_mv | 10.1177/1934578X1601100620 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_AFRWT</sourceid><recordid>TN_cdi_proquest_miscellaneous_1812883719</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sage_id>10.1177_1934578X1601100620</sage_id><sourcerecordid>1812883719</sourcerecordid><originalsourceid>FETCH-LOGICAL-c387t-3a7d31d288e7ff8d62972e32795969e60e3350811c7ed44e6857a4368a444c833</originalsourceid><addsrcrecordid>eNp9kE1LAzEQhoMottT-AQ-SYz2sTTbJJuutlPoBRQtV8LbEzaymbDc12UX7701p9SI4l5nD874wD0LnlFxRKuWY5owLqV5oRiglJEvJEepTIUSScymO4x2BZEf00DCEFYmjFCc8P0W9VArGKRV9NJ_5bfvubaPxzHS1DXi00KvOu0u8BDB44V0LtrnGE_wAn3jpOl8CdhWeNK11X9bopsUL2LTWQDhDJ5WuAwwPe4Ceb2ZP07tk_nh7P53Mk5Ip2SZMS8OoSZUCWVXKZGkuU2CpzEWe5ZARYEwQRWkpwXAOmRJSc5YpzTkvFWMDNNr3brz76CC0xdqGEupaN-C6UFBFYzmTUcEApXu09C4ED1Wx8Xat_bagpNiJLP6KjKGLQ3_3ugbzG_nRFoHxHgj6DYpVlNLEf_-r_AYpb3ha</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1812883719</pqid></control><display><type>article</type><title>Erythrina Edulis (Pajuro) Seed Protein: A New Source of Antioxidant Peptides</title><source>Sage Journals GOLD Open Access 2024</source><creator>Intiquilla, Arturo ; Jiménez-Aliaga, Karim ; Zavaleta, Amparo I. ; Arnao, Inés ; Peña, Carmen ; Chavez-Hidalgo, Elizabeth L. ; Hernández-Ledesma, Blanca</creator><creatorcontrib>Intiquilla, Arturo ; Jiménez-Aliaga, Karim ; Zavaleta, Amparo I. ; Arnao, Inés ; Peña, Carmen ; Chavez-Hidalgo, Elizabeth L. ; Hernández-Ledesma, Blanca</creatorcontrib><description>Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutrase®, Flavourzyme®, and Alcalase® were used to hydrolyze the protein concentrate at different times. By SDS-PAGE, the lower resistance of proteins to Alcalase® action was observed, providing hydrolyzates with higher radical scavenging activity. The 120 min-hydrolyzate showed ORAC and TEAC values of 2.51 and 0.91 μmol Trolox equivalents/mg of protein, respectively. A fraction lower than 3 kDa and rich in hydrophobic and aromatic amino acids was demonstrated to be mainly responsible for the observed activity. E. edulis could be a new alternative in the formulation of functional foods not only for its high protein content but also for the potential biological properties of its hydrolyzates.</description><identifier>ISSN: 1934-578X</identifier><identifier>EISSN: 1555-9475</identifier><identifier>DOI: 10.1177/1934578X1601100620</identifier><identifier>PMID: 27534115</identifier><language>eng</language><publisher>Los Angeles, CA: SAGE Publications</publisher><subject>Antioxidants - chemistry ; Erythrina - chemistry ; Kinetics ; Peptides - chemistry ; Plant Proteins - chemistry ; Seeds - chemistry</subject><ispartof>Natural product communications, 2016-06, Vol.11 (6), p.781-786</ispartof><rights>2016 SAGE Publications Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c387t-3a7d31d288e7ff8d62972e32795969e60e3350811c7ed44e6857a4368a444c833</citedby><cites>FETCH-LOGICAL-c387t-3a7d31d288e7ff8d62972e32795969e60e3350811c7ed44e6857a4368a444c833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://journals.sagepub.com/doi/pdf/10.1177/1934578X1601100620$$EPDF$$P50$$Gsage$$H</linktopdf><linktohtml>$$Uhttps://journals.sagepub.com/doi/10.1177/1934578X1601100620$$EHTML$$P50$$Gsage$$H</linktohtml><link.rule.ids>314,780,784,21966,27853,27924,27925,44945,45333</link.rule.ids><linktorsrc>$$Uhttps://journals.sagepub.com/doi/full/10.1177/1934578X1601100620?utm_source=summon&utm_medium=discovery-provider$$EView_record_in_SAGE_Publications$$FView_record_in_$$GSAGE_Publications</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27534115$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Intiquilla, Arturo</creatorcontrib><creatorcontrib>Jiménez-Aliaga, Karim</creatorcontrib><creatorcontrib>Zavaleta, Amparo I.</creatorcontrib><creatorcontrib>Arnao, Inés</creatorcontrib><creatorcontrib>Peña, Carmen</creatorcontrib><creatorcontrib>Chavez-Hidalgo, Elizabeth L.</creatorcontrib><creatorcontrib>Hernández-Ledesma, Blanca</creatorcontrib><title>Erythrina Edulis (Pajuro) Seed Protein: A New Source of Antioxidant Peptides</title><title>Natural product communications</title><addtitle>Nat Prod Commun</addtitle><description>Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutrase®, Flavourzyme®, and Alcalase® were used to hydrolyze the protein concentrate at different times. By SDS-PAGE, the lower resistance of proteins to Alcalase® action was observed, providing hydrolyzates with higher radical scavenging activity. The 120 min-hydrolyzate showed ORAC and TEAC values of 2.51 and 0.91 μmol Trolox equivalents/mg of protein, respectively. A fraction lower than 3 kDa and rich in hydrophobic and aromatic amino acids was demonstrated to be mainly responsible for the observed activity. E. edulis could be a new alternative in the formulation of functional foods not only for its high protein content but also for the potential biological properties of its hydrolyzates.</description><subject>Antioxidants - chemistry</subject><subject>Erythrina - chemistry</subject><subject>Kinetics</subject><subject>Peptides - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Seeds - chemistry</subject><issn>1934-578X</issn><issn>1555-9475</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMottT-AQ-SYz2sTTbJJuutlPoBRQtV8LbEzaymbDc12UX7701p9SI4l5nD874wD0LnlFxRKuWY5owLqV5oRiglJEvJEepTIUSScymO4x2BZEf00DCEFYmjFCc8P0W9VArGKRV9NJ_5bfvubaPxzHS1DXi00KvOu0u8BDB44V0LtrnGE_wAn3jpOl8CdhWeNK11X9bopsUL2LTWQDhDJ5WuAwwPe4Ceb2ZP07tk_nh7P53Mk5Ip2SZMS8OoSZUCWVXKZGkuU2CpzEWe5ZARYEwQRWkpwXAOmRJSc5YpzTkvFWMDNNr3brz76CC0xdqGEupaN-C6UFBFYzmTUcEApXu09C4ED1Wx8Xat_bagpNiJLP6KjKGLQ3_3ugbzG_nRFoHxHgj6DYpVlNLEf_-r_AYpb3ha</recordid><startdate>201606</startdate><enddate>201606</enddate><creator>Intiquilla, Arturo</creator><creator>Jiménez-Aliaga, Karim</creator><creator>Zavaleta, Amparo I.</creator><creator>Arnao, Inés</creator><creator>Peña, Carmen</creator><creator>Chavez-Hidalgo, Elizabeth L.</creator><creator>Hernández-Ledesma, Blanca</creator><general>SAGE Publications</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></search><sort><creationdate>201606</creationdate><title>Erythrina Edulis (Pajuro) Seed Protein: A New Source of Antioxidant Peptides</title><author>Intiquilla, Arturo ; Jiménez-Aliaga, Karim ; Zavaleta, Amparo I. ; Arnao, Inés ; Peña, Carmen ; Chavez-Hidalgo, Elizabeth L. ; Hernández-Ledesma, Blanca</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c387t-3a7d31d288e7ff8d62972e32795969e60e3350811c7ed44e6857a4368a444c833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Antioxidants - chemistry</topic><topic>Erythrina - chemistry</topic><topic>Kinetics</topic><topic>Peptides - chemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Seeds - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Intiquilla, Arturo</creatorcontrib><creatorcontrib>Jiménez-Aliaga, Karim</creatorcontrib><creatorcontrib>Zavaleta, Amparo I.</creatorcontrib><creatorcontrib>Arnao, Inés</creatorcontrib><creatorcontrib>Peña, Carmen</creatorcontrib><creatorcontrib>Chavez-Hidalgo, Elizabeth L.</creatorcontrib><creatorcontrib>Hernández-Ledesma, Blanca</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><jtitle>Natural product communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Intiquilla, Arturo</au><au>Jiménez-Aliaga, Karim</au><au>Zavaleta, Amparo I.</au><au>Arnao, Inés</au><au>Peña, Carmen</au><au>Chavez-Hidalgo, Elizabeth L.</au><au>Hernández-Ledesma, Blanca</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Erythrina Edulis (Pajuro) Seed Protein: A New Source of Antioxidant Peptides</atitle><jtitle>Natural product communications</jtitle><addtitle>Nat Prod Commun</addtitle><date>2016-06</date><risdate>2016</risdate><volume>11</volume><issue>6</issue><spage>781</spage><epage>786</epage><pages>781-786</pages><issn>1934-578X</issn><eissn>1555-9475</eissn><abstract>Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutrase®, Flavourzyme®, and Alcalase® were used to hydrolyze the protein concentrate at different times. By SDS-PAGE, the lower resistance of proteins to Alcalase® action was observed, providing hydrolyzates with higher radical scavenging activity. The 120 min-hydrolyzate showed ORAC and TEAC values of 2.51 and 0.91 μmol Trolox equivalents/mg of protein, respectively. A fraction lower than 3 kDa and rich in hydrophobic and aromatic amino acids was demonstrated to be mainly responsible for the observed activity. E. edulis could be a new alternative in the formulation of functional foods not only for its high protein content but also for the potential biological properties of its hydrolyzates.</abstract><cop>Los Angeles, CA</cop><pub>SAGE Publications</pub><pmid>27534115</pmid><doi>10.1177/1934578X1601100620</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext_linktorsrc |
| identifier | ISSN: 1934-578X |
| ispartof | Natural product communications, 2016-06, Vol.11 (6), p.781-786 |
| issn | 1934-578X 1555-9475 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1812883719 |
| source | Sage Journals GOLD Open Access 2024 |
| subjects | Antioxidants - chemistry Erythrina - chemistry Kinetics Peptides - chemistry Plant Proteins - chemistry Seeds - chemistry |
| title | Erythrina Edulis (Pajuro) Seed Protein: A New Source of Antioxidant Peptides |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T17%3A19%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_AFRWT&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Erythrina%20Edulis%20(Pajuro)%20Seed%20Protein:%20A%20New%20Source%20of%20Antioxidant%20Peptides&rft.jtitle=Natural%20product%20communications&rft.au=Intiquilla,%20Arturo&rft.date=2016-06&rft.volume=11&rft.issue=6&rft.spage=781&rft.epage=786&rft.pages=781-786&rft.issn=1934-578X&rft.eissn=1555-9475&rft_id=info:doi/10.1177/1934578X1601100620&rft_dat=%3Cproquest_AFRWT%3E1812883719%3C/proquest_AFRWT%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1812883719&rft_id=info:pmid/27534115&rft_sage_id=10.1177_1934578X1601100620&rfr_iscdi=true |