Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates
BACKGROUND: Enzymatic proteolysis of food proteins is used to produce peptide fractions with the potential to act as physiological modulators. Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food ingredients. The...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2010-11, Vol.90 (14), p.2512-2518 |
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| creator | Segura Campos, Maira R Chel Guerrero, Luis A Betancur Ancona, David A |
| description | BACKGROUND: Enzymatic proteolysis of food proteins is used to produce peptide fractions with the potential to act as physiological modulators. Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food ingredients. The present study investigated the angiotensin-I converting enzyme (ACE-I) inhibitory and antioxidant activities for hydrolysates produced by hydrolyzing Vigna unguiculata protein extract as well as ultrafiltered peptide fractions from these hydrolysates.RESULTS: Alcalase®, Flavourzyme® and pepsin-pancreatin were used to produce extensively hydrolyzed V. unguiculata protein extract. Degree of hydrolysis (DH) differed between the enzymatic systems and ranged from 35.7% to 58.8%. Fractionation increased in vitro biological activities in the peptide fractions, with IC₅₀ (hydrolysate concentration in μg protein mL⁻¹ required to produce 50% ACE inhibition) value ranges of 24.3-123 (Alcalase hydrolysate, AH), 0.04-170.6 (Flavourzyme hydrolysate; FH) and 44.7-112 (pepsin-pancreatin hydrolysate, PPH) μg mL⁻¹, and TEAC (Trolox equivalent antioxidant coefficient) value ranges of 303.2-1457 (AH), 357.4-10 211 (FH) and 267.1-2830.4 (PPH) mmol L⁻¹ mg⁻¹ protein.CONCLUSION: The results indicate the possibility of obtaining bioactive peptides from V. unguiculata proteins by means of a controlled protein hydrolysis using Alcalase®, Flavourzyme® and pepsin-pancreatin. The V. unguiculata protein hydrolysates and their corresponding ultrafiltered peptide fractions might be utilized for physiologically functional foods with antihypertensive and antioxidant activities. Copyright |
| doi_str_mv | 10.1002/jsfa.4114 |
| format | Article |
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Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food ingredients. The present study investigated the angiotensin-I converting enzyme (ACE-I) inhibitory and antioxidant activities for hydrolysates produced by hydrolyzing Vigna unguiculata protein extract as well as ultrafiltered peptide fractions from these hydrolysates.RESULTS: Alcalase®, Flavourzyme® and pepsin-pancreatin were used to produce extensively hydrolyzed V. unguiculata protein extract. Degree of hydrolysis (DH) differed between the enzymatic systems and ranged from 35.7% to 58.8%. Fractionation increased in vitro biological activities in the peptide fractions, with IC₅₀ (hydrolysate concentration in μg protein mL⁻¹ required to produce 50% ACE inhibition) value ranges of 24.3-123 (Alcalase hydrolysate, AH), 0.04-170.6 (Flavourzyme hydrolysate; FH) and 44.7-112 (pepsin-pancreatin hydrolysate, PPH) μg mL⁻¹, and TEAC (Trolox equivalent antioxidant coefficient) value ranges of 303.2-1457 (AH), 357.4-10 211 (FH) and 267.1-2830.4 (PPH) mmol L⁻¹ mg⁻¹ protein.CONCLUSION: The results indicate the possibility of obtaining bioactive peptides from V. unguiculata proteins by means of a controlled protein hydrolysis using Alcalase®, Flavourzyme® and pepsin-pancreatin. The V. unguiculata protein hydrolysates and their corresponding ultrafiltered peptide fractions might be utilized for physiologically functional foods with antihypertensive and antioxidant activities. Copyright</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.4114</identifier><identifier>PMID: 20690111</identifier><identifier>CODEN: JSFAAE</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>ACE inhibitors ; Angiotensin-Converting Enzyme Inhibitors - metabolism ; Angiotensin-Converting Enzyme Inhibitors - pharmacology ; antioxidant activity ; Antioxidants ; Biological and medical sciences ; cowpeas ; enzymatic hydrolysis ; enzyme inhibition ; enzyme inhibitors ; Enzymes ; Fabaceae - chemistry ; Food industries ; Functional foods & nutraceuticals ; Fundamental and applied biological sciences. Psychology ; Hydrolysis ; Inhibitory Concentration 50 ; pancreatin ; pepsin ; peptide fractions ; Peptide Hydrolases - metabolism ; Peptides ; Peptides - metabolism ; Peptides - pharmacology ; peptidyl-dipeptidase A ; Plant Extracts - metabolism ; Plant Extracts - pharmacology ; Plant Proteins - metabolism ; Plant Proteins - pharmacology ; protein hydrolysates ; Protein Hydrolysates - metabolism ; Protein Hydrolysates - pharmacology ; Proteins ; Studies ; Ultrafiltration ; Vigna unguiculata</subject><ispartof>Journal of the science of food and agriculture, 2010-11, Vol.90 (14), p.2512-2518</ispartof><rights>Copyright © 2010 Society of Chemical Industry</rights><rights>2015 INIST-CNRS</rights><rights>2010 Society of Chemical Industry</rights><rights>Copyright John Wiley and Sons, Limited Nov 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4434-7c7a39b455081ba6ca73e403006b75f178cd56028e70142ca87d8c699aa25d853</citedby><cites>FETCH-LOGICAL-c4434-7c7a39b455081ba6ca73e403006b75f178cd56028e70142ca87d8c699aa25d853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.4114$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.4114$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23324335$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20690111$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Segura Campos, Maira R</creatorcontrib><creatorcontrib>Chel Guerrero, Luis A</creatorcontrib><creatorcontrib>Betancur Ancona, David A</creatorcontrib><title>Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>BACKGROUND: Enzymatic proteolysis of food proteins is used to produce peptide fractions with the potential to act as physiological modulators. Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food ingredients. The present study investigated the angiotensin-I converting enzyme (ACE-I) inhibitory and antioxidant activities for hydrolysates produced by hydrolyzing Vigna unguiculata protein extract as well as ultrafiltered peptide fractions from these hydrolysates.RESULTS: Alcalase®, Flavourzyme® and pepsin-pancreatin were used to produce extensively hydrolyzed V. unguiculata protein extract. Degree of hydrolysis (DH) differed between the enzymatic systems and ranged from 35.7% to 58.8%. Fractionation increased in vitro biological activities in the peptide fractions, with IC₅₀ (hydrolysate concentration in μg protein mL⁻¹ required to produce 50% ACE inhibition) value ranges of 24.3-123 (Alcalase hydrolysate, AH), 0.04-170.6 (Flavourzyme hydrolysate; FH) and 44.7-112 (pepsin-pancreatin hydrolysate, PPH) μg mL⁻¹, and TEAC (Trolox equivalent antioxidant coefficient) value ranges of 303.2-1457 (AH), 357.4-10 211 (FH) and 267.1-2830.4 (PPH) mmol L⁻¹ mg⁻¹ protein.CONCLUSION: The results indicate the possibility of obtaining bioactive peptides from V. unguiculata proteins by means of a controlled protein hydrolysis using Alcalase®, Flavourzyme® and pepsin-pancreatin. The V. unguiculata protein hydrolysates and their corresponding ultrafiltered peptide fractions might be utilized for physiologically functional foods with antihypertensive and antioxidant activities. Copyright</description><subject>ACE inhibitors</subject><subject>Angiotensin-Converting Enzyme Inhibitors - metabolism</subject><subject>Angiotensin-Converting Enzyme Inhibitors - pharmacology</subject><subject>antioxidant activity</subject><subject>Antioxidants</subject><subject>Biological and medical sciences</subject><subject>cowpeas</subject><subject>enzymatic hydrolysis</subject><subject>enzyme inhibition</subject><subject>enzyme inhibitors</subject><subject>Enzymes</subject><subject>Fabaceae - chemistry</subject><subject>Food industries</subject><subject>Functional foods & nutraceuticals</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolysis</subject><subject>Inhibitory Concentration 50</subject><subject>pancreatin</subject><subject>pepsin</subject><subject>peptide fractions</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Peptides</subject><subject>Peptides - metabolism</subject><subject>Peptides - pharmacology</subject><subject>peptidyl-dipeptidase A</subject><subject>Plant Extracts - metabolism</subject><subject>Plant Extracts - pharmacology</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Proteins - pharmacology</subject><subject>protein hydrolysates</subject><subject>Protein Hydrolysates - metabolism</subject><subject>Protein Hydrolysates - pharmacology</subject><subject>Proteins</subject><subject>Studies</subject><subject>Ultrafiltration</subject><subject>Vigna unguiculata</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kstu1DAUhiMEokNhwQuAhYQQi7THcWwny6Ewpagqi15YWo7jTD1k7MF22glPw6PiaIYiIbGwjy_fufj8zrKXGI4wQHG8Cp08KjEuH2UzDDXPATA8zmbprsgpLouD7FkIKwCoa8aeZgcFsBowxrPs19wujYvaBmPzM6ScvdM-GrtE2v4c1xoZe2saE50fkbRtGtG4rWmTRVJFc2ei0QG5Dm30JppWo85P584GpLdxWusWNSMa-rTpzDRPt5OHcvcbLdGNWVqJBrscjBp6GSW6HVvv-jHIqMPz7Ekn-6Bf7O1hdr34dHXyOT__enp2Mj_PVVmSMueKS1I3JaVQ4UYyJTnRJRAA1nDaYV6pljIoKs0hNUTJireVYnUtZUHbipLD7N0u7sa7H4MOUaxNULrvpdVuCILTGhOgDCfyzT_kyg3epuImqMRFQVmC3u8g5V0IXndi481a-lFgEJNoYhJNTKIl9tU-4NCsdftA_lEpAW_3gAxK9qnDVpnwlyOkKAmZ3nC84-5Nr8f_ZxRfLhfzfep852FC1NsHD-m_C8YJp-Lbxamo6NXi5mP9QVwk_vWO76QTculTFdeXBaTO4Dp9OgbkN6UfybA</recordid><startdate>201011</startdate><enddate>201011</enddate><creator>Segura Campos, Maira R</creator><creator>Chel Guerrero, Luis A</creator><creator>Betancur Ancona, David A</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><general>John Wiley and Sons, Limited</general><scope>FBQ</scope><scope>BSCLL</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>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>201011</creationdate><title>Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates</title><author>Segura Campos, Maira R ; Chel Guerrero, Luis A ; Betancur Ancona, David A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4434-7c7a39b455081ba6ca73e403006b75f178cd56028e70142ca87d8c699aa25d853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>ACE inhibitors</topic><topic>Angiotensin-Converting Enzyme Inhibitors - metabolism</topic><topic>Angiotensin-Converting Enzyme Inhibitors - pharmacology</topic><topic>antioxidant activity</topic><topic>Antioxidants</topic><topic>Biological and medical sciences</topic><topic>cowpeas</topic><topic>enzymatic hydrolysis</topic><topic>enzyme inhibition</topic><topic>enzyme inhibitors</topic><topic>Enzymes</topic><topic>Fabaceae - chemistry</topic><topic>Food industries</topic><topic>Functional foods & nutraceuticals</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolysis</topic><topic>Inhibitory Concentration 50</topic><topic>pancreatin</topic><topic>pepsin</topic><topic>peptide fractions</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Peptides</topic><topic>Peptides - metabolism</topic><topic>Peptides - pharmacology</topic><topic>peptidyl-dipeptidase A</topic><topic>Plant Extracts - metabolism</topic><topic>Plant Extracts - pharmacology</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Proteins - pharmacology</topic><topic>protein hydrolysates</topic><topic>Protein Hydrolysates - metabolism</topic><topic>Protein Hydrolysates - pharmacology</topic><topic>Proteins</topic><topic>Studies</topic><topic>Ultrafiltration</topic><topic>Vigna unguiculata</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Segura Campos, Maira R</creatorcontrib><creatorcontrib>Chel Guerrero, Luis A</creatorcontrib><creatorcontrib>Betancur Ancona, David A</creatorcontrib><collection>AGRIS</collection><collection>Istex</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>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Segura Campos, Maira R</au><au>Chel Guerrero, Luis A</au><au>Betancur Ancona, David A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J. Sci. Food Agric</addtitle><date>2010-11</date><risdate>2010</risdate><volume>90</volume><issue>14</issue><spage>2512</spage><epage>2518</epage><pages>2512-2518</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><coden>JSFAAE</coden><abstract>BACKGROUND: Enzymatic proteolysis of food proteins is used to produce peptide fractions with the potential to act as physiological modulators. Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food ingredients. The present study investigated the angiotensin-I converting enzyme (ACE-I) inhibitory and antioxidant activities for hydrolysates produced by hydrolyzing Vigna unguiculata protein extract as well as ultrafiltered peptide fractions from these hydrolysates.RESULTS: Alcalase®, Flavourzyme® and pepsin-pancreatin were used to produce extensively hydrolyzed V. unguiculata protein extract. Degree of hydrolysis (DH) differed between the enzymatic systems and ranged from 35.7% to 58.8%. Fractionation increased in vitro biological activities in the peptide fractions, with IC₅₀ (hydrolysate concentration in μg protein mL⁻¹ required to produce 50% ACE inhibition) value ranges of 24.3-123 (Alcalase hydrolysate, AH), 0.04-170.6 (Flavourzyme hydrolysate; FH) and 44.7-112 (pepsin-pancreatin hydrolysate, PPH) μg mL⁻¹, and TEAC (Trolox equivalent antioxidant coefficient) value ranges of 303.2-1457 (AH), 357.4-10 211 (FH) and 267.1-2830.4 (PPH) mmol L⁻¹ mg⁻¹ protein.CONCLUSION: The results indicate the possibility of obtaining bioactive peptides from V. unguiculata proteins by means of a controlled protein hydrolysis using Alcalase®, Flavourzyme® and pepsin-pancreatin. The V. unguiculata protein hydrolysates and their corresponding ultrafiltered peptide fractions might be utilized for physiologically functional foods with antihypertensive and antioxidant activities. Copyright</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>20690111</pmid><doi>10.1002/jsfa.4114</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of the science of food and agriculture, 2010-11, Vol.90 (14), p.2512-2518 |
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| subjects | ACE inhibitors Angiotensin-Converting Enzyme Inhibitors - metabolism Angiotensin-Converting Enzyme Inhibitors - pharmacology antioxidant activity Antioxidants Biological and medical sciences cowpeas enzymatic hydrolysis enzyme inhibition enzyme inhibitors Enzymes Fabaceae - chemistry Food industries Functional foods & nutraceuticals Fundamental and applied biological sciences. Psychology Hydrolysis Inhibitory Concentration 50 pancreatin pepsin peptide fractions Peptide Hydrolases - metabolism Peptides Peptides - metabolism Peptides - pharmacology peptidyl-dipeptidase A Plant Extracts - metabolism Plant Extracts - pharmacology Plant Proteins - metabolism Plant Proteins - pharmacology protein hydrolysates Protein Hydrolysates - metabolism Protein Hydrolysates - pharmacology Proteins Studies Ultrafiltration Vigna unguiculata |
| title | Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates |
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