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Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle
Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE)...
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| Published in: | Food research international 2012-11, Vol.49 (1), p.326-333 |
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| container_end_page | 333 |
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| container_start_page | 326 |
| container_title | Food research international |
| container_volume | 49 |
| creator | Gu, Rui-Zeng Liu, Wen-Ying Lin, Feng Jin, Zhen-Tao Chen, Liang Yi, Wei-Xue Lu, Jun Cai, Mu-Yi |
| description | Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. BSFP was then separated by reversed-phase high performance liquid chromatography. Five major fractions were collected and their 2,2′-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging and ACE inhibitory activities were assayed. Fractions 3–5 displaying higher activities were subjected to mass spectrometry to identify the active peptides. A total of 29 peptide sequences were identified, and 11 peptides were synthesized for further ABTS radical scavenging and ACE inhibitory activity analysis. Finally, one potent antioxidative peptide (Leu-Trp-Arg, 3.25±0.11mmol Trolox equivalents/g sample) and two novel potent ACE inhibitory peptides (Leu-Glu-Arg, IC50=45.62±2.40μM; Gly-Ala-Gly-Pro, IC50=253.07±6.66μM) were found. Their activities were approximately 6.9, 14.1 and 2.8 times higher than that of BSFP, respectively.
► We describe a practical way to utilize black-bone silky fowl muscle. ► One potent antioxidant peptide is identified from the hydrolysate. ► Two novel potent ACE inhibitory peptides are identified from the hydrolysate. |
| doi_str_mv | 10.1016/j.foodres.2012.07.009 |
| format | article |
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► We describe a practical way to utilize black-bone silky fowl muscle. ► One potent antioxidant peptide is identified from the hydrolysate. ► Two novel potent ACE inhibitory peptides are identified from the hydrolysate.</description><identifier>ISSN: 0963-9969</identifier><identifier>EISSN: 1873-7145</identifier><identifier>DOI: 10.1016/j.foodres.2012.07.009</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>ACE inhibitory activity ; Antioxidant activity ; Antioxidants ; Biological and medical sciences ; Black-bone silky fowl ; chickens ; Enzymatic hydrolysis ; Enzymes ; Equivalence ; Food industries ; Foods ; Fundamental and applied biological sciences. Psychology ; Gallus gallus ; Low-molecular-weight peptides ; mass spectrometry ; molecular weight ; Muscles ; oligopeptides ; papain ; Peptides ; peptidyl-dipeptidase A ; Radicals ; reversed-phase high performance liquid chromatography ; Scavenging ; subtilisin</subject><ispartof>Food research international, 2012-11, Vol.49 (1), p.326-333</ispartof><rights>2012 Elsevier Ltd</rights><rights>2014 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-6d130de1196d3b90b78ac60454d0624e2f0ad791f41d2b002c59da57031a625e3</citedby><cites>FETCH-LOGICAL-c429t-6d130de1196d3b90b78ac60454d0624e2f0ad791f41d2b002c59da57031a625e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,783,787,27936,27937</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26664617$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Gu, Rui-Zeng</creatorcontrib><creatorcontrib>Liu, Wen-Ying</creatorcontrib><creatorcontrib>Lin, Feng</creatorcontrib><creatorcontrib>Jin, Zhen-Tao</creatorcontrib><creatorcontrib>Chen, Liang</creatorcontrib><creatorcontrib>Yi, Wei-Xue</creatorcontrib><creatorcontrib>Lu, Jun</creatorcontrib><creatorcontrib>Cai, Mu-Yi</creatorcontrib><title>Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle</title><title>Food research international</title><description>Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. BSFP was then separated by reversed-phase high performance liquid chromatography. Five major fractions were collected and their 2,2′-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging and ACE inhibitory activities were assayed. Fractions 3–5 displaying higher activities were subjected to mass spectrometry to identify the active peptides. A total of 29 peptide sequences were identified, and 11 peptides were synthesized for further ABTS radical scavenging and ACE inhibitory activity analysis. Finally, one potent antioxidative peptide (Leu-Trp-Arg, 3.25±0.11mmol Trolox equivalents/g sample) and two novel potent ACE inhibitory peptides (Leu-Glu-Arg, IC50=45.62±2.40μM; Gly-Ala-Gly-Pro, IC50=253.07±6.66μM) were found. Their activities were approximately 6.9, 14.1 and 2.8 times higher than that of BSFP, respectively.
► We describe a practical way to utilize black-bone silky fowl muscle. ► One potent antioxidant peptide is identified from the hydrolysate. ► Two novel potent ACE inhibitory peptides are identified from the hydrolysate.</description><subject>ACE inhibitory activity</subject><subject>Antioxidant activity</subject><subject>Antioxidants</subject><subject>Biological and medical sciences</subject><subject>Black-bone silky fowl</subject><subject>chickens</subject><subject>Enzymatic hydrolysis</subject><subject>Enzymes</subject><subject>Equivalence</subject><subject>Food industries</subject><subject>Foods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gallus gallus</subject><subject>Low-molecular-weight peptides</subject><subject>mass spectrometry</subject><subject>molecular weight</subject><subject>Muscles</subject><subject>oligopeptides</subject><subject>papain</subject><subject>Peptides</subject><subject>peptidyl-dipeptidase A</subject><subject>Radicals</subject><subject>reversed-phase high performance liquid chromatography</subject><subject>Scavenging</subject><subject>subtilisin</subject><issn>0963-9969</issn><issn>1873-7145</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhiMEEsvCT0D4glQOCeN8OPUJlQpKpUocoGfLsSfLbB17sbMLy9_hj-JVVlx7sMYfz8y8nrcoXnOoOHDxfluNIdiIqaqB1xX0FYB8Uqz4Zd-UPW-7p8UKpGhKKYV8XrxIaQsAouvlqvh75WcKv8lqPzPtbV4bCjP6RJ7dlib4A8aZ_Iah_3OckJH_QQPNIR7ZLobd6RETCyMLjjb5vJvJ5guLkQ5o2RjDxAanzUM5BI8skXs4sjH8cuziRju3T2yzBBsmTDOZvP0YKaXg37Fpn4zDl8WzUbuEr85xXdx__vT9-kt59_Xm9vrqrjRtLedSWN6ARc6lsM0gYegvtRHQdq0FUbdYj6BtL_nYclsPALXppNVdDw3Xou6wWRcXS938sZ_7LEZNlAw6pz2GfVK8b4BzXjficbTjTStz1y6j3YKaGFKKOKpdpEnHo-KgTv6prTr7p07-KehV9i_nvT230MloN0btDaX_ybUQohVZ0rp4s3CjDkpv8ujU_bdcqDt5DHkymfiwEJiHdyCMKhlCb9BSRDMrG-gRLf8AmEvAMA</recordid><startdate>20121101</startdate><enddate>20121101</enddate><creator>Gu, Rui-Zeng</creator><creator>Liu, Wen-Ying</creator><creator>Lin, Feng</creator><creator>Jin, Zhen-Tao</creator><creator>Chen, Liang</creator><creator>Yi, Wei-Xue</creator><creator>Lu, Jun</creator><creator>Cai, Mu-Yi</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope></search><sort><creationdate>20121101</creationdate><title>Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle</title><author>Gu, Rui-Zeng ; Liu, Wen-Ying ; Lin, Feng ; Jin, Zhen-Tao ; Chen, Liang ; Yi, Wei-Xue ; Lu, Jun ; Cai, Mu-Yi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-6d130de1196d3b90b78ac60454d0624e2f0ad791f41d2b002c59da57031a625e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>ACE inhibitory activity</topic><topic>Antioxidant activity</topic><topic>Antioxidants</topic><topic>Biological and medical sciences</topic><topic>Black-bone silky fowl</topic><topic>chickens</topic><topic>Enzymatic hydrolysis</topic><topic>Enzymes</topic><topic>Equivalence</topic><topic>Food industries</topic><topic>Foods</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gallus gallus</topic><topic>Low-molecular-weight peptides</topic><topic>mass spectrometry</topic><topic>molecular weight</topic><topic>Muscles</topic><topic>oligopeptides</topic><topic>papain</topic><topic>Peptides</topic><topic>peptidyl-dipeptidase A</topic><topic>Radicals</topic><topic>reversed-phase high performance liquid chromatography</topic><topic>Scavenging</topic><topic>subtilisin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gu, Rui-Zeng</creatorcontrib><creatorcontrib>Liu, Wen-Ying</creatorcontrib><creatorcontrib>Lin, Feng</creatorcontrib><creatorcontrib>Jin, Zhen-Tao</creatorcontrib><creatorcontrib>Chen, Liang</creatorcontrib><creatorcontrib>Yi, Wei-Xue</creatorcontrib><creatorcontrib>Lu, Jun</creatorcontrib><creatorcontrib>Cai, Mu-Yi</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><jtitle>Food research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gu, Rui-Zeng</au><au>Liu, Wen-Ying</au><au>Lin, Feng</au><au>Jin, Zhen-Tao</au><au>Chen, Liang</au><au>Yi, Wei-Xue</au><au>Lu, Jun</au><au>Cai, Mu-Yi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle</atitle><jtitle>Food research international</jtitle><date>2012-11-01</date><risdate>2012</risdate><volume>49</volume><issue>1</issue><spage>326</spage><epage>333</epage><pages>326-333</pages><issn>0963-9969</issn><eissn>1873-7145</eissn><abstract>Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. BSFP was then separated by reversed-phase high performance liquid chromatography. Five major fractions were collected and their 2,2′-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging and ACE inhibitory activities were assayed. Fractions 3–5 displaying higher activities were subjected to mass spectrometry to identify the active peptides. A total of 29 peptide sequences were identified, and 11 peptides were synthesized for further ABTS radical scavenging and ACE inhibitory activity analysis. Finally, one potent antioxidative peptide (Leu-Trp-Arg, 3.25±0.11mmol Trolox equivalents/g sample) and two novel potent ACE inhibitory peptides (Leu-Glu-Arg, IC50=45.62±2.40μM; Gly-Ala-Gly-Pro, IC50=253.07±6.66μM) were found. Their activities were approximately 6.9, 14.1 and 2.8 times higher than that of BSFP, respectively.
► We describe a practical way to utilize black-bone silky fowl muscle. ► One potent antioxidant peptide is identified from the hydrolysate. ► Two novel potent ACE inhibitory peptides are identified from the hydrolysate.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><doi>10.1016/j.foodres.2012.07.009</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0963-9969 |
| ispartof | Food research international, 2012-11, Vol.49 (1), p.326-333 |
| issn | 0963-9969 1873-7145 |
| language | eng |
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| source | ScienceDirect Freedom Collection |
| subjects | ACE inhibitory activity Antioxidant activity Antioxidants Biological and medical sciences Black-bone silky fowl chickens Enzymatic hydrolysis Enzymes Equivalence Food industries Foods Fundamental and applied biological sciences. Psychology Gallus gallus Low-molecular-weight peptides mass spectrometry molecular weight Muscles oligopeptides papain Peptides peptidyl-dipeptidase A Radicals reversed-phase high performance liquid chromatography Scavenging subtilisin |
| title | Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle |
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