Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS/MS
Angiotensin I-converting enzyme (ACE) inhibitors derived from foods are valuable auxiliaries to agents such as captopril. Eight highly functional ACE inhibitory peptides from the mushroom, Agaricus bisporus, were identified by LC-MS/MS. Among these peptides, the most potent ACE inhibitory activity w...
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| Veröffentlicht in: | Food chemistry 2014-04, Vol.148, p.396-401 |
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| creator | CHING CHING LAU ABDULLAH, Noorlidah ADAWIYAH SURIZA SHUIB AMINUDIN, Norhaniza |
| description | Angiotensin I-converting enzyme (ACE) inhibitors derived from foods are valuable auxiliaries to agents such as captopril. Eight highly functional ACE inhibitory peptides from the mushroom, Agaricus bisporus, were identified by LC-MS/MS. Among these peptides, the most potent ACE inhibitory activity was exhibited by AHEPVK, RIGLF and PSSNK with IC₅₀ values of 63, 116 and 129 μM, respectively. These peptides exhibited high ACE inhibitory activity after gastrointestinal digestion. Lineweaver-Burk plots suggested that AHEPVK and RIGLF act as competitive inhibitors against ACE, whereas PSSNK acts as a non-competitive inhibitor. Mushrooms can be a good component of dietary supplement due to their readily available source and, in addition, they rarely cause food allergy. Compared to ACE inhibitory peptides isolated from other edible mushrooms, AHEPVK, RIGLF and PSSNK have lower IC₅₀ values. Therefore, these peptides may serve as an ideal ingredient in the production of antihypertensive supplements. |
| doi_str_mv | 10.1016/j.foodchem.2013.10.053 |
| format | Article |
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Lange) Imbach identified by LC-MS/MS</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>CHING CHING LAU ; ABDULLAH, Noorlidah ; ADAWIYAH SURIZA SHUIB ; AMINUDIN, Norhaniza</creator><creatorcontrib>CHING CHING LAU ; ABDULLAH, Noorlidah ; ADAWIYAH SURIZA SHUIB ; AMINUDIN, Norhaniza</creatorcontrib><description>Angiotensin I-converting enzyme (ACE) inhibitors derived from foods are valuable auxiliaries to agents such as captopril. Eight highly functional ACE inhibitory peptides from the mushroom, Agaricus bisporus, were identified by LC-MS/MS. Among these peptides, the most potent ACE inhibitory activity was exhibited by AHEPVK, RIGLF and PSSNK with IC₅₀ values of 63, 116 and 129 μM, respectively. These peptides exhibited high ACE inhibitory activity after gastrointestinal digestion. Lineweaver-Burk plots suggested that AHEPVK and RIGLF act as competitive inhibitors against ACE, whereas PSSNK acts as a non-competitive inhibitor. Mushrooms can be a good component of dietary supplement due to their readily available source and, in addition, they rarely cause food allergy. Compared to ACE inhibitory peptides isolated from other edible mushrooms, AHEPVK, RIGLF and PSSNK have lower IC₅₀ values. Therefore, these peptides may serve as an ideal ingredient in the production of antihypertensive supplements.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2013.10.053</identifier><identifier>PMID: 24262574</identifier><identifier>CODEN: FOCHDJ</identifier><language>eng</language><publisher>Kidlington: Elsevier</publisher><subject>Agaricus - chemistry ; Agaricus bisporus ; Amino Acid Sequence ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Angiotensin-Converting Enzyme Inhibitors - isolation & purification ; Biological and medical sciences ; Chromatography, Liquid ; Food toxicology ; Humans ; Medical sciences ; Molecular Sequence Data ; Peptide Mapping ; Peptides - chemistry ; Peptides - isolation & purification ; Peptidyl-Dipeptidase A - analysis ; Tandem Mass Spectrometry ; Toxicology</subject><ispartof>Food chemistry, 2014-04, Vol.148, p.396-401</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright © 2013 Elsevier Ltd. 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Lange) Imbach identified by LC-MS/MS</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>Angiotensin I-converting enzyme (ACE) inhibitors derived from foods are valuable auxiliaries to agents such as captopril. Eight highly functional ACE inhibitory peptides from the mushroom, Agaricus bisporus, were identified by LC-MS/MS. Among these peptides, the most potent ACE inhibitory activity was exhibited by AHEPVK, RIGLF and PSSNK with IC₅₀ values of 63, 116 and 129 μM, respectively. These peptides exhibited high ACE inhibitory activity after gastrointestinal digestion. Lineweaver-Burk plots suggested that AHEPVK and RIGLF act as competitive inhibitors against ACE, whereas PSSNK acts as a non-competitive inhibitor. Mushrooms can be a good component of dietary supplement due to their readily available source and, in addition, they rarely cause food allergy. Compared to ACE inhibitory peptides isolated from other edible mushrooms, AHEPVK, RIGLF and PSSNK have lower IC₅₀ values. Therefore, these peptides may serve as an ideal ingredient in the production of antihypertensive supplements.</description><subject>Agaricus - chemistry</subject><subject>Agaricus bisporus</subject><subject>Amino Acid Sequence</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Liquid</subject><subject>Food toxicology</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Peptide Mapping</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptidyl-Dipeptidase A - analysis</subject><subject>Tandem Mass Spectrometry</subject><subject>Toxicology</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtu1DAUhi0EotPCK1TeIJVFUt8SO8tq1MKgKSwK65EvJzOuEjvYyUjDa_DCWOoglmzOTZ_-_5yD0DUlNSW0vX2u-xidPcBYM0J5Gdak4a_QiirJK0kke41WhBNVKSraC3SZ8zMhpLDqLbpggrWskWKFfn-NRxiwDnsfZwjZB7ypbAxHSLMPewzh12kE7MPBGz_HdMITTLN3kLGD5I_gcJ_iiMF5MwAel3xIsfR3e528XTI2Pk8xleLmS31f421xgo94MxptD7johNn3vqiYE96uq8en28end-hNr4cM78_5Cv14uP--_lxtv33arO-21cSkmKvWGgYNuKaToFRHhBTWGkUa0RlugABw13asV-XYVrQdlYo3QASVnVOtcfwK3bzoTin-XCDPu9FnC8OgA8Ql72jDCJecU_V_VLRUKaEoL-j1GV3MCG43JT_qdNr9_XkBPpwBna0e-qSD9fkfV7ZkJfA_QneS9Q</recordid><startdate>20140401</startdate><enddate>20140401</enddate><creator>CHING CHING LAU</creator><creator>ABDULLAH, Noorlidah</creator><creator>ADAWIYAH SURIZA SHUIB</creator><creator>AMINUDIN, Norhaniza</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>M7N</scope></search><sort><creationdate>20140401</creationdate><title>Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS/MS</title><author>CHING CHING LAU ; ABDULLAH, Noorlidah ; ADAWIYAH SURIZA SHUIB ; AMINUDIN, Norhaniza</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p274t-6cb2e5ed597e8890474ccb80549b3be0ee3d692f8426646917835e04179d86bd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Agaricus - chemistry</topic><topic>Agaricus bisporus</topic><topic>Amino Acid Sequence</topic><topic>Angiotensin-Converting Enzyme Inhibitors - chemistry</topic><topic>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Liquid</topic><topic>Food toxicology</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Peptide Mapping</topic><topic>Peptides - chemistry</topic><topic>Peptides - isolation & purification</topic><topic>Peptidyl-Dipeptidase A - analysis</topic><topic>Tandem Mass Spectrometry</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CHING CHING LAU</creatorcontrib><creatorcontrib>ABDULLAH, Noorlidah</creatorcontrib><creatorcontrib>ADAWIYAH SURIZA SHUIB</creatorcontrib><creatorcontrib>AMINUDIN, Norhaniza</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CHING CHING LAU</au><au>ABDULLAH, Noorlidah</au><au>ADAWIYAH SURIZA SHUIB</au><au>AMINUDIN, Norhaniza</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. 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Mushrooms can be a good component of dietary supplement due to their readily available source and, in addition, they rarely cause food allergy. Compared to ACE inhibitory peptides isolated from other edible mushrooms, AHEPVK, RIGLF and PSSNK have lower IC₅₀ values. Therefore, these peptides may serve as an ideal ingredient in the production of antihypertensive supplements.</abstract><cop>Kidlington</cop><pub>Elsevier</pub><pmid>24262574</pmid><doi>10.1016/j.foodchem.2013.10.053</doi><tpages>6</tpages></addata></record> |
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| ispartof | Food chemistry, 2014-04, Vol.148, p.396-401 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Agaricus - chemistry Agaricus bisporus Amino Acid Sequence Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Biological and medical sciences Chromatography, Liquid Food toxicology Humans Medical sciences Molecular Sequence Data Peptide Mapping Peptides - chemistry Peptides - isolation & purification Peptidyl-Dipeptidase A - analysis Tandem Mass Spectrometry Toxicology |
| title | Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS/MS |
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