Angiotensin I-Converting Enzyme Inhibitor Derived from Cross-Linked Oyster Protein
Following cross-linking by microbial transglutaminase, modified oyster proteins were hydrolyzed to improve inhibitory activity against angiotensin-converting enzyme (ACE) inhibitory activity with the use of a single protease, or a combination of six proteases. The oyster hydrolysate with the lowest...
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| description | Following cross-linking by microbial transglutaminase, modified oyster proteins were hydrolyzed to improve inhibitory activity against angiotensin-converting enzyme (ACE) inhibitory activity with the use of a single protease, or a combination of six proteases. The oyster hydrolysate with the lowest 50% ACE inhibitory concentration (IC50) of 0.40 mg/mL was obtained by two-step hydrolysis of the cross-linked oyster protein using Protamex and Neutrase. Five ACE inhibitory peptides were purified from the oyster hydrolysate using a multistep chromatographic procedure comprised of ion-exchange, size exclusion, and reversed-phase liquid chromatography. Their sequences were identified as TAY, VK, KY, FYN, and YA, using automated Edman degradation and mass spectrometry. These peptides were synthesized, and their IC50 values were measured to be 16.7, 29.0, 51.5, 68.2, and 93.9 μM, respectively. Toxicity of the peptides on the HepG2 cell line was not detected. The oyster hydrolysate also significantly decreased the systolic blood pressure of spontaneously hypertensive rats (SHR). The antihypertensive effect of the oyster hydrolysate on SHR was rapid and long-lasting, compared to commercially obtained sardine hydrolysate. These results suggest that the oyster hydrolysate could be a source of effective nutraceuticals against hypertension. |
| doi_str_mv | 10.1155/2014/379234 |
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The oyster hydrolysate with the lowest 50% ACE inhibitory concentration (IC50) of 0.40 mg/mL was obtained by two-step hydrolysis of the cross-linked oyster protein using Protamex and Neutrase. Five ACE inhibitory peptides were purified from the oyster hydrolysate using a multistep chromatographic procedure comprised of ion-exchange, size exclusion, and reversed-phase liquid chromatography. Their sequences were identified as TAY, VK, KY, FYN, and YA, using automated Edman degradation and mass spectrometry. These peptides were synthesized, and their IC50 values were measured to be 16.7, 29.0, 51.5, 68.2, and 93.9 μM, respectively. Toxicity of the peptides on the HepG2 cell line was not detected. The oyster hydrolysate also significantly decreased the systolic blood pressure of spontaneously hypertensive rats (SHR). The antihypertensive effect of the oyster hydrolysate on SHR was rapid and long-lasting, compared to commercially obtained sardine hydrolysate. These results suggest that the oyster hydrolysate could be a source of effective nutraceuticals against hypertension.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2014/379234</identifier><identifier>PMID: 25140307</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Puplishing Corporation</publisher><subject>ACE inhibitors ; Angiotensin-Converting Enzyme Inhibitors - administration & dosage ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Angiotensin-Converting Enzyme Inhibitors - isolation & purification ; Animals ; Biomedical research ; Blood pressure ; Blood Pressure - drug effects ; Chromatography ; Crassostrea ; Crosslinking ; Enzymes ; Food ; Functional foods & nutraceuticals ; Health aspects ; Hep G2 Cells ; Humans ; Hypertension ; Hypertension - drug therapy ; Hypertension - pathology ; Ostreidae - enzymology ; Oysters ; Peptides ; Peptides - administration & dosage ; Peptides - chemistry ; Peptides - isolation & purification ; Peptidyl-Dipeptidase A - metabolism ; Proteins ; Rats ; Sardinops ; Studies</subject><ispartof>BioMed research international, 2014-01, Vol.2014 (2014), p.1-9</ispartof><rights>Copyright © 2014 Cheng-Liang Xie et al.</rights><rights>COPYRIGHT 2014 John Wiley & Sons, Inc.</rights><rights>Copyright © 2014 Cheng-Liang Xie et al. Cheng-Liang Xie et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2014 Cheng-Liang Xie et al. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c527t-4b182efcd33705e3757f91bfba84a79e67d9002a1a4e11032e459e23251ffb7a3</citedby><cites>FETCH-LOGICAL-c527t-4b182efcd33705e3757f91bfba84a79e67d9002a1a4e11032e459e23251ffb7a3</cites><orcidid>0000-0002-5124-4991</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4130196/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4130196/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25140307$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Bandiera, Stelvio M.</contributor><creatorcontrib>Xie, Cheng-Liang</creatorcontrib><creatorcontrib>Kim, Jin-Soo</creatorcontrib><creatorcontrib>Ha, Jong-Myung</creatorcontrib><creatorcontrib>Choung, Se-Young</creatorcontrib><creatorcontrib>Choi, Yeung-Joon</creatorcontrib><title>Angiotensin I-Converting Enzyme Inhibitor Derived from Cross-Linked Oyster Protein</title><title>BioMed research international</title><addtitle>Biomed Res Int</addtitle><description>Following cross-linking by microbial transglutaminase, modified oyster proteins were hydrolyzed to improve inhibitory activity against angiotensin-converting enzyme (ACE) inhibitory activity with the use of a single protease, or a combination of six proteases. The oyster hydrolysate with the lowest 50% ACE inhibitory concentration (IC50) of 0.40 mg/mL was obtained by two-step hydrolysis of the cross-linked oyster protein using Protamex and Neutrase. Five ACE inhibitory peptides were purified from the oyster hydrolysate using a multistep chromatographic procedure comprised of ion-exchange, size exclusion, and reversed-phase liquid chromatography. Their sequences were identified as TAY, VK, KY, FYN, and YA, using automated Edman degradation and mass spectrometry. These peptides were synthesized, and their IC50 values were measured to be 16.7, 29.0, 51.5, 68.2, and 93.9 μM, respectively. Toxicity of the peptides on the HepG2 cell line was not detected. The oyster hydrolysate also significantly decreased the systolic blood pressure of spontaneously hypertensive rats (SHR). The antihypertensive effect of the oyster hydrolysate on SHR was rapid and long-lasting, compared to commercially obtained sardine hydrolysate. These results suggest that the oyster hydrolysate could be a source of effective nutraceuticals against hypertension.</description><subject>ACE inhibitors</subject><subject>Angiotensin-Converting Enzyme Inhibitors - administration & dosage</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</subject><subject>Animals</subject><subject>Biomedical research</subject><subject>Blood pressure</subject><subject>Blood Pressure - drug effects</subject><subject>Chromatography</subject><subject>Crassostrea</subject><subject>Crosslinking</subject><subject>Enzymes</subject><subject>Food</subject><subject>Functional foods & nutraceuticals</subject><subject>Health aspects</subject><subject>Hep G2 Cells</subject><subject>Humans</subject><subject>Hypertension</subject><subject>Hypertension - drug therapy</subject><subject>Hypertension - pathology</subject><subject>Ostreidae - enzymology</subject><subject>Oysters</subject><subject>Peptides</subject><subject>Peptides - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>BioMed research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xie, Cheng-Liang</au><au>Kim, Jin-Soo</au><au>Ha, Jong-Myung</au><au>Choung, Se-Young</au><au>Choi, Yeung-Joon</au><au>Bandiera, Stelvio M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Angiotensin I-Converting Enzyme Inhibitor Derived from Cross-Linked Oyster Protein</atitle><jtitle>BioMed research international</jtitle><addtitle>Biomed Res Int</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>2014</volume><issue>2014</issue><spage>1</spage><epage>9</epage><pages>1-9</pages><issn>2314-6133</issn><eissn>2314-6141</eissn><abstract>Following cross-linking by microbial transglutaminase, modified oyster proteins were hydrolyzed to improve inhibitory activity against angiotensin-converting enzyme (ACE) inhibitory activity with the use of a single protease, or a combination of six proteases. The oyster hydrolysate with the lowest 50% ACE inhibitory concentration (IC50) of 0.40 mg/mL was obtained by two-step hydrolysis of the cross-linked oyster protein using Protamex and Neutrase. Five ACE inhibitory peptides were purified from the oyster hydrolysate using a multistep chromatographic procedure comprised of ion-exchange, size exclusion, and reversed-phase liquid chromatography. Their sequences were identified as TAY, VK, KY, FYN, and YA, using automated Edman degradation and mass spectrometry. These peptides were synthesized, and their IC50 values were measured to be 16.7, 29.0, 51.5, 68.2, and 93.9 μM, respectively. Toxicity of the peptides on the HepG2 cell line was not detected. The oyster hydrolysate also significantly decreased the systolic blood pressure of spontaneously hypertensive rats (SHR). The antihypertensive effect of the oyster hydrolysate on SHR was rapid and long-lasting, compared to commercially obtained sardine hydrolysate. These results suggest that the oyster hydrolysate could be a source of effective nutraceuticals against hypertension.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Puplishing Corporation</pub><pmid>25140307</pmid><doi>10.1155/2014/379234</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-5124-4991</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | ACE inhibitors Angiotensin-Converting Enzyme Inhibitors - administration & dosage Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals Biomedical research Blood pressure Blood Pressure - drug effects Chromatography Crassostrea Crosslinking Enzymes Food Functional foods & nutraceuticals Health aspects Hep G2 Cells Humans Hypertension Hypertension - drug therapy Hypertension - pathology Ostreidae - enzymology Oysters Peptides Peptides - administration & dosage Peptides - chemistry Peptides - isolation & purification Peptidyl-Dipeptidase A - metabolism Proteins Rats Sardinops Studies |
| title | Angiotensin I-Converting Enzyme Inhibitor Derived from Cross-Linked Oyster Protein |
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