Isolation and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten
Wheat gluten was hydrolyzed with both alkaline protease and neutral protease to produce high-protein and low-wheat-weight oligopeptides (WOP), which was subjected to a multistage purification. Then, high performance liquid chromatography was applied to separate WOP. In order to identify WOP sequence...
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| Veröffentlicht in: | Journal of food science and technology 2021-09, Vol.58 (9), p.3504-3513 |
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| creator | Liu, Wen-Ying Miyakawa, Takuya Lu, Jun Hsieh, Yun Hua Gu, Ruizeng Miyauchi, Yumiko Katsuno, Kana Cai, Mu-Yi Tanokura, Masaru |
| description | Wheat gluten was hydrolyzed with both alkaline protease and neutral protease to produce high-protein and low-wheat-weight oligopeptides (WOP), which was subjected to a multistage purification. Then, high performance liquid chromatography was applied to separate WOP. In order to identify WOP sequences, six major fractions were gathered for mass spectrometry. A total of 15 peptides were synthesized for further in vitro analyses of their antithrombotic activity, vasorelaxation activity, and cholesterol reducing activity. Two antithrombotic peptides (ILPR and ILR), three vasorelaxant peptides (VN, FPQ, and FR), and four cholesterol-lowering peptides (QRQ, ILPR, FPQ, and ILR) were identified. These active peptides in WOP were also quantified. These peptides are novel candidate peptides with vascular disease suppressing effects. The results indicate WOP as good protein sources for multifunctional peptides. |
| doi_str_mv | 10.1007/s13197-021-05040-5 |
| format | Article |
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Then, high performance liquid chromatography was applied to separate WOP. In order to identify WOP sequences, six major fractions were gathered for mass spectrometry. A total of 15 peptides were synthesized for further in vitro analyses of their antithrombotic activity, vasorelaxation activity, and cholesterol reducing activity. Two antithrombotic peptides (ILPR and ILR), three vasorelaxant peptides (VN, FPQ, and FR), and four cholesterol-lowering peptides (QRQ, ILPR, FPQ, and ILR) were identified. These active peptides in WOP were also quantified. These peptides are novel candidate peptides with vascular disease suppressing effects. The results indicate WOP as good protein sources for multifunctional peptides.</description><identifier>ISSN: 0022-1155</identifier><identifier>EISSN: 0975-8402</identifier><identifier>DOI: 10.1007/s13197-021-05040-5</identifier><identifier>PMID: 34366467</identifier><language>eng</language><publisher>New Delhi: Springer India</publisher><subject>Alkaline protease ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Cholesterol ; Food Science ; Gluten ; High performance liquid chromatography ; Liquid chromatography ; Mass spectrometry ; Mass spectroscopy ; Nutrition ; Oligopeptides ; Original ; Original Article ; Peptides ; Protease ; Protein purification ; Protein sources ; Proteins ; Sequences ; Vascular diseases ; Vasodilation ; Wheat</subject><ispartof>Journal of food science and technology, 2021-09, Vol.58 (9), p.3504-3513</ispartof><rights>Association of Food Scientists & Technologists (India) 2021</rights><rights>Association of Food Scientists & Technologists (India) 2021.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-38404df59729255395d88cb10a55288303218a567d159259f04a3d18a1a949ae3</citedby><cites>FETCH-LOGICAL-c474t-38404df59729255395d88cb10a55288303218a567d159259f04a3d18a1a949ae3</cites><orcidid>0000-0001-8369-0809</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/PMC8292472/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8292472/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,41464,42533,51294,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34366467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Wen-Ying</creatorcontrib><creatorcontrib>Miyakawa, Takuya</creatorcontrib><creatorcontrib>Lu, Jun</creatorcontrib><creatorcontrib>Hsieh, Yun Hua</creatorcontrib><creatorcontrib>Gu, Ruizeng</creatorcontrib><creatorcontrib>Miyauchi, Yumiko</creatorcontrib><creatorcontrib>Katsuno, Kana</creatorcontrib><creatorcontrib>Cai, Mu-Yi</creatorcontrib><creatorcontrib>Tanokura, Masaru</creatorcontrib><title>Isolation and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten</title><title>Journal of food science and technology</title><addtitle>J Food Sci Technol</addtitle><addtitle>J Food Sci Technol</addtitle><description>Wheat gluten was hydrolyzed with both alkaline protease and neutral protease to produce high-protein and low-wheat-weight oligopeptides (WOP), which was subjected to a multistage purification. Then, high performance liquid chromatography was applied to separate WOP. In order to identify WOP sequences, six major fractions were gathered for mass spectrometry. A total of 15 peptides were synthesized for further in vitro analyses of their antithrombotic activity, vasorelaxation activity, and cholesterol reducing activity. Two antithrombotic peptides (ILPR and ILR), three vasorelaxant peptides (VN, FPQ, and FR), and four cholesterol-lowering peptides (QRQ, ILPR, FPQ, and ILR) were identified. These active peptides in WOP were also quantified. These peptides are novel candidate peptides with vascular disease suppressing effects. The results indicate WOP as good protein sources for multifunctional peptides.</description><subject>Alkaline protease</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Cholesterol</subject><subject>Food Science</subject><subject>Gluten</subject><subject>High performance liquid chromatography</subject><subject>Liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Nutrition</subject><subject>Oligopeptides</subject><subject>Original</subject><subject>Original Article</subject><subject>Peptides</subject><subject>Protease</subject><subject>Protein purification</subject><subject>Protein sources</subject><subject>Proteins</subject><subject>Sequences</subject><subject>Vascular diseases</subject><subject>Vasodilation</subject><subject>Wheat</subject><issn>0022-1155</issn><issn>0975-8402</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kUtr3TAQhUVpaEKSP9BFEXTTjVs9LWtTKKGPQKCbdC0Ua3yvgq_lauQb0l9f3TpNH4toIzH65swcDiEvOXvLGTPvkEtuTcMEb5hmijX6GTlh1uimU0w8r28mRMO51sfkHPGW1SOF6QR7QY6lkm2rWnNC8BLT6EtME_VToP3WZ98XyPHHWkwDTWPcpBnmEgMgvYtlS_ce-2X0mYaI4BEoLvOcAfHQAsMAfUEaqsoeAh1y2tG7LfhCN-NSYDojR4MfEc4f7lPy7dPH64svzdXXz5cXH66aXhlVGlmNqDBoa4QVWkurQ9f1N5x5rUXXyWqHd163JnBdATsw5WWoJe6tsh7kKXm_6s7LzQ5CD1PJfnRzjjuf713y0f37M8Wt26S96-pAZUQVePMgkNP3BbC4XcQextFPkBZ0dSvbGi35AX39H3qbljxVewdKSlsVWaXESvU5IWYYHpfhzB1idWusrsbqfsXqdG169beNx5bfIVZArgDWr2kD-c_sJ2R_AuN0ruk</recordid><startdate>20210901</startdate><enddate>20210901</enddate><creator>Liu, Wen-Ying</creator><creator>Miyakawa, Takuya</creator><creator>Lu, Jun</creator><creator>Hsieh, Yun Hua</creator><creator>Gu, 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and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten</title><author>Liu, Wen-Ying ; Miyakawa, Takuya ; Lu, Jun ; Hsieh, Yun Hua ; Gu, Ruizeng ; Miyauchi, Yumiko ; Katsuno, Kana ; Cai, Mu-Yi ; Tanokura, Masaru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-38404df59729255395d88cb10a55288303218a567d159259f04a3d18a1a949ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Alkaline protease</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Cholesterol</topic><topic>Food Science</topic><topic>Gluten</topic><topic>High performance liquid chromatography</topic><topic>Liquid chromatography</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Nutrition</topic><topic>Oligopeptides</topic><topic>Original</topic><topic>Original 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technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Wen-Ying</au><au>Miyakawa, Takuya</au><au>Lu, Jun</au><au>Hsieh, Yun Hua</au><au>Gu, Ruizeng</au><au>Miyauchi, Yumiko</au><au>Katsuno, Kana</au><au>Cai, Mu-Yi</au><au>Tanokura, Masaru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten</atitle><jtitle>Journal of food science and technology</jtitle><stitle>J Food Sci Technol</stitle><addtitle>J Food Sci Technol</addtitle><date>2021-09-01</date><risdate>2021</risdate><volume>58</volume><issue>9</issue><spage>3504</spage><epage>3513</epage><pages>3504-3513</pages><issn>0022-1155</issn><eissn>0975-8402</eissn><abstract>Wheat gluten was hydrolyzed with both alkaline protease and neutral protease to produce high-protein and low-wheat-weight oligopeptides (WOP), which was subjected to a multistage purification. Then, high performance liquid chromatography was applied to separate WOP. In order to identify WOP sequences, six major fractions were gathered for mass spectrometry. A total of 15 peptides were synthesized for further in vitro analyses of their antithrombotic activity, vasorelaxation activity, and cholesterol reducing activity. Two antithrombotic peptides (ILPR and ILR), three vasorelaxant peptides (VN, FPQ, and FR), and four cholesterol-lowering peptides (QRQ, ILPR, FPQ, and ILR) were identified. These active peptides in WOP were also quantified. These peptides are novel candidate peptides with vascular disease suppressing effects. The results indicate WOP as good protein sources for multifunctional peptides.</abstract><cop>New Delhi</cop><pub>Springer India</pub><pmid>34366467</pmid><doi>10.1007/s13197-021-05040-5</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-8369-0809</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alkaline protease Chemistry Chemistry and Materials Science Chemistry/Food Science Cholesterol Food Science Gluten High performance liquid chromatography Liquid chromatography Mass spectrometry Mass spectroscopy Nutrition Oligopeptides Original Original Article Peptides Protease Protein purification Protein sources Proteins Sequences Vascular diseases Vasodilation Wheat |
| title | Isolation and characterization of oligopeptides with vascular disease suppression effects derived from wheat gluten |
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