Intrinsic Peroxidase-like Activity of Ficin
Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for the intrinsic peroxidase-like activity of ficin and designed e...
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| Veröffentlicht in: | Scientific reports 2017-02, Vol.7 (1), p.43141-43141, Article 43141 |
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| creator | Yang, Yufang Shen, Dongjun Long, Yijuan Xie, Zhixiong Zheng, Huzhi |
| description | Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for the intrinsic peroxidase-like activity of ficin and designed experiments to examine its effectiveness in a variety of scenarios. Ficin can transform peroxidase substrates to colored products in the existence of H
2
O
2
. Our results also indicate that the active sites of peroxidase-like activity of ficin are different from that of protease, which reveals that one enzyme may catalyze more than one kind of substrate to perform different types of reactions. On the basis of these findings, H
2
O
2
releasing from MCF-7 cells was detected successfully. Our findings support a wider application of ficin in biochemistry and open up the possibility of utilizing ficin as enzymatic mimics in biotechnology and environmental monitoring. |
| doi_str_mv | 10.1038/srep43141 |
| format | Article |
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2
O
2
. Our results also indicate that the active sites of peroxidase-like activity of ficin are different from that of protease, which reveals that one enzyme may catalyze more than one kind of substrate to perform different types of reactions. On the basis of these findings, H
2
O
2
releasing from MCF-7 cells was detected successfully. Our findings support a wider application of ficin in biochemistry and open up the possibility of utilizing ficin as enzymatic mimics in biotechnology and environmental monitoring.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep43141</identifier><identifier>PMID: 28224979</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>639/638/11/872 ; 639/638/77/603 ; Biotechnology ; Catalytic Domain ; Environmental monitoring ; Enzymes ; Ficain - metabolism ; Fruit trees ; Humanities and Social Sciences ; Humans ; Hydrogen Peroxide - metabolism ; Latex ; MCF-7 Cells ; multidisciplinary ; Oxidation-Reduction ; Peroxidase ; Peroxidase - metabolism ; Proteinase ; Science</subject><ispartof>Scientific reports, 2017-02, Vol.7 (1), p.43141-43141, Article 43141</ispartof><rights>The Author(s) 2017</rights><rights>Copyright Nature Publishing Group Feb 2017</rights><rights>Copyright © 2017, The Author(s) 2017 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-ff78b87bd43eaabd82921964663b8f63a130bb6c896d1fe94264af02eae7a1463</citedby><cites>FETCH-LOGICAL-c504t-ff78b87bd43eaabd82921964663b8f63a130bb6c896d1fe94264af02eae7a1463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5320487/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5320487/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27923,27924,41119,42188,51575,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28224979$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Yufang</creatorcontrib><creatorcontrib>Shen, Dongjun</creatorcontrib><creatorcontrib>Long, Yijuan</creatorcontrib><creatorcontrib>Xie, Zhixiong</creatorcontrib><creatorcontrib>Zheng, Huzhi</creatorcontrib><title>Intrinsic Peroxidase-like Activity of Ficin</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for the intrinsic peroxidase-like activity of ficin and designed experiments to examine its effectiveness in a variety of scenarios. Ficin can transform peroxidase substrates to colored products in the existence of H
2
O
2
. Our results also indicate that the active sites of peroxidase-like activity of ficin are different from that of protease, which reveals that one enzyme may catalyze more than one kind of substrate to perform different types of reactions. On the basis of these findings, H
2
O
2
releasing from MCF-7 cells was detected successfully. Our findings support a wider application of ficin in biochemistry and open up the possibility of utilizing ficin as enzymatic mimics in biotechnology and environmental monitoring.</description><subject>639/638/11/872</subject><subject>639/638/77/603</subject><subject>Biotechnology</subject><subject>Catalytic Domain</subject><subject>Environmental monitoring</subject><subject>Enzymes</subject><subject>Ficain - metabolism</subject><subject>Fruit trees</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Latex</subject><subject>MCF-7 Cells</subject><subject>multidisciplinary</subject><subject>Oxidation-Reduction</subject><subject>Peroxidase</subject><subject>Peroxidase - metabolism</subject><subject>Proteinase</subject><subject>Science</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNplkU1LAzEQhoMottQe_AOy4MUPVvPVbHIRSrFaKOhBzyGbTWrqdrcmu8X-eyOtpepcZmAe3nlnBoBTBG8QJPw2eLOkBFF0ALoY0kGKCcaHe3UH9EOYwxgDLCgSx6CDOcZUZKILridV410VnE6eja8_XaGCSUv3bpKhbtzKNeuktsnYaVedgCOrymD629wDr-P7l9FjOn16mIyG01QPIG1SazOe8ywvKDFK5QXHAiPBKGMk55YRhQjMc6a5YAWyRlDMqLIQG2UyhSgjPXC30V22-cIU2kSLqpRL7xbKr2WtnPzdqdybnNUrOSBxaZ5FgYutgK8_WhMauXBBm7JUlanbIBHPoOBUcB7R8z_ovG59FdeTSECU4UjSSF1uKO3rEA9ud2YQlN9fkLsvRPZs3_2O_Ll5BK42QIitamb83sh_al8HRY_0</recordid><startdate>20170222</startdate><enddate>20170222</enddate><creator>Yang, Yufang</creator><creator>Shen, Dongjun</creator><creator>Long, Yijuan</creator><creator>Xie, Zhixiong</creator><creator>Zheng, Huzhi</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20170222</creationdate><title>Intrinsic Peroxidase-like Activity of Ficin</title><author>Yang, Yufang ; Shen, Dongjun ; Long, Yijuan ; Xie, Zhixiong ; Zheng, Huzhi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-ff78b87bd43eaabd82921964663b8f63a130bb6c896d1fe94264af02eae7a1463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>639/638/11/872</topic><topic>639/638/77/603</topic><topic>Biotechnology</topic><topic>Catalytic Domain</topic><topic>Environmental monitoring</topic><topic>Enzymes</topic><topic>Ficain - metabolism</topic><topic>Fruit trees</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Latex</topic><topic>MCF-7 Cells</topic><topic>multidisciplinary</topic><topic>Oxidation-Reduction</topic><topic>Peroxidase</topic><topic>Peroxidase - metabolism</topic><topic>Proteinase</topic><topic>Science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Yufang</creatorcontrib><creatorcontrib>Shen, Dongjun</creatorcontrib><creatorcontrib>Long, Yijuan</creatorcontrib><creatorcontrib>Xie, Zhixiong</creatorcontrib><creatorcontrib>Zheng, Huzhi</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Yufang</au><au>Shen, Dongjun</au><au>Long, Yijuan</au><au>Xie, Zhixiong</au><au>Zheng, Huzhi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Intrinsic Peroxidase-like Activity of Ficin</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-02-22</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>43141</spage><epage>43141</epage><pages>43141-43141</pages><artnum>43141</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for the intrinsic peroxidase-like activity of ficin and designed experiments to examine its effectiveness in a variety of scenarios. Ficin can transform peroxidase substrates to colored products in the existence of H
2
O
2
. Our results also indicate that the active sites of peroxidase-like activity of ficin are different from that of protease, which reveals that one enzyme may catalyze more than one kind of substrate to perform different types of reactions. On the basis of these findings, H
2
O
2
releasing from MCF-7 cells was detected successfully. Our findings support a wider application of ficin in biochemistry and open up the possibility of utilizing ficin as enzymatic mimics in biotechnology and environmental monitoring.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28224979</pmid><doi>10.1038/srep43141</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 639/638/11/872 639/638/77/603 Biotechnology Catalytic Domain Environmental monitoring Enzymes Ficain - metabolism Fruit trees Humanities and Social Sciences Humans Hydrogen Peroxide - metabolism Latex MCF-7 Cells multidisciplinary Oxidation-Reduction Peroxidase Peroxidase - metabolism Proteinase Science |
| title | Intrinsic Peroxidase-like Activity of Ficin |
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