Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library
A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a...
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| creator | Zhang, Lin Fan, Yongxin Zheng, Haoying Du, Fengguang Zhang, Ke-qin Huang, Xiaowei Wang, Linfeng Zhang, Man Niu, Qiuhong |
| description | A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application. |
| doi_str_mv | 10.1371/journal.pone.0082437 |
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Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0082437</identifier><identifier>PMID: 24386096</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Analysis ; Animals ; Bacillus ; Biocatalysts ; Biomass ; Biotechnology ; Bursaphelenchus xylophilus ; Cellulase ; Cellulase - chemistry ; Cellulase - genetics ; Cellulase - isolation & purification ; Cellulase - metabolism ; Cellulose ; Cloning ; Copper ; Crystalline cellulose ; Deoxyribonucleic acid ; DNA ; E coli ; Endoglucanase ; Enzymes ; Filter paper ; Gel electrophoresis ; Genes ; Genomic Library ; Helminth Proteins - chemistry ; Helminth Proteins - genetics ; Helminth Proteins - isolation & purification ; Helminth Proteins - metabolism ; Iron ; Laboratories ; Libraries ; Life sciences ; Lignocellulose ; Medical screening ; Mercury (metal) ; Metagenome ; Metals ; Microorganisms ; Nematoda - enzymology ; Nematoda - genetics ; pH effects ; Phylogeny ; Polysaccharides ; Proteins ; Saccharides ; Sodium lauryl sulfate</subject><ispartof>PloS one, 2013-12, Vol.8 (12), p.e82437-e82437</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Zhang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Zhang et al 2013 Zhang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-4d816df6079d8841c5f4dfb1231a0e2c12fa0c313e411ff18d1ab70f35f770053</citedby><cites>FETCH-LOGICAL-c758t-4d816df6079d8841c5f4dfb1231a0e2c12fa0c313e411ff18d1ab70f35f770053</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/PMC3873927/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873927/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2929,23871,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24386096$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Schuch, Raymond</contributor><creatorcontrib>Zhang, Lin</creatorcontrib><creatorcontrib>Fan, Yongxin</creatorcontrib><creatorcontrib>Zheng, Haoying</creatorcontrib><creatorcontrib>Du, Fengguang</creatorcontrib><creatorcontrib>Zhang, Ke-qin</creatorcontrib><creatorcontrib>Huang, Xiaowei</creatorcontrib><creatorcontrib>Wang, Linfeng</creatorcontrib><creatorcontrib>Zhang, Man</creatorcontrib><creatorcontrib>Niu, Qiuhong</creatorcontrib><title>Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.</description><subject>Amino acids</subject><subject>Analysis</subject><subject>Animals</subject><subject>Bacillus</subject><subject>Biocatalysts</subject><subject>Biomass</subject><subject>Biotechnology</subject><subject>Bursaphelenchus xylophilus</subject><subject>Cellulase</subject><subject>Cellulase - chemistry</subject><subject>Cellulase - genetics</subject><subject>Cellulase - isolation & purification</subject><subject>Cellulase - metabolism</subject><subject>Cellulose</subject><subject>Cloning</subject><subject>Copper</subject><subject>Crystalline cellulose</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>E coli</subject><subject>Endoglucanase</subject><subject>Enzymes</subject><subject>Filter paper</subject><subject>Gel electrophoresis</subject><subject>Genes</subject><subject>Genomic Library</subject><subject>Helminth Proteins - chemistry</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - isolation & purification</subject><subject>Helminth Proteins - metabolism</subject><subject>Iron</subject><subject>Laboratories</subject><subject>Libraries</subject><subject>Life sciences</subject><subject>Lignocellulose</subject><subject>Medical screening</subject><subject>Mercury (metal)</subject><subject>Metagenome</subject><subject>Metals</subject><subject>Microorganisms</subject><subject>Nematoda - enzymology</subject><subject>Nematoda - genetics</subject><subject>pH effects</subject><subject>Phylogeny</subject><subject>Polysaccharides</subject><subject>Proteins</subject><subject>Saccharides</subject><subject>Sodium lauryl sulfate</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk01r3DAQhk1padK0_6C0hkJpD7uVLFuyL4U09GMhEOjXVYxlydYiS1vJDkl-feSuE9Ylh6KDxOiZdzSjmSR5idEaE4Y_bN3oLZj1zlm5RqjMcsIeJce4ItmKZog8PjgfJc9C2CJUkJLSp8lRZEuKKnqc9JvgDAza2RRsk4oOPIhBen2zNzqVQmrdpTSptI1rzSjAQpCp8q6PV59GH2DXSSOt6MaQXl0bt-u0icdeDtBK63otUqNrD_76efJEgQnyxbyfJL--fP559m11fvF1c3Z6vhKsKIdV3pSYNooiVjVlmWNRqLxRNc4IBiQzgTMFSBBMZI6xUrhsMNQMKVIoxqYsT5LXe92dcYHPlQoc5wyjnO6JzZ5oHGz5zus-Po870PyvwfmWgx-0MJJXssYVJSxrBMpJUQErEK4zggqagShx1Po4RxvrXjZC2sGDWYgub6zueOsuOSkZqTIWBd7NAt79GWUYeK-DkMaAlW6c3l0hhmmOJ_TNP-jD2c1UCzEBbZWLccUkyk9zxqoyI4RGav0AFVcj45_FtlI62hcO7xcOkRnk1dDCGALf_Pj-_-zF7yX79oDtJJihi205Th0YlmC-B4V3IXip7ouMEZ-m4q4afJoKPk9FdHt1-EH3TndjQG4Bm6sIDw</recordid><startdate>20131227</startdate><enddate>20131227</enddate><creator>Zhang, Lin</creator><creator>Fan, Yongxin</creator><creator>Zheng, Haoying</creator><creator>Du, Fengguang</creator><creator>Zhang, Ke-qin</creator><creator>Huang, Xiaowei</creator><creator>Wang, Linfeng</creator><creator>Zhang, Man</creator><creator>Niu, Qiuhong</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20131227</creationdate><title>Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library</title><author>Zhang, Lin ; Fan, Yongxin ; Zheng, Haoying ; Du, Fengguang ; Zhang, Ke-qin ; Huang, Xiaowei ; Wang, Linfeng ; Zhang, Man ; Niu, Qiuhong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-4d816df6079d8841c5f4dfb1231a0e2c12fa0c313e411ff18d1ab70f35f770053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino acids</topic><topic>Analysis</topic><topic>Animals</topic><topic>Bacillus</topic><topic>Biocatalysts</topic><topic>Biomass</topic><topic>Biotechnology</topic><topic>Bursaphelenchus xylophilus</topic><topic>Cellulase</topic><topic>Cellulase - chemistry</topic><topic>Cellulase - genetics</topic><topic>Cellulase - isolation & purification</topic><topic>Cellulase - metabolism</topic><topic>Cellulose</topic><topic>Cloning</topic><topic>Copper</topic><topic>Crystalline cellulose</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>E coli</topic><topic>Endoglucanase</topic><topic>Enzymes</topic><topic>Filter paper</topic><topic>Gel electrophoresis</topic><topic>Genes</topic><topic>Genomic Library</topic><topic>Helminth Proteins - chemistry</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - isolation & purification</topic><topic>Helminth Proteins - metabolism</topic><topic>Iron</topic><topic>Laboratories</topic><topic>Libraries</topic><topic>Life sciences</topic><topic>Lignocellulose</topic><topic>Medical screening</topic><topic>Mercury (metal)</topic><topic>Metagenome</topic><topic>Metals</topic><topic>Microorganisms</topic><topic>Nematoda - enzymology</topic><topic>Nematoda - genetics</topic><topic>pH effects</topic><topic>Phylogeny</topic><topic>Polysaccharides</topic><topic>Proteins</topic><topic>Saccharides</topic><topic>Sodium lauryl sulfate</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Lin</creatorcontrib><creatorcontrib>Fan, Yongxin</creatorcontrib><creatorcontrib>Zheng, Haoying</creatorcontrib><creatorcontrib>Du, Fengguang</creatorcontrib><creatorcontrib>Zhang, Ke-qin</creatorcontrib><creatorcontrib>Huang, Xiaowei</creatorcontrib><creatorcontrib>Wang, Linfeng</creatorcontrib><creatorcontrib>Zhang, Man</creatorcontrib><creatorcontrib>Niu, Qiuhong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Lin</au><au>Fan, Yongxin</au><au>Zheng, Haoying</au><au>Du, Fengguang</au><au>Zhang, Ke-qin</au><au>Huang, Xiaowei</au><au>Wang, Linfeng</au><au>Zhang, Man</au><au>Niu, Qiuhong</au><au>Schuch, Raymond</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-12-27</date><risdate>2013</risdate><volume>8</volume><issue>12</issue><spage>e82437</spage><epage>e82437</epage><pages>e82437-e82437</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24386096</pmid><doi>10.1371/journal.pone.0082437</doi><tpages>e82437</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Analysis Animals Bacillus Biocatalysts Biomass Biotechnology Bursaphelenchus xylophilus Cellulase Cellulase - chemistry Cellulase - genetics Cellulase - isolation & purification Cellulase - metabolism Cellulose Cloning Copper Crystalline cellulose Deoxyribonucleic acid DNA E coli Endoglucanase Enzymes Filter paper Gel electrophoresis Genes Genomic Library Helminth Proteins - chemistry Helminth Proteins - genetics Helminth Proteins - isolation & purification Helminth Proteins - metabolism Iron Laboratories Libraries Life sciences Lignocellulose Medical screening Mercury (metal) Metagenome Metals Microorganisms Nematoda - enzymology Nematoda - genetics pH effects Phylogeny Polysaccharides Proteins Saccharides Sodium lauryl sulfate |
| title | Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-13T10%3A52%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Isolation%20and%20characterization%20of%20a%20novel%20endoglucanase%20from%20a%20Bursaphelenchus%20xylophilus%20metagenomic%20library&rft.jtitle=PloS%20one&rft.au=Zhang,%20Lin&rft.date=2013-12-27&rft.volume=8&rft.issue=12&rft.spage=e82437&rft.epage=e82437&rft.pages=e82437-e82437&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0082437&rft_dat=%3Cgale_plos_%3EA477982336%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1471046005&rft_id=info:pmid/24386096&rft_galeid=A477982336&rft_doaj_id=oai_doaj_org_article_9eb196372dc04359a7501b230562ac81&rfr_iscdi=true |