The ant Lasius niger is a new source of bacterial enzymes with biotechnological potential for bleaching dye
Industrial synthetic dyes cause health and environmental problems. This work describes the isolation of 84 bacterial strains from the midgut of the Lasius niger ant and the evaluation of their potential application in dye bioremediation. Strains were identified and classified as judged by rRNA 16S....
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| Veröffentlicht in: | Scientific reports 2019-10, Vol.9 (1), p.15217-11, Article 15217 |
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| description | Industrial synthetic dyes cause health and environmental problems. This work describes the isolation of 84 bacterial strains from the midgut of the
Lasius niger
ant and the evaluation of their potential application in dye bioremediation. Strains were identified and classified as judged by rRNA 16S. The most abundant isolates were found to belong to Actinobacteria (49%) and Firmicutes (47.2%). We analyzed the content in laccase, azoreductase and peroxidase activities and their ability to degrade three known dyes (azo, thiazine and anthraquinone) with different chemical structures. Strain Ln26 (identified as
Brevibacterium permense
) strongly decolorized the three dyes tested at different conditions. Strain Ln78 (
Streptomyces ambofaciens)
exhibited a high level of activity in the presence of Toluidine Blue (TB). It was determined that 8.5 was the optimal pH for these two strains, the optimal temperature conditions ranged between 22 and 37 °C, and acidic pHs and temperatures around 50 °C caused enzyme inactivation. Finally, the genome of the most promising candidate (Ln26, approximately 4.2 Mb in size) was sequenced. Genes coding for two DyP-type peroxidases, one laccase and one azoreductase were identified and account for the ability of this strain to effectively oxidize a variety of dyes with different chemical structures. |
| doi_str_mv | 10.1038/s41598-019-51669-w |
| format | Article |
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Lasius niger
ant and the evaluation of their potential application in dye bioremediation. Strains were identified and classified as judged by rRNA 16S. The most abundant isolates were found to belong to Actinobacteria (49%) and Firmicutes (47.2%). We analyzed the content in laccase, azoreductase and peroxidase activities and their ability to degrade three known dyes (azo, thiazine and anthraquinone) with different chemical structures. Strain Ln26 (identified as
Brevibacterium permense
) strongly decolorized the three dyes tested at different conditions. Strain Ln78 (
Streptomyces ambofaciens)
exhibited a high level of activity in the presence of Toluidine Blue (TB). It was determined that 8.5 was the optimal pH for these two strains, the optimal temperature conditions ranged between 22 and 37 °C, and acidic pHs and temperatures around 50 °C caused enzyme inactivation. Finally, the genome of the most promising candidate (Ln26, approximately 4.2 Mb in size) was sequenced. Genes coding for two DyP-type peroxidases, one laccase and one azoreductase were identified and account for the ability of this strain to effectively oxidize a variety of dyes with different chemical structures.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-019-51669-w</identifier><identifier>PMID: 31645628</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject><![CDATA[45/43 ; 704/172 ; 704/172/169/896 ; 704/172/4081 ; Actinobacteria - enzymology ; Actinobacteria - isolation & purification ; Actinobacteria - metabolism ; Animals ; Anthraquinone ; Ants - microbiology ; Azo dyes ; Azoreductase ; Bacteria - enzymology ; Bacteria - isolation & purification ; Bacteria - metabolism ; Biodegradation, Environmental ; Bioremediation ; Biotechnology ; Bleaching ; Brevibacterium - enzymology ; Brevibacterium - isolation & purification ; Brevibacterium - metabolism ; Coloring Agents - isolation & purification ; Coloring Agents - metabolism ; Dyes ; Environmental Pollutants - isolation & purification ; Environmental Pollutants - metabolism ; Firmicutes - enzymology ; Firmicutes - isolation & purification ; Firmicutes - metabolism ; Genomes ; Humanities and Social Sciences ; Inactivation ; Laccase ; Laccase - isolation & purification ; Laccase - metabolism ; Lasius niger ; Midgut ; multidisciplinary ; NADH, NADPH Oxidoreductases - isolation & purification ; NADH, NADPH Oxidoreductases - metabolism ; Peroxidase ; Peroxidase - isolation & purification ; Peroxidase - metabolism ; rRNA 16S ; Science ; Science (multidisciplinary) ; Strains (organisms) ; Streptomyces - enzymology ; Streptomyces - isolation & purification ; Streptomyces - metabolism ; Toluidine]]></subject><ispartof>Scientific reports, 2019-10, Vol.9 (1), p.15217-11, Article 15217</ispartof><rights>The Author(s) 2019</rights><rights>2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-e4b48f1427654e06a1c8ef57b3dc3d645ede366dcfd2a875a04ffe3432b96f7c3</citedby><cites>FETCH-LOGICAL-c474t-e4b48f1427654e06a1c8ef57b3dc3d645ede366dcfd2a875a04ffe3432b96f7c3</cites><orcidid>0000-0001-9612-761X</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/PMC6811527/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6811527/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31645628$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Díez-Méndez, Alexandra</creatorcontrib><creatorcontrib>García-Fraile, Paula</creatorcontrib><creatorcontrib>Solano, Francisco</creatorcontrib><creatorcontrib>Rivas, Raúl</creatorcontrib><title>The ant Lasius niger is a new source of bacterial enzymes with biotechnological potential for bleaching dye</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Industrial synthetic dyes cause health and environmental problems. This work describes the isolation of 84 bacterial strains from the midgut of the
Lasius niger
ant and the evaluation of their potential application in dye bioremediation. Strains were identified and classified as judged by rRNA 16S. The most abundant isolates were found to belong to Actinobacteria (49%) and Firmicutes (47.2%). We analyzed the content in laccase, azoreductase and peroxidase activities and their ability to degrade three known dyes (azo, thiazine and anthraquinone) with different chemical structures. Strain Ln26 (identified as
Brevibacterium permense
) strongly decolorized the three dyes tested at different conditions. Strain Ln78 (
Streptomyces ambofaciens)
exhibited a high level of activity in the presence of Toluidine Blue (TB). It was determined that 8.5 was the optimal pH for these two strains, the optimal temperature conditions ranged between 22 and 37 °C, and acidic pHs and temperatures around 50 °C caused enzyme inactivation. Finally, the genome of the most promising candidate (Ln26, approximately 4.2 Mb in size) was sequenced. Genes coding for two DyP-type peroxidases, one laccase and one azoreductase were identified and account for the ability of this strain to effectively oxidize a variety of dyes with different chemical structures.</description><subject>45/43</subject><subject>704/172</subject><subject>704/172/169/896</subject><subject>704/172/4081</subject><subject>Actinobacteria - enzymology</subject><subject>Actinobacteria - isolation & purification</subject><subject>Actinobacteria - metabolism</subject><subject>Animals</subject><subject>Anthraquinone</subject><subject>Ants - microbiology</subject><subject>Azo dyes</subject><subject>Azoreductase</subject><subject>Bacteria - enzymology</subject><subject>Bacteria - isolation & purification</subject><subject>Bacteria - metabolism</subject><subject>Biodegradation, Environmental</subject><subject>Bioremediation</subject><subject>Biotechnology</subject><subject>Bleaching</subject><subject>Brevibacterium - enzymology</subject><subject>Brevibacterium - isolation & purification</subject><subject>Brevibacterium - 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enzymology</topic><topic>Actinobacteria - isolation & purification</topic><topic>Actinobacteria - metabolism</topic><topic>Animals</topic><topic>Anthraquinone</topic><topic>Ants - microbiology</topic><topic>Azo dyes</topic><topic>Azoreductase</topic><topic>Bacteria - enzymology</topic><topic>Bacteria - isolation & purification</topic><topic>Bacteria - metabolism</topic><topic>Biodegradation, Environmental</topic><topic>Bioremediation</topic><topic>Biotechnology</topic><topic>Bleaching</topic><topic>Brevibacterium - enzymology</topic><topic>Brevibacterium - isolation & purification</topic><topic>Brevibacterium - metabolism</topic><topic>Coloring Agents - isolation & purification</topic><topic>Coloring Agents - metabolism</topic><topic>Dyes</topic><topic>Environmental Pollutants - isolation & purification</topic><topic>Environmental Pollutants - metabolism</topic><topic>Firmicutes - enzymology</topic><topic>Firmicutes - isolation & purification</topic><topic>Firmicutes - metabolism</topic><topic>Genomes</topic><topic>Humanities and Social Sciences</topic><topic>Inactivation</topic><topic>Laccase</topic><topic>Laccase - isolation & purification</topic><topic>Laccase - metabolism</topic><topic>Lasius niger</topic><topic>Midgut</topic><topic>multidisciplinary</topic><topic>NADH, NADPH Oxidoreductases - isolation & purification</topic><topic>NADH, NADPH Oxidoreductases - metabolism</topic><topic>Peroxidase</topic><topic>Peroxidase - isolation & purification</topic><topic>Peroxidase - metabolism</topic><topic>rRNA 16S</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Strains (organisms)</topic><topic>Streptomyces - enzymology</topic><topic>Streptomyces - isolation & purification</topic><topic>Streptomyces - metabolism</topic><topic>Toluidine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Díez-Méndez, Alexandra</creatorcontrib><creatorcontrib>García-Fraile, Paula</creatorcontrib><creatorcontrib>Solano, Francisco</creatorcontrib><creatorcontrib>Rivas, Raúl</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>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Díez-Méndez, Alexandra</au><au>García-Fraile, Paula</au><au>Solano, Francisco</au><au>Rivas, Raúl</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ant Lasius niger is a new source of bacterial enzymes with biotechnological potential for bleaching dye</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2019-10-23</date><risdate>2019</risdate><volume>9</volume><issue>1</issue><spage>15217</spage><epage>11</epage><pages>15217-11</pages><artnum>15217</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Industrial synthetic dyes cause health and environmental problems. This work describes the isolation of 84 bacterial strains from the midgut of the
Lasius niger
ant and the evaluation of their potential application in dye bioremediation. Strains were identified and classified as judged by rRNA 16S. The most abundant isolates were found to belong to Actinobacteria (49%) and Firmicutes (47.2%). We analyzed the content in laccase, azoreductase and peroxidase activities and their ability to degrade three known dyes (azo, thiazine and anthraquinone) with different chemical structures. Strain Ln26 (identified as
Brevibacterium permense
) strongly decolorized the three dyes tested at different conditions. Strain Ln78 (
Streptomyces ambofaciens)
exhibited a high level of activity in the presence of Toluidine Blue (TB). It was determined that 8.5 was the optimal pH for these two strains, the optimal temperature conditions ranged between 22 and 37 °C, and acidic pHs and temperatures around 50 °C caused enzyme inactivation. Finally, the genome of the most promising candidate (Ln26, approximately 4.2 Mb in size) was sequenced. Genes coding for two DyP-type peroxidases, one laccase and one azoreductase were identified and account for the ability of this strain to effectively oxidize a variety of dyes with different chemical structures.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31645628</pmid><doi>10.1038/s41598-019-51669-w</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-9612-761X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 45/43 704/172 704/172/169/896 704/172/4081 Actinobacteria - enzymology Actinobacteria - isolation & purification Actinobacteria - metabolism Animals Anthraquinone Ants - microbiology Azo dyes Azoreductase Bacteria - enzymology Bacteria - isolation & purification Bacteria - metabolism Biodegradation, Environmental Bioremediation Biotechnology Bleaching Brevibacterium - enzymology Brevibacterium - isolation & purification Brevibacterium - metabolism Coloring Agents - isolation & purification Coloring Agents - metabolism Dyes Environmental Pollutants - isolation & purification Environmental Pollutants - metabolism Firmicutes - enzymology Firmicutes - isolation & purification Firmicutes - metabolism Genomes Humanities and Social Sciences Inactivation Laccase Laccase - isolation & purification Laccase - metabolism Lasius niger Midgut multidisciplinary NADH, NADPH Oxidoreductases - isolation & purification NADH, NADPH Oxidoreductases - metabolism Peroxidase Peroxidase - isolation & purification Peroxidase - metabolism rRNA 16S Science Science (multidisciplinary) Strains (organisms) Streptomyces - enzymology Streptomyces - isolation & purification Streptomyces - metabolism Toluidine |
| title | The ant Lasius niger is a new source of bacterial enzymes with biotechnological potential for bleaching dye |
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