Identification of a novel glycerophosphodiester phosphodiesterase from Bacillus altitudinis W3 and its application in degradation of diphenyl phosphate
Diphenyl phosphate (DPHP) has been increasingly detected in environmental samples, posing a potential hazard to humans and other organisms and arousing concern regarding its adverse effects. Biological degradation of DPHP is considered a promising and environmentally friendly method for its removal....
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| Veröffentlicht in: | 3 Biotech 2021-04, Vol.11 (4), p.161, Article 161 |
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| creator | Ren, Runxian Zhai, Lixin Tian, Qiaopeng Meng, Di Guan, Zhengbin Cai, Yujie Liao, Xiangru |
| description | Diphenyl phosphate (DPHP) has been increasingly detected in environmental samples, posing a potential hazard to humans and other organisms and arousing concern regarding its adverse effects. Biological degradation of DPHP is considered a promising and environmentally friendly method for its removal. In this study, the
bagdpd
gene was mined from the
Bacillus altitudinis
W3 genome and identified as a glycerophosphodiester phosphodiesterase by bioinformatics analysis. The enzyme was expressed and its biochemical properties were studied. When using bis(4-nitrophenyl) phosphate as substrate, enzyme activity was optimal at 55 °C and a pH of 8.5. The enzyme remained stable in the pH range of 8.0 − 10.0. The rBaGDPD enzyme degraded DPHP and the reaction product was identified as phenyl phosphate by LC–MS. This is the first report of a glycerophosphodiester phosphodiesterase exhibiting hydrolytic activity against DPHP. This study demonstrated that rBaGDPD could have the potential for bioremediation and industrial applications. |
| doi_str_mv | 10.1007/s13205-021-02704-z |
| format | Article |
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bagdpd
gene was mined from the
Bacillus altitudinis
W3 genome and identified as a glycerophosphodiester phosphodiesterase by bioinformatics analysis. The enzyme was expressed and its biochemical properties were studied. When using bis(4-nitrophenyl) phosphate as substrate, enzyme activity was optimal at 55 °C and a pH of 8.5. The enzyme remained stable in the pH range of 8.0 − 10.0. The rBaGDPD enzyme degraded DPHP and the reaction product was identified as phenyl phosphate by LC–MS. This is the first report of a glycerophosphodiester phosphodiesterase exhibiting hydrolytic activity against DPHP. This study demonstrated that rBaGDPD could have the potential for bioremediation and industrial applications.</description><identifier>ISSN: 2190-572X</identifier><identifier>EISSN: 2190-5738</identifier><identifier>DOI: 10.1007/s13205-021-02704-z</identifier><identifier>PMID: 33758739</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Agriculture ; Bacillus altitudinis ; Biodegradation ; Bioinformatics ; Biological effects ; Biomaterials ; Bioremediation ; Biotechnology ; Cancer Research ; Chemistry ; Chemistry and Materials Science ; Degradation ; Enzymatic activity ; Enzyme activity ; Enzymes ; Genomes ; Glycerophosphodiester phosphodiesterase ; Industrial applications ; pH effects ; Phosphodiesterase ; Reaction products ; Short Reports ; Stem Cells ; Substrates</subject><ispartof>3 Biotech, 2021-04, Vol.11 (4), p.161, Article 161</ispartof><rights>King Abdulaziz City for Science and Technology 2021</rights><rights>King Abdulaziz City for Science and Technology 2021.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-2b0107e393d73c01b206c88a4e6886ccf75071aa8c54d5862dc61224591ef6673</citedby><cites>FETCH-LOGICAL-c441t-2b0107e393d73c01b206c88a4e6886ccf75071aa8c54d5862dc61224591ef6673</cites><orcidid>0000-0002-0661-6311</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/PMC7937590/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7937590/$$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/33758739$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ren, Runxian</creatorcontrib><creatorcontrib>Zhai, Lixin</creatorcontrib><creatorcontrib>Tian, Qiaopeng</creatorcontrib><creatorcontrib>Meng, Di</creatorcontrib><creatorcontrib>Guan, Zhengbin</creatorcontrib><creatorcontrib>Cai, Yujie</creatorcontrib><creatorcontrib>Liao, Xiangru</creatorcontrib><title>Identification of a novel glycerophosphodiester phosphodiesterase from Bacillus altitudinis W3 and its application in degradation of diphenyl phosphate</title><title>3 Biotech</title><addtitle>3 Biotech</addtitle><addtitle>3 Biotech</addtitle><description>Diphenyl phosphate (DPHP) has been increasingly detected in environmental samples, posing a potential hazard to humans and other organisms and arousing concern regarding its adverse effects. Biological degradation of DPHP is considered a promising and environmentally friendly method for its removal. In this study, the
bagdpd
gene was mined from the
Bacillus altitudinis
W3 genome and identified as a glycerophosphodiester phosphodiesterase by bioinformatics analysis. The enzyme was expressed and its biochemical properties were studied. When using bis(4-nitrophenyl) phosphate as substrate, enzyme activity was optimal at 55 °C and a pH of 8.5. The enzyme remained stable in the pH range of 8.0 − 10.0. The rBaGDPD enzyme degraded DPHP and the reaction product was identified as phenyl phosphate by LC–MS. This is the first report of a glycerophosphodiester phosphodiesterase exhibiting hydrolytic activity against DPHP. This study demonstrated that rBaGDPD could have the potential for bioremediation and industrial applications.</description><subject>Agriculture</subject><subject>Bacillus altitudinis</subject><subject>Biodegradation</subject><subject>Bioinformatics</subject><subject>Biological effects</subject><subject>Biomaterials</subject><subject>Bioremediation</subject><subject>Biotechnology</subject><subject>Cancer Research</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Degradation</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Genomes</subject><subject>Glycerophosphodiester phosphodiesterase</subject><subject>Industrial applications</subject><subject>pH effects</subject><subject>Phosphodiesterase</subject><subject>Reaction products</subject><subject>Short Reports</subject><subject>Stem Cells</subject><subject>Substrates</subject><issn>2190-572X</issn><issn>2190-5738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9UctqGzEUFSWlMW5-oIsiyHpaPUYjzSaQmDQNGLJpaXdCljS2gixNpRmD_SP53Six4zSbCC56nXvO5RwAvmD0DSPEv2dMCWIVIrgUR3W1-wAmBLeoYpyKk-OZ_D0FZznfo7IYZi1Gn8AppZwJTtsJeLg1Ngyuc1oNLgYYO6hgiBvr4dJvtU2xX8VcyjibB5vg26vKFnYpruGV0s77MUPlBzeMxgWX4R8KVTDQDeW57_2LhgvQ2GVS5ihpXL-yYesP7Gqwn8HHTvlszw77FPz-cf1r9rOa393czi7nla5rPFRkgTDilrbUcKoRXhDUaCFUbRshGq07zhDHSgnNasNEQ4xuMCF18cF2TcPpFFzseftxsbZGFzOS8rJPbq3SVkbl5Nuf4FZyGTeSt8XDFhWC8wNBiv_GYoq8j2MKZWZJ6lYwVpcJCorsUTrFnJPtjgoYyac85T5PWfKUz3nKXWn6-v9sx5aX9AqA7gG5fIWlTa_a79A-AmDrsFs</recordid><startdate>20210401</startdate><enddate>20210401</enddate><creator>Ren, Runxian</creator><creator>Zhai, Lixin</creator><creator>Tian, Qiaopeng</creator><creator>Meng, Di</creator><creator>Guan, Zhengbin</creator><creator>Cai, Yujie</creator><creator>Liao, Xiangru</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0661-6311</orcidid></search><sort><creationdate>20210401</creationdate><title>Identification of a novel glycerophosphodiester phosphodiesterase from Bacillus altitudinis W3 and its application in degradation of diphenyl phosphate</title><author>Ren, Runxian ; Zhai, Lixin ; Tian, Qiaopeng ; Meng, Di ; Guan, Zhengbin ; Cai, Yujie ; Liao, Xiangru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-2b0107e393d73c01b206c88a4e6886ccf75071aa8c54d5862dc61224591ef6673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Agriculture</topic><topic>Bacillus altitudinis</topic><topic>Biodegradation</topic><topic>Bioinformatics</topic><topic>Biological effects</topic><topic>Biomaterials</topic><topic>Bioremediation</topic><topic>Biotechnology</topic><topic>Cancer Research</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Degradation</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>Genomes</topic><topic>Glycerophosphodiester phosphodiesterase</topic><topic>Industrial applications</topic><topic>pH effects</topic><topic>Phosphodiesterase</topic><topic>Reaction products</topic><topic>Short Reports</topic><topic>Stem Cells</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ren, Runxian</creatorcontrib><creatorcontrib>Zhai, Lixin</creatorcontrib><creatorcontrib>Tian, Qiaopeng</creatorcontrib><creatorcontrib>Meng, Di</creatorcontrib><creatorcontrib>Guan, Zhengbin</creatorcontrib><creatorcontrib>Cai, Yujie</creatorcontrib><creatorcontrib>Liao, Xiangru</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>3 Biotech</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ren, Runxian</au><au>Zhai, Lixin</au><au>Tian, Qiaopeng</au><au>Meng, Di</au><au>Guan, Zhengbin</au><au>Cai, Yujie</au><au>Liao, Xiangru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a novel glycerophosphodiester phosphodiesterase from Bacillus altitudinis W3 and its application in degradation of diphenyl phosphate</atitle><jtitle>3 Biotech</jtitle><stitle>3 Biotech</stitle><addtitle>3 Biotech</addtitle><date>2021-04-01</date><risdate>2021</risdate><volume>11</volume><issue>4</issue><spage>161</spage><pages>161-</pages><artnum>161</artnum><issn>2190-572X</issn><eissn>2190-5738</eissn><abstract>Diphenyl phosphate (DPHP) has been increasingly detected in environmental samples, posing a potential hazard to humans and other organisms and arousing concern regarding its adverse effects. Biological degradation of DPHP is considered a promising and environmentally friendly method for its removal. In this study, the
bagdpd
gene was mined from the
Bacillus altitudinis
W3 genome and identified as a glycerophosphodiester phosphodiesterase by bioinformatics analysis. The enzyme was expressed and its biochemical properties were studied. When using bis(4-nitrophenyl) phosphate as substrate, enzyme activity was optimal at 55 °C and a pH of 8.5. The enzyme remained stable in the pH range of 8.0 − 10.0. The rBaGDPD enzyme degraded DPHP and the reaction product was identified as phenyl phosphate by LC–MS. This is the first report of a glycerophosphodiester phosphodiesterase exhibiting hydrolytic activity against DPHP. This study demonstrated that rBaGDPD could have the potential for bioremediation and industrial applications.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>33758739</pmid><doi>10.1007/s13205-021-02704-z</doi><orcidid>https://orcid.org/0000-0002-0661-6311</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Agriculture Bacillus altitudinis Biodegradation Bioinformatics Biological effects Biomaterials Bioremediation Biotechnology Cancer Research Chemistry Chemistry and Materials Science Degradation Enzymatic activity Enzyme activity Enzymes Genomes Glycerophosphodiester phosphodiesterase Industrial applications pH effects Phosphodiesterase Reaction products Short Reports Stem Cells Substrates |
| title | Identification of a novel glycerophosphodiester phosphodiesterase from Bacillus altitudinis W3 and its application in degradation of diphenyl phosphate |
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