Characterization of a Recombinant Thermostable Dehalogenase Isolated from the Hot Spring Thermophile Sulfolobus tokodaii
A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HADST remains fully active a...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2009-11, Vol.159 (2), p.382-393 |
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| creator | Bachas-Daunert, Philip G Law, Stacy A Wei, Yinan |
| description | A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HADST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications. |
| doi_str_mv | 10.1007/s12010-009-8589-9 |
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The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HADST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-009-8589-9</identifier><identifier>PMID: 19266316</identifier><language>eng</language><publisher>New York: New York : Humana Press Inc</publisher><subject>Bacteria ; Biochemistry ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Cloning ; Cloning, Molecular - methods ; Crenarchaeota ; dehalogenase ; dehalogenation ; E coli ; Enzyme Activation ; enzyme activity ; Enzyme Stability ; Enzymes ; Escherichia coli ; Escherichia coli - physiology ; gene expression ; Hot springs ; Hot Springs - microbiology ; Hydrolases - chemistry ; Hydrolases - genetics ; Hydrolases - metabolism ; molecular cloning ; Protein Engineering - methods ; provenance ; recombinant proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; springs (water) ; Sulfolobus - enzymology ; Sulfolobus - genetics ; Sulfolobus - metabolism ; Sulfolobus tokodaii ; Temperature ; thermal stability ; thermophilic microorganisms</subject><ispartof>Applied biochemistry and biotechnology, 2009-11, Vol.159 (2), p.382-393</ispartof><rights>Humana Press 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-c0ff5e4d84eb45635512fc68bc37b1c3d0337ea8db7c60a48ce619f9207da323</citedby><cites>FETCH-LOGICAL-c425t-c0ff5e4d84eb45635512fc68bc37b1c3d0337ea8db7c60a48ce619f9207da323</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-009-8589-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-009-8589-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19266316$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bachas-Daunert, Philip G</creatorcontrib><creatorcontrib>Law, Stacy A</creatorcontrib><creatorcontrib>Wei, Yinan</creatorcontrib><title>Characterization of a Recombinant Thermostable Dehalogenase Isolated from the Hot Spring Thermophile Sulfolobus tokodaii</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HADST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.</description><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cloning</subject><subject>Cloning, Molecular - methods</subject><subject>Crenarchaeota</subject><subject>dehalogenase</subject><subject>dehalogenation</subject><subject>E coli</subject><subject>Enzyme Activation</subject><subject>enzyme activity</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - physiology</subject><subject>gene expression</subject><subject>Hot springs</subject><subject>Hot Springs - microbiology</subject><subject>Hydrolases - chemistry</subject><subject>Hydrolases - genetics</subject><subject>Hydrolases - metabolism</subject><subject>molecular cloning</subject><subject>Protein Engineering - methods</subject><subject>provenance</subject><subject>recombinant proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>springs (water)</subject><subject>Sulfolobus - enzymology</subject><subject>Sulfolobus - genetics</subject><subject>Sulfolobus - metabolism</subject><subject>Sulfolobus tokodaii</subject><subject>Temperature</subject><subject>thermal stability</subject><subject>thermophilic microorganisms</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</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><recordid>eNp9kcFu1DAQhi0EotvCA3ABiwOcAh47tuNjtVBaqRISu5wtx7E3KUm82I4EPD0uWQnEoae5fN8_mvkRegHkHRAi3yegBEhFiKoa3qhKPUIb4FxVhCp4jDaESlZR2qgzdJ7SHSFAGy6fojNQVAgGYoN-bHsTjc0uDr9MHsKMg8cGf3E2TO0wmznjfe_iFFI27ejwB9ebMRzcbJLDNymMJrsO-xgmnHuHr0PGu2Mc5sNJO_ZDsXbL6MMY2iXhHL6FzgzDM_TEmzG556d5gfZXH_fb6-r286eb7eVtZWvKc2WJ99zVXVO7tuaCcQ7UW9G0lskWLOsIY9KZpmulFcTUjXUClFeUyM4wyi7Q2zX2GMP3xaWspyFZN45mdmFJWrKaCMUZK-SbB0kKVNSg6gK-_g-8C0ucyxEalAQQQpICwQrZGFKKzuvylcnEnxqIvi9Pr-XpUp6-L0-r4rw8BS_t5Lq_xqmtAtAVSH9e7OI_mx9IfbVK3gRtDnFI-uuuQIyAaFQtGfsN6FyvFQ</recordid><startdate>20091101</startdate><enddate>20091101</enddate><creator>Bachas-Daunert, Philip G</creator><creator>Law, Stacy A</creator><creator>Wei, Yinan</creator><general>New York : Humana Press Inc</general><general>Humana Press Inc</general><general>Springer Nature B.V</general><scope>FBQ</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>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</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>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</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>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7QL</scope><scope>7QO</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20091101</creationdate><title>Characterization of a Recombinant Thermostable Dehalogenase Isolated from the Hot Spring Thermophile Sulfolobus tokodaii</title><author>Bachas-Daunert, Philip G ; Law, Stacy A ; Wei, Yinan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-c0ff5e4d84eb45635512fc68bc37b1c3d0337ea8db7c60a48ce619f9207da323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Bacteria</topic><topic>Biochemistry</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Cloning</topic><topic>Cloning, Molecular - methods</topic><topic>Crenarchaeota</topic><topic>dehalogenase</topic><topic>dehalogenation</topic><topic>E coli</topic><topic>Enzyme Activation</topic><topic>enzyme activity</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - physiology</topic><topic>gene expression</topic><topic>Hot springs</topic><topic>Hot Springs - microbiology</topic><topic>Hydrolases - chemistry</topic><topic>Hydrolases - genetics</topic><topic>Hydrolases - metabolism</topic><topic>molecular cloning</topic><topic>Protein Engineering - methods</topic><topic>provenance</topic><topic>recombinant proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>springs (water)</topic><topic>Sulfolobus - enzymology</topic><topic>Sulfolobus - genetics</topic><topic>Sulfolobus - metabolism</topic><topic>Sulfolobus tokodaii</topic><topic>Temperature</topic><topic>thermal stability</topic><topic>thermophilic microorganisms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bachas-Daunert, Philip G</creatorcontrib><creatorcontrib>Law, Stacy A</creatorcontrib><creatorcontrib>Wei, Yinan</creatorcontrib><collection>AGRIS</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>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</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 Pharma Collection</collection><collection>Technology Research Database</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 (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</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>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>Biotechnology and BioEngineering Abstracts</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>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bachas-Daunert, Philip G</au><au>Law, Stacy A</au><au>Wei, Yinan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a Recombinant Thermostable Dehalogenase Isolated from the Hot Spring Thermophile Sulfolobus tokodaii</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2009-11-01</date><risdate>2009</risdate><volume>159</volume><issue>2</issue><spage>382</spage><epage>393</epage><pages>382-393</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>A putative dehalogenase, l-HADST, from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of l-2-haloacids with similar levels of activity as its homolog from mesophiles. l-HADST remains fully active after being incubated for 4 h at 70 °C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.</abstract><cop>New York</cop><pub>New York : Humana Press Inc</pub><pmid>19266316</pmid><doi>10.1007/s12010-009-8589-9</doi><tpages>12</tpages></addata></record> |
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| subjects | Bacteria Biochemistry Biotechnology Chemistry Chemistry and Materials Science Cloning Cloning, Molecular - methods Crenarchaeota dehalogenase dehalogenation E coli Enzyme Activation enzyme activity Enzyme Stability Enzymes Escherichia coli Escherichia coli - physiology gene expression Hot springs Hot Springs - microbiology Hydrolases - chemistry Hydrolases - genetics Hydrolases - metabolism molecular cloning Protein Engineering - methods provenance recombinant proteins Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism springs (water) Sulfolobus - enzymology Sulfolobus - genetics Sulfolobus - metabolism Sulfolobus tokodaii Temperature thermal stability thermophilic microorganisms |
| title | Characterization of a Recombinant Thermostable Dehalogenase Isolated from the Hot Spring Thermophile Sulfolobus tokodaii |
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