Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1
The thermophilic bacterium Thermoanaerobacterium saccharolyticum NTOU1 was isolated from a hydrothermal vent near Taiwan. A complete gene, xynFCB, encoding 413 amino acids and belonging to the glycosyl hydrolyase family 10 (GH10) of xylanases was identified from the genome sequence of strain NTOU1....
Gespeichert in:
| Veröffentlicht in: | Process biochemistry (1991) 2011-06, Vol.46 (6), p.1257-1263 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1263 |
|---|---|
| container_issue | 6 |
| container_start_page | 1257 |
| container_title | Process biochemistry (1991) |
| container_volume | 46 |
| creator | Hung, Kuo-Sheng Liu, Shiu-Mei Tzou, Wen-Shyong Lin, Fu-Pang Pan, Chorng-Liang Fang, Tsuei-Yun Sun, Kuang-Hui Tang, Shye-Jye |
| description | The thermophilic bacterium Thermoanaerobacterium saccharolyticum NTOU1 was isolated from a hydrothermal vent near Taiwan. A complete gene, xynFCB, encoding 413 amino acids and belonging to the glycosyl hydrolyase family 10 (GH10) of xylanases was identified from the genome sequence of strain NTOU1. This gene was cloned and expressed in Escherichia coli BL21(DE3)pLys. The enzyme was purified by Nickel affinity chromatography and had a molecular mass of 50kDa. XynFCB hydrolyzed xylan with optimal activity at 63°C and pH 6.4, and preferentially hydrolyzed oat spelt xylan. The enzyme retained more 70% of its activity between the pH values of 5.5–8.0, and its half-life was 55min at 65°C. XynFCB displayed enhanced activity in a dose-dependent manner in 0–12.5% (w/v) NaCl. Optimal activity was observed in 12.5% (w/v) NaCl, while 67% of its activity was retained in 15% (w/v) NaCl after a 48-h incubation. This is the first report describing the cloning, expression and characterization of a thermostable, halophilic xylanase from T. saccharolyticum. |
| doi_str_mv | 10.1016/j.procbio.2011.02.009 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_869589290</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1359511311000663</els_id><sourcerecordid>869589290</sourcerecordid><originalsourceid>FETCH-LOGICAL-c431t-8d740539f89e9aab924ae33b0d224ca69f560f2e8996aa8666a7534eaa9f14d63</originalsourceid><addsrcrecordid>eNqFkM1u1DAURiMEEqXtI1R4x4aEazvx2CuERtAiVe2CmbV149wwHiXxYGcqhifgsfGQSixZ-Ufnu1ffKYobDhUHrj7sq0MMrvWhEsB5BaICMC-KC65XspTC6Jf5LhtTNpzL18WblPYAknMOF8Xv9Q4jupmi_4WzDxMLPUM2hSca2O0dBzbvKI4hzdgO9J7tcAiHnR-8Yz9PA06YiPUxjGeMjRj9RKxd5h1HtvmbzRTF8O83oXN5axhOs3f5_bB53PKr4lWPQ6Lr5_Oy2H75vFnflfePt1_Xn-5LV0s-l7pb1dBI02tDBrE1okaSsoVOiNqhMn2joBekjVGIWimFq0bWhGh6XndKXhbvlrnZ2Y8jpdmOPjkachcKx2S1Mo02wkAmm4V0MaQUqbeH6HPFk-Vgz-Lt3j6Lt2fxFoTN4nPu7ZLrMVj8Hn2y228ZUACwklqLTHxcCMpFnzxFm5ynyVHnI7nZdsH_Z8cfdPCa0w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>869589290</pqid></control><display><type>article</type><title>Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1</title><source>ScienceDirect Journals (5 years ago - present)</source><creator>Hung, Kuo-Sheng ; Liu, Shiu-Mei ; Tzou, Wen-Shyong ; Lin, Fu-Pang ; Pan, Chorng-Liang ; Fang, Tsuei-Yun ; Sun, Kuang-Hui ; Tang, Shye-Jye</creator><creatorcontrib>Hung, Kuo-Sheng ; Liu, Shiu-Mei ; Tzou, Wen-Shyong ; Lin, Fu-Pang ; Pan, Chorng-Liang ; Fang, Tsuei-Yun ; Sun, Kuang-Hui ; Tang, Shye-Jye</creatorcontrib><description>The thermophilic bacterium Thermoanaerobacterium saccharolyticum NTOU1 was isolated from a hydrothermal vent near Taiwan. A complete gene, xynFCB, encoding 413 amino acids and belonging to the glycosyl hydrolyase family 10 (GH10) of xylanases was identified from the genome sequence of strain NTOU1. This gene was cloned and expressed in Escherichia coli BL21(DE3)pLys. The enzyme was purified by Nickel affinity chromatography and had a molecular mass of 50kDa. XynFCB hydrolyzed xylan with optimal activity at 63°C and pH 6.4, and preferentially hydrolyzed oat spelt xylan. The enzyme retained more 70% of its activity between the pH values of 5.5–8.0, and its half-life was 55min at 65°C. XynFCB displayed enhanced activity in a dose-dependent manner in 0–12.5% (w/v) NaCl. Optimal activity was observed in 12.5% (w/v) NaCl, while 67% of its activity was retained in 15% (w/v) NaCl after a 48-h incubation. This is the first report describing the cloning, expression and characterization of a thermostable, halophilic xylanase from T. saccharolyticum.</description><identifier>ISSN: 1359-5113</identifier><identifier>EISSN: 1873-3298</identifier><identifier>DOI: 10.1016/j.procbio.2011.02.009</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>affinity chromatography ; Amino acids ; dose response ; Enzymes ; Escherichia coli ; Genes ; Genomes ; GH10 xylanases ; half life ; Halophilism ; hydrolysis ; molecular weight ; nickel ; nucleotide sequences ; oats ; Optimization ; Pyrosequencing ; sodium chloride ; thermal stability ; Thermoanaerobacterium saccharolyticum ; Thermoanaerobacterium saccharolyticum NTOU1 ; thermophilic bacteria ; Thermostable xylanase ; xylan ; Xylanase ; xylanases</subject><ispartof>Process biochemistry (1991), 2011-06, Vol.46 (6), p.1257-1263</ispartof><rights>2011 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-8d740539f89e9aab924ae33b0d224ca69f560f2e8996aa8666a7534eaa9f14d63</citedby><cites>FETCH-LOGICAL-c431t-8d740539f89e9aab924ae33b0d224ca69f560f2e8996aa8666a7534eaa9f14d63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.procbio.2011.02.009$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids></links><search><creatorcontrib>Hung, Kuo-Sheng</creatorcontrib><creatorcontrib>Liu, Shiu-Mei</creatorcontrib><creatorcontrib>Tzou, Wen-Shyong</creatorcontrib><creatorcontrib>Lin, Fu-Pang</creatorcontrib><creatorcontrib>Pan, Chorng-Liang</creatorcontrib><creatorcontrib>Fang, Tsuei-Yun</creatorcontrib><creatorcontrib>Sun, Kuang-Hui</creatorcontrib><creatorcontrib>Tang, Shye-Jye</creatorcontrib><title>Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1</title><title>Process biochemistry (1991)</title><description>The thermophilic bacterium Thermoanaerobacterium saccharolyticum NTOU1 was isolated from a hydrothermal vent near Taiwan. A complete gene, xynFCB, encoding 413 amino acids and belonging to the glycosyl hydrolyase family 10 (GH10) of xylanases was identified from the genome sequence of strain NTOU1. This gene was cloned and expressed in Escherichia coli BL21(DE3)pLys. The enzyme was purified by Nickel affinity chromatography and had a molecular mass of 50kDa. XynFCB hydrolyzed xylan with optimal activity at 63°C and pH 6.4, and preferentially hydrolyzed oat spelt xylan. The enzyme retained more 70% of its activity between the pH values of 5.5–8.0, and its half-life was 55min at 65°C. XynFCB displayed enhanced activity in a dose-dependent manner in 0–12.5% (w/v) NaCl. Optimal activity was observed in 12.5% (w/v) NaCl, while 67% of its activity was retained in 15% (w/v) NaCl after a 48-h incubation. This is the first report describing the cloning, expression and characterization of a thermostable, halophilic xylanase from T. saccharolyticum.</description><subject>affinity chromatography</subject><subject>Amino acids</subject><subject>dose response</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Genes</subject><subject>Genomes</subject><subject>GH10 xylanases</subject><subject>half life</subject><subject>Halophilism</subject><subject>hydrolysis</subject><subject>molecular weight</subject><subject>nickel</subject><subject>nucleotide sequences</subject><subject>oats</subject><subject>Optimization</subject><subject>Pyrosequencing</subject><subject>sodium chloride</subject><subject>thermal stability</subject><subject>Thermoanaerobacterium saccharolyticum</subject><subject>Thermoanaerobacterium saccharolyticum NTOU1</subject><subject>thermophilic bacteria</subject><subject>Thermostable xylanase</subject><subject>xylan</subject><subject>Xylanase</subject><subject>xylanases</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNqFkM1u1DAURiMEEqXtI1R4x4aEazvx2CuERtAiVe2CmbV149wwHiXxYGcqhifgsfGQSixZ-Ufnu1ffKYobDhUHrj7sq0MMrvWhEsB5BaICMC-KC65XspTC6Jf5LhtTNpzL18WblPYAknMOF8Xv9Q4jupmi_4WzDxMLPUM2hSca2O0dBzbvKI4hzdgO9J7tcAiHnR-8Yz9PA06YiPUxjGeMjRj9RKxd5h1HtvmbzRTF8O83oXN5axhOs3f5_bB53PKr4lWPQ6Lr5_Oy2H75vFnflfePt1_Xn-5LV0s-l7pb1dBI02tDBrE1okaSsoVOiNqhMn2joBekjVGIWimFq0bWhGh6XndKXhbvlrnZ2Y8jpdmOPjkachcKx2S1Mo02wkAmm4V0MaQUqbeH6HPFk-Vgz-Lt3j6Lt2fxFoTN4nPu7ZLrMVj8Hn2y228ZUACwklqLTHxcCMpFnzxFm5ynyVHnI7nZdsH_Z8cfdPCa0w</recordid><startdate>20110601</startdate><enddate>20110601</enddate><creator>Hung, Kuo-Sheng</creator><creator>Liu, Shiu-Mei</creator><creator>Tzou, Wen-Shyong</creator><creator>Lin, Fu-Pang</creator><creator>Pan, Chorng-Liang</creator><creator>Fang, Tsuei-Yun</creator><creator>Sun, Kuang-Hui</creator><creator>Tang, Shye-Jye</creator><general>Elsevier Ltd</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>L7M</scope></search><sort><creationdate>20110601</creationdate><title>Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1</title><author>Hung, Kuo-Sheng ; Liu, Shiu-Mei ; Tzou, Wen-Shyong ; Lin, Fu-Pang ; Pan, Chorng-Liang ; Fang, Tsuei-Yun ; Sun, Kuang-Hui ; Tang, Shye-Jye</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-8d740539f89e9aab924ae33b0d224ca69f560f2e8996aa8666a7534eaa9f14d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>affinity chromatography</topic><topic>Amino acids</topic><topic>dose response</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Genes</topic><topic>Genomes</topic><topic>GH10 xylanases</topic><topic>half life</topic><topic>Halophilism</topic><topic>hydrolysis</topic><topic>molecular weight</topic><topic>nickel</topic><topic>nucleotide sequences</topic><topic>oats</topic><topic>Optimization</topic><topic>Pyrosequencing</topic><topic>sodium chloride</topic><topic>thermal stability</topic><topic>Thermoanaerobacterium saccharolyticum</topic><topic>Thermoanaerobacterium saccharolyticum NTOU1</topic><topic>thermophilic bacteria</topic><topic>Thermostable xylanase</topic><topic>xylan</topic><topic>Xylanase</topic><topic>xylanases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hung, Kuo-Sheng</creatorcontrib><creatorcontrib>Liu, Shiu-Mei</creatorcontrib><creatorcontrib>Tzou, Wen-Shyong</creatorcontrib><creatorcontrib>Lin, Fu-Pang</creatorcontrib><creatorcontrib>Pan, Chorng-Liang</creatorcontrib><creatorcontrib>Fang, Tsuei-Yun</creatorcontrib><creatorcontrib>Sun, Kuang-Hui</creatorcontrib><creatorcontrib>Tang, Shye-Jye</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hung, Kuo-Sheng</au><au>Liu, Shiu-Mei</au><au>Tzou, Wen-Shyong</au><au>Lin, Fu-Pang</au><au>Pan, Chorng-Liang</au><au>Fang, Tsuei-Yun</au><au>Sun, Kuang-Hui</au><au>Tang, Shye-Jye</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2011-06-01</date><risdate>2011</risdate><volume>46</volume><issue>6</issue><spage>1257</spage><epage>1263</epage><pages>1257-1263</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>The thermophilic bacterium Thermoanaerobacterium saccharolyticum NTOU1 was isolated from a hydrothermal vent near Taiwan. A complete gene, xynFCB, encoding 413 amino acids and belonging to the glycosyl hydrolyase family 10 (GH10) of xylanases was identified from the genome sequence of strain NTOU1. This gene was cloned and expressed in Escherichia coli BL21(DE3)pLys. The enzyme was purified by Nickel affinity chromatography and had a molecular mass of 50kDa. XynFCB hydrolyzed xylan with optimal activity at 63°C and pH 6.4, and preferentially hydrolyzed oat spelt xylan. The enzyme retained more 70% of its activity between the pH values of 5.5–8.0, and its half-life was 55min at 65°C. XynFCB displayed enhanced activity in a dose-dependent manner in 0–12.5% (w/v) NaCl. Optimal activity was observed in 12.5% (w/v) NaCl, while 67% of its activity was retained in 15% (w/v) NaCl after a 48-h incubation. This is the first report describing the cloning, expression and characterization of a thermostable, halophilic xylanase from T. saccharolyticum.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.procbio.2011.02.009</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1359-5113 |
| ispartof | Process biochemistry (1991), 2011-06, Vol.46 (6), p.1257-1263 |
| issn | 1359-5113 1873-3298 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_869589290 |
| source | ScienceDirect Journals (5 years ago - present) |
| subjects | affinity chromatography Amino acids dose response Enzymes Escherichia coli Genes Genomes GH10 xylanases half life Halophilism hydrolysis molecular weight nickel nucleotide sequences oats Optimization Pyrosequencing sodium chloride thermal stability Thermoanaerobacterium saccharolyticum Thermoanaerobacterium saccharolyticum NTOU1 thermophilic bacteria Thermostable xylanase xylan Xylanase xylanases |
| title | Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T18%3A30%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20a%20novel%20GH10%20thermostable,%20halophilic%20xylanase%20from%20the%20marine%20bacterium%20Thermoanaerobacterium%20saccharolyticum%20NTOU1&rft.jtitle=Process%20biochemistry%20(1991)&rft.au=Hung,%20Kuo-Sheng&rft.date=2011-06-01&rft.volume=46&rft.issue=6&rft.spage=1257&rft.epage=1263&rft.pages=1257-1263&rft.issn=1359-5113&rft.eissn=1873-3298&rft_id=info:doi/10.1016/j.procbio.2011.02.009&rft_dat=%3Cproquest_cross%3E869589290%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=869589290&rft_id=info:pmid/&rft_els_id=S1359511311000663&rfr_iscdi=true |