Characterization, gene cloning, and expression of a novel xylanase XYNB from Streptomyces olivaceoviridis A1
A novel xylanase XYNB from S treptomyces olivaceoviridis A1 was purified to electrophoretic homogeneity with the specific activity of 2869.78 U/mg, by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified XYNB was further characterized. The optimal pH and tem...
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| Veröffentlicht in: | Aquaculture 2007-07, Vol.267 (1), p.328-334 |
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| creator | Wang, Yaru Zhang, Honglian He, Yongzhi Luo, Huiying Yao, Bin |
| description | A novel xylanase XYNB from S
treptomyces olivaceoviridis A1 was purified to electrophoretic homogeneity with the specific activity of 2869.78 U/mg, by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified XYNB was further characterized. The optimal pH and temperature for XYNB activity are 5.2 and 60 °C, respectively. Metal cations, EDTA and SDS had no or little effect on enzyme activity. The gene
xynB coding mature protein of XYNB was cloned by degenerated PCR, which consisted of 576 bp and encoded 191 amino acid residues. The putative molecular weight of XYNB is about 20.8 kD. The
xynB was expressed actively in both
Escherichia coli and
Pichia pastoris. In a 3 L fermentor, the expressed xylanase protein was accumulated up to 7 mg/mL in recombinant
P. pastoris, and the xylanase activity exceeded 15,000 IU/mL. XYNB can be potentially utilized in fish feed industry. |
| doi_str_mv | 10.1016/j.aquaculture.2007.03.005 |
| format | Article |
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treptomyces olivaceoviridis A1 was purified to electrophoretic homogeneity with the specific activity of 2869.78 U/mg, by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified XYNB was further characterized. The optimal pH and temperature for XYNB activity are 5.2 and 60 °C, respectively. Metal cations, EDTA and SDS had no or little effect on enzyme activity. The gene
xynB coding mature protein of XYNB was cloned by degenerated PCR, which consisted of 576 bp and encoded 191 amino acid residues. The putative molecular weight of XYNB is about 20.8 kD. The
xynB was expressed actively in both
Escherichia coli and
Pichia pastoris. In a 3 L fermentor, the expressed xylanase protein was accumulated up to 7 mg/mL in recombinant
P. pastoris, and the xylanase activity exceeded 15,000 IU/mL. XYNB can be potentially utilized in fish feed industry.</description><identifier>ISSN: 0044-8486</identifier><identifier>EISSN: 1873-5622</identifier><identifier>DOI: 10.1016/j.aquaculture.2007.03.005</identifier><identifier>CODEN: AQCLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>amino acid sequences ; Ammonia ; Animal aquaculture ; Animal productions ; bacterial proteins ; Biological and medical sciences ; Characterization ; Cloning ; E coli ; endo-1,4-beta-xylanase ; Escherichia coli ; Expression ; Fundamental and applied biological sciences. Psychology ; Gene cloning ; Gene expression ; gene expression regulation ; General aspects ; Genes ; molecular sequence data ; Pichia pastoris ; soil bacteria ; Streptomyces olivaceoviridis ; Streptomyces olivaceoviridis A1 ; Xylanase ; XYNB</subject><ispartof>Aquaculture, 2007-07, Vol.267 (1), p.328-334</ispartof><rights>2007 Elsevier B.V.</rights><rights>2007 INIST-CNRS</rights><rights>Copyright Elsevier Sequoia S.A. Jul 3, 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-b08124b19ae01f51dedfbce44279c045c2f58ea6b17b6fb8e2fae98f1a84df0e3</citedby><cites>FETCH-LOGICAL-c499t-b08124b19ae01f51dedfbce44279c045c2f58ea6b17b6fb8e2fae98f1a84df0e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.aquaculture.2007.03.005$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>309,310,314,780,784,789,790,3550,23930,23931,25140,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18919660$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yaru</creatorcontrib><creatorcontrib>Zhang, Honglian</creatorcontrib><creatorcontrib>He, Yongzhi</creatorcontrib><creatorcontrib>Luo, Huiying</creatorcontrib><creatorcontrib>Yao, Bin</creatorcontrib><title>Characterization, gene cloning, and expression of a novel xylanase XYNB from Streptomyces olivaceoviridis A1</title><title>Aquaculture</title><description>A novel xylanase XYNB from S
treptomyces olivaceoviridis A1 was purified to electrophoretic homogeneity with the specific activity of 2869.78 U/mg, by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified XYNB was further characterized. The optimal pH and temperature for XYNB activity are 5.2 and 60 °C, respectively. Metal cations, EDTA and SDS had no or little effect on enzyme activity. The gene
xynB coding mature protein of XYNB was cloned by degenerated PCR, which consisted of 576 bp and encoded 191 amino acid residues. The putative molecular weight of XYNB is about 20.8 kD. The
xynB was expressed actively in both
Escherichia coli and
Pichia pastoris. In a 3 L fermentor, the expressed xylanase protein was accumulated up to 7 mg/mL in recombinant
P. pastoris, and the xylanase activity exceeded 15,000 IU/mL. XYNB can be potentially utilized in fish feed industry.</description><subject>amino acid sequences</subject><subject>Ammonia</subject><subject>Animal aquaculture</subject><subject>Animal productions</subject><subject>bacterial proteins</subject><subject>Biological and medical sciences</subject><subject>Characterization</subject><subject>Cloning</subject><subject>E coli</subject><subject>endo-1,4-beta-xylanase</subject><subject>Escherichia coli</subject><subject>Expression</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene cloning</subject><subject>Gene expression</subject><subject>gene expression regulation</subject><subject>General aspects</subject><subject>Genes</subject><subject>molecular sequence data</subject><subject>Pichia pastoris</subject><subject>soil bacteria</subject><subject>Streptomyces olivaceoviridis</subject><subject>Streptomyces olivaceoviridis A1</subject><subject>Xylanase</subject><subject>XYNB</subject><issn>0044-8486</issn><issn>1873-5622</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqNkcFu1DAQhiMEEkvhGTBIcOqGsRM7zrGsaEGq4FAqwcmaOOPFq6y9tZNVl6cny1YCceI0B3_-59P8RfGKQ8mBq3ebEu8mtNMwTolKAdCUUJUA8lGx4LqpllIJ8bhYANT1UtdaPS2e5bwBAKUkXxTD6gcmtCMl_xNHH8M5W1MgZocYfFifMww9o_tdopznVxYdQxbingZ2fxgwYCb27fvn98yluGU3Y6LdGLcHS5nFwe_RUtz75Huf2QV_XjxxOGR68TDPitvLD19XH5fXX64-rS6ul7Zu23HZgeai7niLBNxJ3lPvOkt1LZrWQi2tcFITqo43nXKdJuGQWu046rp3QNVZ8faUu0vxbqI8mq3PlobZl-KUDW9bLXWlZvD1P-AmTinMbkZA3VSNBDlD7QmyKeacyJld8ltMB8PBHEswG_NXCeZYgoHKwO-_bx4WYLY4uITB-vwnQLe8VQpm7uWJcxgNrtPM3N4I4NWcpaVQR9XViaD5cHtPyWTrKVjqfSI7mj76__D5BbcdroI</recordid><startdate>20070703</startdate><enddate>20070703</enddate><creator>Wang, Yaru</creator><creator>Zhang, Honglian</creator><creator>He, Yongzhi</creator><creator>Luo, Huiying</creator><creator>Yao, Bin</creator><general>Elsevier B.V</general><general>Elsevier Science</general><general>Elsevier Sequoia S.A</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QR</scope><scope>7ST</scope><scope>7TN</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H94</scope><scope>H95</scope><scope>H98</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7QO</scope><scope>RC3</scope></search><sort><creationdate>20070703</creationdate><title>Characterization, gene cloning, and expression of a novel xylanase XYNB from Streptomyces olivaceoviridis A1</title><author>Wang, Yaru ; Zhang, Honglian ; He, Yongzhi ; Luo, Huiying ; Yao, Bin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-b08124b19ae01f51dedfbce44279c045c2f58ea6b17b6fb8e2fae98f1a84df0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>amino acid sequences</topic><topic>Ammonia</topic><topic>Animal aquaculture</topic><topic>Animal productions</topic><topic>bacterial proteins</topic><topic>Biological and medical sciences</topic><topic>Characterization</topic><topic>Cloning</topic><topic>E coli</topic><topic>endo-1,4-beta-xylanase</topic><topic>Escherichia coli</topic><topic>Expression</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene cloning</topic><topic>Gene expression</topic><topic>gene expression regulation</topic><topic>General aspects</topic><topic>Genes</topic><topic>molecular sequence data</topic><topic>Pichia pastoris</topic><topic>soil bacteria</topic><topic>Streptomyces olivaceoviridis</topic><topic>Streptomyces olivaceoviridis A1</topic><topic>Xylanase</topic><topic>XYNB</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Yaru</creatorcontrib><creatorcontrib>Zhang, Honglian</creatorcontrib><creatorcontrib>He, Yongzhi</creatorcontrib><creatorcontrib>Luo, Huiying</creatorcontrib><creatorcontrib>Yao, Bin</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Environment Abstracts</collection><collection>Oceanic Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Aquaculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Yaru</au><au>Zhang, Honglian</au><au>He, Yongzhi</au><au>Luo, Huiying</au><au>Yao, Bin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization, gene cloning, and expression of a novel xylanase XYNB from Streptomyces olivaceoviridis A1</atitle><jtitle>Aquaculture</jtitle><date>2007-07-03</date><risdate>2007</risdate><volume>267</volume><issue>1</issue><spage>328</spage><epage>334</epage><pages>328-334</pages><issn>0044-8486</issn><eissn>1873-5622</eissn><coden>AQCLAL</coden><abstract>A novel xylanase XYNB from S
treptomyces olivaceoviridis A1 was purified to electrophoretic homogeneity with the specific activity of 2869.78 U/mg, by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified XYNB was further characterized. The optimal pH and temperature for XYNB activity are 5.2 and 60 °C, respectively. Metal cations, EDTA and SDS had no or little effect on enzyme activity. The gene
xynB coding mature protein of XYNB was cloned by degenerated PCR, which consisted of 576 bp and encoded 191 amino acid residues. The putative molecular weight of XYNB is about 20.8 kD. The
xynB was expressed actively in both
Escherichia coli and
Pichia pastoris. In a 3 L fermentor, the expressed xylanase protein was accumulated up to 7 mg/mL in recombinant
P. pastoris, and the xylanase activity exceeded 15,000 IU/mL. XYNB can be potentially utilized in fish feed industry.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/j.aquaculture.2007.03.005</doi><tpages>7</tpages></addata></record> |
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| subjects | amino acid sequences Ammonia Animal aquaculture Animal productions bacterial proteins Biological and medical sciences Characterization Cloning E coli endo-1,4-beta-xylanase Escherichia coli Expression Fundamental and applied biological sciences. Psychology Gene cloning Gene expression gene expression regulation General aspects Genes molecular sequence data Pichia pastoris soil bacteria Streptomyces olivaceoviridis Streptomyces olivaceoviridis A1 Xylanase XYNB |
| title | Characterization, gene cloning, and expression of a novel xylanase XYNB from Streptomyces olivaceoviridis A1 |
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