Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli
A novel microbial transglutaminase (TGase) from the cultural filtrate of Streptomyces netropsis BCRC 12429 (Sn) was purified. The specific activity of the purified TGase was 18.2 U/mg protein with an estimated molecular mass of 38 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis anal...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2008-12, Vol.81 (3), p.523-532 |
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| creator | Yu, Yu-Jen Wu, Shih-Cheng Chan, Hung-Hsiang Chen, Yu-Cheng Chen, Zong-Yu Yang, Ming-Te |
| description | A novel microbial transglutaminase (TGase) from the cultural filtrate of Streptomyces netropsis BCRC 12429 (Sn) was purified. The specific activity of the purified TGase was 18.2 U/mg protein with an estimated molecular mass of 38 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The TGase gene of S. netropsis was cloned and an open reading frame of 1,242 bp encoding a protein of 413 amino acids was identified. The Sn TGase was synthesized as a precursor protein with a preproregion of 82 amino acid residues. The deduced amino acid sequence of the mature S. netropsis TGase shares 78.9-89.6% identities with TGases from Streptomyces spp. A high level of soluble Sn TGase with its N-terminal propeptide fused with thioredoxin was expressed in E. coli. A simple and efficient process was applied to convert the purified recombinant protein into an active enzyme and showed activity equivalent to the authentic mature TGase. |
| doi_str_mv | 10.1007/s00253-008-1688-7 |
| format | Article |
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The specific activity of the purified TGase was 18.2 U/mg protein with an estimated molecular mass of 38 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The TGase gene of S. netropsis was cloned and an open reading frame of 1,242 bp encoding a protein of 413 amino acids was identified. The Sn TGase was synthesized as a precursor protein with a preproregion of 82 amino acid residues. The deduced amino acid sequence of the mature S. netropsis TGase shares 78.9-89.6% identities with TGases from Streptomyces spp. A high level of soluble Sn TGase with its N-terminal propeptide fused with thioredoxin was expressed in E. coli. A simple and efficient process was applied to convert the purified recombinant protein into an active enzyme and showed activity equivalent to the authentic mature TGase.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-008-1688-7</identifier><identifier>PMID: 18810430</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Amino Acid Sequence ; Amino acids ; Applied Genetics and Molecular Biotechnology ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Cloning ; Cloning, Molecular ; E coli ; Enzyme Stability ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Filtrate ; Fundamental and applied biological sciences. Psychology ; Fusion protein ; Gene Expression ; Genetic engineering ; Life Sciences ; Microbial Genetics and Genomics ; Microbial transglutaminase ; Microbiology ; Molecular Sequence Data ; Molecular Weight ; Physiology ; Plasmids ; Proregion ; Proteins ; R&D ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Research & development ; Streptomyces ; Streptomyces - enzymology ; Streptomyces netropsis ; Studies ; Thioredoxin ; Transglutaminases - chemistry ; Transglutaminases - genetics ; Transglutaminases - isolation & purification ; Transglutaminases - metabolism</subject><ispartof>Applied microbiology and biotechnology, 2008-12, Vol.81 (3), p.523-532</ispartof><rights>Springer-Verlag 2008</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-d0b2386668744952952489703f540262f21626da3b8b7c0ca8dfc331a719c5323</citedby><cites>FETCH-LOGICAL-c520t-d0b2386668744952952489703f540262f21626da3b8b7c0ca8dfc331a719c5323</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/s00253-008-1688-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-008-1688-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21017834$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18810430$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, Yu-Jen</creatorcontrib><creatorcontrib>Wu, Shih-Cheng</creatorcontrib><creatorcontrib>Chan, Hung-Hsiang</creatorcontrib><creatorcontrib>Chen, Yu-Cheng</creatorcontrib><creatorcontrib>Chen, Zong-Yu</creatorcontrib><creatorcontrib>Yang, Ming-Te</creatorcontrib><title>Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>A novel microbial transglutaminase (TGase) from the cultural filtrate of Streptomyces netropsis BCRC 12429 (Sn) was purified. The specific activity of the purified TGase was 18.2 U/mg protein with an estimated molecular mass of 38 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The TGase gene of S. netropsis was cloned and an open reading frame of 1,242 bp encoding a protein of 413 amino acids was identified. The Sn TGase was synthesized as a precursor protein with a preproregion of 82 amino acid residues. The deduced amino acid sequence of the mature S. netropsis TGase shares 78.9-89.6% identities with TGases from Streptomyces spp. A high level of soluble Sn TGase with its N-terminal propeptide fused with thioredoxin was expressed in E. coli. A simple and efficient process was applied to convert the purified recombinant protein into an active enzyme and showed activity equivalent to the authentic mature TGase.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Applied Genetics and Molecular Biotechnology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>E coli</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Filtrate</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fusion protein</subject><subject>Gene Expression</subject><subject>Genetic engineering</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbial transglutaminase</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Physiology</subject><subject>Plasmids</subject><subject>Proregion</subject><subject>Proteins</subject><subject>R&D</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Research & development</subject><subject>Streptomyces</subject><subject>Streptomyces - enzymology</subject><subject>Streptomyces netropsis</subject><subject>Studies</subject><subject>Thioredoxin</subject><subject>Transglutaminases - chemistry</subject><subject>Transglutaminases - genetics</subject><subject>Transglutaminases - isolation & purification</subject><subject>Transglutaminases - metabolism</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</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>eNqFkU9rFTEUxYMo9ln9AG40CLobvbmZSTJLKfUPFLqoXYdMJnlNmUmeyYzQb28e87DgQiEQSH7n5NwcQl4z-MgA5KcCgB1vAFTDhFKNfEJ2rOXYgGDtU7IDJrtGdr06Iy9KuQdgqIR4Ts6YUgxaDjvir3-5fMhpXO0SUqTJ05KmdZgczc6meQjRxIUu2cSyn9bFzPWgOOpzmunNkt1hSfODdYVGt-R0KKHQEOllsXcuB3sXDLVpCi_JM2-m4l6d9nNy--Xyx8W35ur66_eLz1eN7RCWZoQBeY0olGzbvsO6WtVL4L5rAQV6ZALFaPigBmnBGjV6yzkzkvW248jPyYfNt470c3Vl0XMo1k2TiS6tRYteqp7j_0Fk2Cneqgq--wu8T2uOdQiNNZ_kQh7d2AbZnErJzutDDrPJD5qBPlalt6p0rUofq9Kyat6cjNdhduOj4tRNBd6fAFOsmXytwIbyh0NW660RK4cbV-pV3Lv8mPBfr7_dRN4kbfa5Gt_eIDAOrBOo6lf-BgNatGo</recordid><startdate>20081201</startdate><enddate>20081201</enddate><creator>Yu, Yu-Jen</creator><creator>Wu, Shih-Cheng</creator><creator>Chan, Hung-Hsiang</creator><creator>Chen, Yu-Cheng</creator><creator>Chen, Zong-Yu</creator><creator>Yang, Ming-Te</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</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>8FL</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>20081201</creationdate><title>Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli</title><author>Yu, Yu-Jen ; Wu, Shih-Cheng ; Chan, Hung-Hsiang ; Chen, Yu-Cheng ; Chen, Zong-Yu ; Yang, Ming-Te</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-d0b2386668744952952489703f540262f21626da3b8b7c0ca8dfc331a719c5323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Applied Genetics and Molecular Biotechnology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>E coli</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Filtrate</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fusion protein</topic><topic>Gene Expression</topic><topic>Genetic engineering</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbial transglutaminase</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Physiology</topic><topic>Plasmids</topic><topic>Proregion</topic><topic>Proteins</topic><topic>R&D</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Research & development</topic><topic>Streptomyces</topic><topic>Streptomyces - enzymology</topic><topic>Streptomyces netropsis</topic><topic>Studies</topic><topic>Thioredoxin</topic><topic>Transglutaminases - chemistry</topic><topic>Transglutaminases - genetics</topic><topic>Transglutaminases - isolation & purification</topic><topic>Transglutaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, Yu-Jen</creatorcontrib><creatorcontrib>Wu, Shih-Cheng</creatorcontrib><creatorcontrib>Chan, Hung-Hsiang</creatorcontrib><creatorcontrib>Chen, Yu-Cheng</creatorcontrib><creatorcontrib>Chen, Zong-Yu</creatorcontrib><creatorcontrib>Yang, Ming-Te</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Access via ABI/INFORM (ProQuest)</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</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>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</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>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</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>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, Yu-Jen</au><au>Wu, Shih-Cheng</au><au>Chan, Hung-Hsiang</au><au>Chen, Yu-Cheng</au><au>Chen, Zong-Yu</au><au>Yang, Ming-Te</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2008-12-01</date><risdate>2008</risdate><volume>81</volume><issue>3</issue><spage>523</spage><epage>532</epage><pages>523-532</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>A novel microbial transglutaminase (TGase) from the cultural filtrate of Streptomyces netropsis BCRC 12429 (Sn) was purified. The specific activity of the purified TGase was 18.2 U/mg protein with an estimated molecular mass of 38 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The TGase gene of S. netropsis was cloned and an open reading frame of 1,242 bp encoding a protein of 413 amino acids was identified. The Sn TGase was synthesized as a precursor protein with a preproregion of 82 amino acid residues. The deduced amino acid sequence of the mature S. netropsis TGase shares 78.9-89.6% identities with TGases from Streptomyces spp. A high level of soluble Sn TGase with its N-terminal propeptide fused with thioredoxin was expressed in E. coli. A simple and efficient process was applied to convert the purified recombinant protein into an active enzyme and showed activity equivalent to the authentic mature TGase.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>18810430</pmid><doi>10.1007/s00253-008-1688-7</doi><tpages>10</tpages></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Applied Genetics and Molecular Biotechnology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Base Sequence Biological and medical sciences Biotechnology Cloning Cloning, Molecular E coli Enzyme Stability Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Filtrate Fundamental and applied biological sciences. Psychology Fusion protein Gene Expression Genetic engineering Life Sciences Microbial Genetics and Genomics Microbial transglutaminase Microbiology Molecular Sequence Data Molecular Weight Physiology Plasmids Proregion Proteins R&D Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Research & development Streptomyces Streptomyces - enzymology Streptomyces netropsis Studies Thioredoxin Transglutaminases - chemistry Transglutaminases - genetics Transglutaminases - isolation & purification Transglutaminases - metabolism |
| title | Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli |
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