Large-scale production and characterization of Bacillus thuringiensis subsp. tenebrionis insecticidal protein from Escherichia coli
Bacillus thuringiensis subsp. tenebrionis insecticidal protein was produced in recombinant Escherichia coli and purified to near homogeneity to provide quantities of protein for safety-assessment studies associated with the registration of transgenic potato plants. The 68-kDa protein is produced nat...
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| Veröffentlicht in: | Applied microbiology and biotechnology 1997-03, Vol.47 (3), p.255-261 |
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| container_title | Applied microbiology and biotechnology |
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| creator | Gustafson, M.E Clayton, R.A Lavrik, P.B Johnson, G.V Leimgruber, R.M Sims, S.R Bartnicki, D.E |
| description | Bacillus thuringiensis subsp. tenebrionis insecticidal protein was produced in recombinant Escherichia coli and purified to near homogeneity to provide quantities of protein for safety-assessment studies associated with the registration of transgenic potato plants. The 68-kDa protein is produced naturally by Bacillus thuringiensis subsp. tenebrionis by translation initiation at an internal initiation site in the native DNA sequence. The gene sequence specific for this truncated protein was expressed in E. coli strain JM 101 and fermented at the 1000-1 scale. The protein accumulated as insoluble inclusion bodies, and was purified by extraction at pH 10.8 with carbonate buffer, selective precipitation at pH 9.0. and differential centrifugation. No chromatography steps were required to produce over 50 g purified protein as a lyophilized powder with a purity greater than 95% and demonstrating full insecticidal activity against Colorado potato beetle larvae. The protein was further characterized to assure identity and suitability for use in safety-assessment studies. |
| doi_str_mv | 10.1007/s002530050923 |
| format | Article |
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The 68-kDa protein is produced naturally by Bacillus thuringiensis subsp. tenebrionis by translation initiation at an internal initiation site in the native DNA sequence. The gene sequence specific for this truncated protein was expressed in E. coli strain JM 101 and fermented at the 1000-1 scale. The protein accumulated as insoluble inclusion bodies, and was purified by extraction at pH 10.8 with carbonate buffer, selective precipitation at pH 9.0. and differential centrifugation. No chromatography steps were required to produce over 50 g purified protein as a lyophilized powder with a purity greater than 95% and demonstrating full insecticidal activity against Colorado potato beetle larvae. The protein was further characterized to assure identity and suitability for use in safety-assessment studies.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s002530050923</identifier><identifier>PMID: 9114517</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>agrochemicals ; Analysis ; Animals ; Bacillus thuringiensis ; Bacillus thuringiensis - chemistry ; Bacillus thuringiensis tenebrionis ; Bacteria ; Bacterial proteins ; Bacterial Proteins - analysis ; Bacterial Proteins - biosynthesis ; Bacterial Proteins - pharmacology ; Bacterial Toxins ; Biological and medical sciences ; Biotechnology ; Butterflies & moths ; Centrifugation ; E coli ; Endotoxins - analysis ; Endotoxins - biosynthesis ; Endotoxins - pharmacology ; Escherichia coli ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Genetic technics ; Hemolysin Proteins ; Larvae ; Methods. Procedures. Technologies ; Microbiological chemistry ; Microbiological synthesis ; Microbiology ; Modification of gene expression level ; Pest Control, Biological ; pesticides ; Potatoes ; Proteins ; Recombinant Proteins - biosynthesis</subject><ispartof>Applied microbiology and biotechnology, 1997-03, Vol.47 (3), p.255-261</ispartof><rights>1997 INIST-CNRS</rights><rights>COPYRIGHT 1997 Springer</rights><rights>Springer-Verlag Berlin Heidelberg 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c529t-5fffc85f424f54a0986abec0c4a4303781a95d7dd886ebe0a3f7bf33f1e22df63</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2625262$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9114517$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gustafson, M.E</creatorcontrib><creatorcontrib>Clayton, R.A</creatorcontrib><creatorcontrib>Lavrik, P.B</creatorcontrib><creatorcontrib>Johnson, G.V</creatorcontrib><creatorcontrib>Leimgruber, R.M</creatorcontrib><creatorcontrib>Sims, S.R</creatorcontrib><creatorcontrib>Bartnicki, D.E</creatorcontrib><title>Large-scale production and characterization of Bacillus thuringiensis subsp. tenebrionis insecticidal protein from Escherichia coli</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><description>Bacillus thuringiensis subsp. tenebrionis insecticidal protein was produced in recombinant Escherichia coli and purified to near homogeneity to provide quantities of protein for safety-assessment studies associated with the registration of transgenic potato plants. The 68-kDa protein is produced naturally by Bacillus thuringiensis subsp. tenebrionis by translation initiation at an internal initiation site in the native DNA sequence. The gene sequence specific for this truncated protein was expressed in E. coli strain JM 101 and fermented at the 1000-1 scale. The protein accumulated as insoluble inclusion bodies, and was purified by extraction at pH 10.8 with carbonate buffer, selective precipitation at pH 9.0. and differential centrifugation. No chromatography steps were required to produce over 50 g purified protein as a lyophilized powder with a purity greater than 95% and demonstrating full insecticidal activity against Colorado potato beetle larvae. The protein was further characterized to assure identity and suitability for use in safety-assessment studies.</description><subject>agrochemicals</subject><subject>Analysis</subject><subject>Animals</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - chemistry</subject><subject>Bacillus thuringiensis tenebrionis</subject><subject>Bacteria</subject><subject>Bacterial proteins</subject><subject>Bacterial Proteins - analysis</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - pharmacology</subject><subject>Bacterial Toxins</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Butterflies & moths</subject><subject>Centrifugation</subject><subject>E coli</subject><subject>Endotoxins - analysis</subject><subject>Endotoxins - biosynthesis</subject><subject>Endotoxins - pharmacology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Hemolysin Proteins</subject><subject>Larvae</subject><subject>Methods. Procedures. Technologies</subject><subject>Microbiological chemistry</subject><subject>Microbiological synthesis</subject><subject>Microbiology</subject><subject>Modification of gene expression level</subject><subject>Pest Control, Biological</subject><subject>pesticides</subject><subject>Potatoes</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqF0sGL1DAUBvAiyjquHj2KRUXx0PUladL0uC6rLgwIrnsOr2nSydJJxqQF9eo_buoMC-NBDyGQ_Ph4bb6ieErgjAA07xIA5QyAQ0vZvWJFakYrEKS-X6yANLxqeCsfFo9SugUgVApxUpy0hNScNKvi1xrjYKqkcTTlLoZ-1pMLvkTfl3qDEfVkovuJfw6DLd-jduM4p3LazNH5wRmfXCrT3KXdWTkZb7qYaT5yPpmcpV2P45I8GedLG8O2vEx6k0P1xmGpw-geFw8sjsk8Oeynxc2Hy68Xn6r1549XF-frSnPaThW31mrJbU1ry2uEVgrsjAZdY82ANZJgy_um76UUpjOAzDadZcwSQ2lvBTst3uxz8zTfZpMmtXVJm3FEb8KcVEtACAmkzfL1P2UjW8EbRv8LiQBJSb3AF3_B2zBHnz9XSVkLzhoBGb3coyG_hnLehik_wJKozhkQJmlLWFZvj5QOfjLfpwHnlNTV9ZdjW-2tjiGlaKzaRbfF-EMRUEt91FF9sn92GHPutqa_04e-5PtXh3tcKmMjeu3SHaOC8rwye75nFoPCIWZyc03zVJD7R3n-H78B0rrVRg</recordid><startdate>19970301</startdate><enddate>19970301</enddate><creator>Gustafson, M.E</creator><creator>Clayton, R.A</creator><creator>Lavrik, P.B</creator><creator>Johnson, G.V</creator><creator>Leimgruber, R.M</creator><creator>Sims, S.R</creator><creator>Bartnicki, D.E</creator><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>ISR</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>AEUYN</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>19970301</creationdate><title>Large-scale production and characterization of Bacillus thuringiensis subsp. tenebrionis insecticidal protein from Escherichia coli</title><author>Gustafson, M.E ; Clayton, R.A ; Lavrik, P.B ; Johnson, G.V ; Leimgruber, R.M ; Sims, S.R ; Bartnicki, D.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c529t-5fffc85f424f54a0986abec0c4a4303781a95d7dd886ebe0a3f7bf33f1e22df63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>agrochemicals</topic><topic>Analysis</topic><topic>Animals</topic><topic>Bacillus thuringiensis</topic><topic>Bacillus thuringiensis - chemistry</topic><topic>Bacillus thuringiensis tenebrionis</topic><topic>Bacteria</topic><topic>Bacterial proteins</topic><topic>Bacterial Proteins - analysis</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - pharmacology</topic><topic>Bacterial Toxins</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Butterflies & moths</topic><topic>Centrifugation</topic><topic>E coli</topic><topic>Endotoxins - analysis</topic><topic>Endotoxins - biosynthesis</topic><topic>Endotoxins - pharmacology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gustafson, M.E</au><au>Clayton, R.A</au><au>Lavrik, P.B</au><au>Johnson, G.V</au><au>Leimgruber, R.M</au><au>Sims, S.R</au><au>Bartnicki, D.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Large-scale production and characterization of Bacillus thuringiensis subsp. tenebrionis insecticidal protein from Escherichia coli</atitle><jtitle>Applied microbiology and biotechnology</jtitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>1997-03-01</date><risdate>1997</risdate><volume>47</volume><issue>3</issue><spage>255</spage><epage>261</epage><pages>255-261</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>Bacillus thuringiensis subsp. tenebrionis insecticidal protein was produced in recombinant Escherichia coli and purified to near homogeneity to provide quantities of protein for safety-assessment studies associated with the registration of transgenic potato plants. The 68-kDa protein is produced naturally by Bacillus thuringiensis subsp. tenebrionis by translation initiation at an internal initiation site in the native DNA sequence. The gene sequence specific for this truncated protein was expressed in E. coli strain JM 101 and fermented at the 1000-1 scale. The protein accumulated as insoluble inclusion bodies, and was purified by extraction at pH 10.8 with carbonate buffer, selective precipitation at pH 9.0. and differential centrifugation. No chromatography steps were required to produce over 50 g purified protein as a lyophilized powder with a purity greater than 95% and demonstrating full insecticidal activity against Colorado potato beetle larvae. The protein was further characterized to assure identity and suitability for use in safety-assessment studies.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>9114517</pmid><doi>10.1007/s002530050923</doi><tpages>7</tpages></addata></record> |
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| subjects | agrochemicals Analysis Animals Bacillus thuringiensis Bacillus thuringiensis - chemistry Bacillus thuringiensis tenebrionis Bacteria Bacterial proteins Bacterial Proteins - analysis Bacterial Proteins - biosynthesis Bacterial Proteins - pharmacology Bacterial Toxins Biological and medical sciences Biotechnology Butterflies & moths Centrifugation E coli Endotoxins - analysis Endotoxins - biosynthesis Endotoxins - pharmacology Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genetic engineering Genetic technics Hemolysin Proteins Larvae Methods. Procedures. Technologies Microbiological chemistry Microbiological synthesis Microbiology Modification of gene expression level Pest Control, Biological pesticides Potatoes Proteins Recombinant Proteins - biosynthesis |
| title | Large-scale production and characterization of Bacillus thuringiensis subsp. tenebrionis insecticidal protein from Escherichia coli |
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