Purification and properties of a new Brevibacterium sterolicum cholesterol oxidase produced by E. coli MM294/pnH10
A gene encoding a cholesterol oxidase from Brevibacterium sterolicum novo sp. ATCC21387 was isolated by an expression cloning method and highly expressed by a recombinant strain Escherichia coli MM294/pnH10. The purified cholesterol oxidase was a typical flavoprotein with a molecular mass of 46.5 kD...
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| Veröffentlicht in: | FEMS microbiology letters 2002-10, Vol.215 (2), p.243-248 |
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| creator | Fujishiro, K Uchida, H Shimokawa, K Nakano, M Sano, F Ohta, T Kayahara, N Aisaka, K Uwajima, T |
| description | A gene encoding a cholesterol oxidase from Brevibacterium sterolicum novo sp. ATCC21387 was isolated by an expression cloning method and highly expressed by a recombinant strain Escherichia coli MM294/pnH10. The purified cholesterol oxidase was a typical flavoprotein with a molecular mass of 46.5 kDa, absorption peaks at 280, 360, and 450 nm. Optimum pH and temperature were found at pH 6.5 and 55 degrees C, respectively. The enzyme acted on 3 beta-hydroxysteroids such as cholesterol, pregnenolone, and beta-sitosterol at high rates, but on dehydro-epi-androsterone to a lesser degree. The molecular and catalytic properties were different from those of cholesterol oxidase I, which was initially discovered in B. sterolicum novo sp. ATCC21387. The new enzyme, designated cholesterol oxidase II, was distinguished by its high affinity toward cholesterol (K(m) = 30 micromolar). |
| doi_str_mv | 10.1111/j.1574-6968.2002.tb11397.x |
| format | Article |
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ATCC21387 was isolated by an expression cloning method and highly expressed by a recombinant strain Escherichia coli MM294/pnH10. The purified cholesterol oxidase was a typical flavoprotein with a molecular mass of 46.5 kDa, absorption peaks at 280, 360, and 450 nm. Optimum pH and temperature were found at pH 6.5 and 55 degrees C, respectively. The enzyme acted on 3 beta-hydroxysteroids such as cholesterol, pregnenolone, and beta-sitosterol at high rates, but on dehydro-epi-androsterone to a lesser degree. The molecular and catalytic properties were different from those of cholesterol oxidase I, which was initially discovered in B. sterolicum novo sp. ATCC21387. The new enzyme, designated cholesterol oxidase II, was distinguished by its high affinity toward cholesterol (K(m) = 30 micromolar).</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2002.tb11397.x</identifier><identifier>PMID: 12399041</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>absorption ; Bacteriology ; beta-sitosterol ; Biological and medical sciences ; Brevibacterium ; Brevibacterium - enzymology ; Brevibacterium - genetics ; Brevibacterium sterolicum ; Cholesterol ; Cholesterol oxidase ; Cholesterol Oxidase - chemistry ; Cholesterol Oxidase - genetics ; Cholesterol Oxidase - isolation & purification ; Cholesterol Oxidase - metabolism ; Chromatography, High Pressure Liquid ; Cloning ; Cloning, Molecular ; Colony hybridization ; E coli ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli MM294 ; Expression cloning ; flavoproteins ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Bacterial ; genes ; Hydrogen-Ion Concentration ; Hydroxysteroids ; Metabolism. Enzymes ; Microbiology ; molecular weight ; New species ; pH effects ; Pregnenolone ; Purification ; Substrate Specificity ; temperature</subject><ispartof>FEMS microbiology letters, 2002-10, Vol.215 (2), p.243-248</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2003 INIST-CNRS</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3763-64dd05fd6c07fbe6f7d38d73a24a82bcca304709159bfa60317a24442c323feb3</citedby><cites>FETCH-LOGICAL-c3763-64dd05fd6c07fbe6f7d38d73a24a82bcca304709159bfa60317a24442c323feb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2002.tb11397.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2002.tb11397.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13979412$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12399041$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fujishiro, K</creatorcontrib><creatorcontrib>Uchida, H</creatorcontrib><creatorcontrib>Shimokawa, K</creatorcontrib><creatorcontrib>Nakano, M</creatorcontrib><creatorcontrib>Sano, F</creatorcontrib><creatorcontrib>Ohta, T</creatorcontrib><creatorcontrib>Kayahara, N</creatorcontrib><creatorcontrib>Aisaka, K</creatorcontrib><creatorcontrib>Uwajima, T</creatorcontrib><title>Purification and properties of a new Brevibacterium sterolicum cholesterol oxidase produced by E. coli MM294/pnH10</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>A gene encoding a cholesterol oxidase from Brevibacterium sterolicum novo sp. ATCC21387 was isolated by an expression cloning method and highly expressed by a recombinant strain Escherichia coli MM294/pnH10. The purified cholesterol oxidase was a typical flavoprotein with a molecular mass of 46.5 kDa, absorption peaks at 280, 360, and 450 nm. Optimum pH and temperature were found at pH 6.5 and 55 degrees C, respectively. The enzyme acted on 3 beta-hydroxysteroids such as cholesterol, pregnenolone, and beta-sitosterol at high rates, but on dehydro-epi-androsterone to a lesser degree. The molecular and catalytic properties were different from those of cholesterol oxidase I, which was initially discovered in B. sterolicum novo sp. ATCC21387. The new enzyme, designated cholesterol oxidase II, was distinguished by its high affinity toward cholesterol (K(m) = 30 micromolar).</description><subject>absorption</subject><subject>Bacteriology</subject><subject>beta-sitosterol</subject><subject>Biological and medical sciences</subject><subject>Brevibacterium</subject><subject>Brevibacterium - enzymology</subject><subject>Brevibacterium - genetics</subject><subject>Brevibacterium sterolicum</subject><subject>Cholesterol</subject><subject>Cholesterol oxidase</subject><subject>Cholesterol Oxidase - chemistry</subject><subject>Cholesterol Oxidase - genetics</subject><subject>Cholesterol Oxidase - isolation & purification</subject><subject>Cholesterol Oxidase - metabolism</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Colony hybridization</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli MM294</subject><subject>Expression cloning</subject><subject>flavoproteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>genes</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydroxysteroids</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>molecular weight</subject><subject>New species</subject><subject>pH effects</subject><subject>Pregnenolone</subject><subject>Purification</subject><subject>Substrate Specificity</subject><subject>temperature</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</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>eNqVkl9rFDEUxQdR7Fr9ChoU-zbTmz-TTHwQtLRW2EVB-xwymUSzzE7WZMfufnszzNKCKGJebkJ-5-ZcToriJYYK53W-rnAtWMklbyoCQKpdizGVoto_KBZ3Vw-LBVDRlBikOCmepLQGAEaAPy5OMKFSAsOLIn4eo3fe6J0PA9JDh7YxbG3ceZtQcEijwd6i99H-9K02Oxv9uEEp19B7k7fme-jtfEZh7zud7NShG43tUHtAlxUyGUWrFZHsfDtcY3haPHK6T_bZsZ4WN1eXXy-uy-WnDx8v3i1LQwWnJWddB7XruAHhWsud6GjTCaoJ0w1pjdEUmACJa9k6zYFika8YI4YS6mxLT4uzuW_282PMJtXGJ2P7Xg82jEkJwolsgPwTxE2NgQLN4KvfwHUY45CHUIRi4ALzus7Um5kyMaQUrVPb6Dc6HhQGNQWo1mpKSU0pqSlAdQxQ7bP4-fGJsd3Y7l56TCwDr4-ATkb3LurB-HTP5TaS4WmotzN363t7-A8L6mq1JGwatp4bhHH7F3n55wlezDqng9LfYjZ384UA5vn7SdGQhv4CqSjQBQ</recordid><startdate>200210</startdate><enddate>200210</enddate><creator>Fujishiro, K</creator><creator>Uchida, H</creator><creator>Shimokawa, K</creator><creator>Nakano, M</creator><creator>Sano, F</creator><creator>Ohta, T</creator><creator>Kayahara, N</creator><creator>Aisaka, K</creator><creator>Uwajima, T</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</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>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200210</creationdate><title>Purification and properties of a new Brevibacterium sterolicum cholesterol oxidase produced by E. coli MM294/pnH10</title><author>Fujishiro, K ; Uchida, H ; Shimokawa, K ; Nakano, M ; Sano, F ; Ohta, T ; Kayahara, N ; Aisaka, K ; Uwajima, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3763-64dd05fd6c07fbe6f7d38d73a24a82bcca304709159bfa60317a24442c323feb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>absorption</topic><topic>Bacteriology</topic><topic>beta-sitosterol</topic><topic>Biological and medical sciences</topic><topic>Brevibacterium</topic><topic>Brevibacterium - enzymology</topic><topic>Brevibacterium - genetics</topic><topic>Brevibacterium sterolicum</topic><topic>Cholesterol</topic><topic>Cholesterol oxidase</topic><topic>Cholesterol Oxidase - chemistry</topic><topic>Cholesterol Oxidase - genetics</topic><topic>Cholesterol Oxidase - isolation & purification</topic><topic>Cholesterol Oxidase - metabolism</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>Colony hybridization</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli MM294</topic><topic>Expression cloning</topic><topic>flavoproteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>genes</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydroxysteroids</topic><topic>Metabolism. 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ATCC21387 was isolated by an expression cloning method and highly expressed by a recombinant strain Escherichia coli MM294/pnH10. The purified cholesterol oxidase was a typical flavoprotein with a molecular mass of 46.5 kDa, absorption peaks at 280, 360, and 450 nm. Optimum pH and temperature were found at pH 6.5 and 55 degrees C, respectively. The enzyme acted on 3 beta-hydroxysteroids such as cholesterol, pregnenolone, and beta-sitosterol at high rates, but on dehydro-epi-androsterone to a lesser degree. The molecular and catalytic properties were different from those of cholesterol oxidase I, which was initially discovered in B. sterolicum novo sp. ATCC21387. The new enzyme, designated cholesterol oxidase II, was distinguished by its high affinity toward cholesterol (K(m) = 30 micromolar).</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>12399041</pmid><doi>10.1111/j.1574-6968.2002.tb11397.x</doi><tpages>6</tpages></addata></record> |
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| ispartof | FEMS microbiology letters, 2002-10, Vol.215 (2), p.243-248 |
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| subjects | absorption Bacteriology beta-sitosterol Biological and medical sciences Brevibacterium Brevibacterium - enzymology Brevibacterium - genetics Brevibacterium sterolicum Cholesterol Cholesterol oxidase Cholesterol Oxidase - chemistry Cholesterol Oxidase - genetics Cholesterol Oxidase - isolation & purification Cholesterol Oxidase - metabolism Chromatography, High Pressure Liquid Cloning Cloning, Molecular Colony hybridization E coli Enzymes Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli MM294 Expression cloning flavoproteins Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial genes Hydrogen-Ion Concentration Hydroxysteroids Metabolism. Enzymes Microbiology molecular weight New species pH effects Pregnenolone Purification Substrate Specificity temperature |
| title | Purification and properties of a new Brevibacterium sterolicum cholesterol oxidase produced by E. coli MM294/pnH10 |
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