Characterization of a recombinant mannobiose 2-epimerase from Spirochaeta thermophila that is suggested to be a cellobiose 2-epimerase
A purified recombinant enzyme from Spirochaeta thermophila, that is suggested to be a cellobiose 2-epimerase, was a 47 kDa monomer with a specific activity of 29.2 U min⁻¹ for mannobiose. The epimerization activity of the recombinant enzyme for mannobiose was maximal at pH 7.0 and 60 °C with a half-...
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| Veröffentlicht in: | Biotechnology letters 2013-11, Vol.35 (11), p.1873-1880 |
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| container_title | Biotechnology letters |
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| creator | Park, Chang-Su Kim, Jung-Eun Lee, Seon-Hwa Kim, Yeong-Su Kang, Lin-Woo Oh, Deok-Kun |
| description | A purified recombinant enzyme from Spirochaeta thermophila, that is suggested to be a cellobiose 2-epimerase, was a 47 kDa monomer with a specific activity of 29.2 U min⁻¹ for mannobiose. The epimerization activity of the recombinant enzyme for mannobiose was maximal at pH 7.0 and 60 °C with a half-life of 124 h. The enzyme exhibited a higher epimerization activity for mannose or the mannose moiety at the reducing end of β- and α-1,4-glycosyl-mannose than for glucose or the glucose moiety of β- and α-1,4-glycosyl-glucose. The enzyme was identified as a mannobiose 2-epimerase by evaluating its substrate specificity with not only glucose-containing sugars but also mannose-containing sugars. The activities of the reported cellobiose 2-epimerases from Caldicellulosiruptor saccharolyticus, Dictyoglomus turgidum and Ruminococcus marinus for mannobiose were higher than those for cellobiose, strongly suggesting that these enzymes are not cellobiose 2-epimerases but are mannobiose 2-epimerases. |
| doi_str_mv | 10.1007/s10529-013-1267-6 |
| format | Article |
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The epimerization activity of the recombinant enzyme for mannobiose was maximal at pH 7.0 and 60 °C with a half-life of 124 h. The enzyme exhibited a higher epimerization activity for mannose or the mannose moiety at the reducing end of β- and α-1,4-glycosyl-mannose than for glucose or the glucose moiety of β- and α-1,4-glycosyl-glucose. The enzyme was identified as a mannobiose 2-epimerase by evaluating its substrate specificity with not only glucose-containing sugars but also mannose-containing sugars. The activities of the reported cellobiose 2-epimerases from Caldicellulosiruptor saccharolyticus, Dictyoglomus turgidum and Ruminococcus marinus for mannobiose were higher than those for cellobiose, strongly suggesting that these enzymes are not cellobiose 2-epimerases but are mannobiose 2-epimerases.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-013-1267-6</identifier><identifier>PMID: 23801120</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Applied Microbiology ; Bacteria ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Caldicellulosiruptor ; Caldicellulosiruptor saccharolyticus ; Carbohydrate Epimerases - chemistry ; Carbohydrate Epimerases - genetics ; Carbohydrate Epimerases - isolation & purification ; Carbohydrate Epimerases - metabolism ; Carbohydrates ; cellobiose ; Cellobiose - metabolism ; Dictyoglomus ; Enzyme Stability ; Enzymes ; Glucose ; half life ; Hydrogen-Ion Concentration ; Life Sciences ; Mannans - metabolism ; Mannose ; Microbiology ; Molecular Weight ; Monomers ; Original Research Paper ; Phylogeny ; Recombinant ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Ruminococcus ; Sequence Homology, Amino Acid ; Spirochaeta ; Spirochaeta - enzymology ; Spirochaeta - genetics ; Spirochaeta thermophila ; Substrate Specificity ; Sugar ; Sugars ; Temperature</subject><ispartof>Biotechnology letters, 2013-11, Vol.35 (11), p.1873-1880</ispartof><rights>Springer Science+Business Media Dordrecht 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-457f70c46c7bd41287dd9d7bc0af65f1e49ccd66d534b80c5051762e08fb8cb33</citedby><cites>FETCH-LOGICAL-c462t-457f70c46c7bd41287dd9d7bc0af65f1e49ccd66d534b80c5051762e08fb8cb33</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/s10529-013-1267-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-013-1267-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27906,27907,41470,42539,51301</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23801120$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Chang-Su</creatorcontrib><creatorcontrib>Kim, Jung-Eun</creatorcontrib><creatorcontrib>Lee, Seon-Hwa</creatorcontrib><creatorcontrib>Kim, Yeong-Su</creatorcontrib><creatorcontrib>Kang, Lin-Woo</creatorcontrib><creatorcontrib>Oh, Deok-Kun</creatorcontrib><title>Characterization of a recombinant mannobiose 2-epimerase from Spirochaeta thermophila that is suggested to be a cellobiose 2-epimerase</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>A purified recombinant enzyme from Spirochaeta thermophila, that is suggested to be a cellobiose 2-epimerase, was a 47 kDa monomer with a specific activity of 29.2 U min⁻¹ for mannobiose. The epimerization activity of the recombinant enzyme for mannobiose was maximal at pH 7.0 and 60 °C with a half-life of 124 h. The enzyme exhibited a higher epimerization activity for mannose or the mannose moiety at the reducing end of β- and α-1,4-glycosyl-mannose than for glucose or the glucose moiety of β- and α-1,4-glycosyl-glucose. The enzyme was identified as a mannobiose 2-epimerase by evaluating its substrate specificity with not only glucose-containing sugars but also mannose-containing sugars. The activities of the reported cellobiose 2-epimerases from Caldicellulosiruptor saccharolyticus, Dictyoglomus turgidum and Ruminococcus marinus for mannobiose were higher than those for cellobiose, strongly suggesting that these enzymes are not cellobiose 2-epimerases but are mannobiose 2-epimerases.</description><subject>Applied Microbiology</subject><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Caldicellulosiruptor</subject><subject>Caldicellulosiruptor saccharolyticus</subject><subject>Carbohydrate Epimerases - chemistry</subject><subject>Carbohydrate Epimerases - genetics</subject><subject>Carbohydrate Epimerases - isolation & purification</subject><subject>Carbohydrate Epimerases - metabolism</subject><subject>Carbohydrates</subject><subject>cellobiose</subject><subject>Cellobiose - metabolism</subject><subject>Dictyoglomus</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Glucose</subject><subject>half life</subject><subject>Hydrogen-Ion Concentration</subject><subject>Life Sciences</subject><subject>Mannans - metabolism</subject><subject>Mannose</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Monomers</subject><subject>Original Research Paper</subject><subject>Phylogeny</subject><subject>Recombinant</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Ruminococcus</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spirochaeta</subject><subject>Spirochaeta - enzymology</subject><subject>Spirochaeta - genetics</subject><subject>Spirochaeta thermophila</subject><subject>Substrate Specificity</subject><subject>Sugar</subject><subject>Sugars</subject><subject>Temperature</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</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>eNqNks1u1TAQhS0EopfCA7ABS2y6MXj8nyW6goJUiUXp2nIc515XN3Gwk0V5AJ4bRykIgQSsPJK_OXPsMwg9B_oaKNVvClDJGkKBE2BKE_UA7UBqTpTW6iHaURBApGjYGXpSyi2ltNFUP0ZnjBsKwOgOfdsfXXZ-Djl-dXNMI049djgHn4Y2jm6c8eDGMbUxlYAZCVMcQna17nMa8PUUc_JHF2aH52PIQ5qO8bTWbsax4LIcDqHMocNzwm2oyj6cTn-qPUWPencq4dn9eY5u3r_7vP9Arj5dfty_vSJeKDYTIXWvaa29bjsBzOiuazrdeup6JXsIovG-U6qTXLSGekklaMUCNX1rfMv5ObrYdKecvizVmR1iWS25MaSlWFBGGpCNUv9GhTCMCVV__z9QLsDwRlb01W_obVryWN-8UqAb3hhdKdgon1MpOfR2ynFw-c4CtWv0dove1uF2jd6ufl_cKy_tELqfHT-yrgDbgFKvxkPIv4z-i-rLral3ybpDjsXeXLO6WHWZhAau-Xcju8Jv</recordid><startdate>20131101</startdate><enddate>20131101</enddate><creator>Park, Chang-Su</creator><creator>Kim, Jung-Eun</creator><creator>Lee, Seon-Hwa</creator><creator>Kim, Yeong-Su</creator><creator>Kang, Lin-Woo</creator><creator>Oh, Deok-Kun</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</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>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</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>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope><scope>RC3</scope></search><sort><creationdate>20131101</creationdate><title>Characterization of a recombinant mannobiose 2-epimerase from Spirochaeta thermophila that is suggested to be a cellobiose 2-epimerase</title><author>Park, Chang-Su ; Kim, Jung-Eun ; Lee, Seon-Hwa ; Kim, Yeong-Su ; Kang, Lin-Woo ; Oh, Deok-Kun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-457f70c46c7bd41287dd9d7bc0af65f1e49ccd66d534b80c5051762e08fb8cb33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Applied Microbiology</topic><topic>Bacteria</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Caldicellulosiruptor</topic><topic>Caldicellulosiruptor saccharolyticus</topic><topic>Carbohydrate Epimerases - chemistry</topic><topic>Carbohydrate Epimerases - genetics</topic><topic>Carbohydrate Epimerases - isolation & purification</topic><topic>Carbohydrate Epimerases - metabolism</topic><topic>Carbohydrates</topic><topic>cellobiose</topic><topic>Cellobiose - metabolism</topic><topic>Dictyoglomus</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Glucose</topic><topic>half life</topic><topic>Hydrogen-Ion Concentration</topic><topic>Life Sciences</topic><topic>Mannans - metabolism</topic><topic>Mannose</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Monomers</topic><topic>Original Research Paper</topic><topic>Phylogeny</topic><topic>Recombinant</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Ruminococcus</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spirochaeta</topic><topic>Spirochaeta - enzymology</topic><topic>Spirochaeta - genetics</topic><topic>Spirochaeta thermophila</topic><topic>Substrate Specificity</topic><topic>Sugar</topic><topic>Sugars</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Chang-Su</creatorcontrib><creatorcontrib>Kim, Jung-Eun</creatorcontrib><creatorcontrib>Lee, Seon-Hwa</creatorcontrib><creatorcontrib>Kim, Yeong-Su</creatorcontrib><creatorcontrib>Kang, Lin-Woo</creatorcontrib><creatorcontrib>Oh, Deok-Kun</creatorcontrib><collection>AGRIS</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>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</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 Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology 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>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</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>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Chang-Su</au><au>Kim, Jung-Eun</au><au>Lee, Seon-Hwa</au><au>Kim, Yeong-Su</au><au>Kang, Lin-Woo</au><au>Oh, Deok-Kun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a recombinant mannobiose 2-epimerase from Spirochaeta thermophila that is suggested to be a cellobiose 2-epimerase</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2013-11-01</date><risdate>2013</risdate><volume>35</volume><issue>11</issue><spage>1873</spage><epage>1880</epage><pages>1873-1880</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>A purified recombinant enzyme from Spirochaeta thermophila, that is suggested to be a cellobiose 2-epimerase, was a 47 kDa monomer with a specific activity of 29.2 U min⁻¹ for mannobiose. The epimerization activity of the recombinant enzyme for mannobiose was maximal at pH 7.0 and 60 °C with a half-life of 124 h. The enzyme exhibited a higher epimerization activity for mannose or the mannose moiety at the reducing end of β- and α-1,4-glycosyl-mannose than for glucose or the glucose moiety of β- and α-1,4-glycosyl-glucose. The enzyme was identified as a mannobiose 2-epimerase by evaluating its substrate specificity with not only glucose-containing sugars but also mannose-containing sugars. The activities of the reported cellobiose 2-epimerases from Caldicellulosiruptor saccharolyticus, Dictyoglomus turgidum and Ruminococcus marinus for mannobiose were higher than those for cellobiose, strongly suggesting that these enzymes are not cellobiose 2-epimerases but are mannobiose 2-epimerases.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>23801120</pmid><doi>10.1007/s10529-013-1267-6</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biotechnology letters, 2013-11, Vol.35 (11), p.1873-1880 |
| issn | 0141-5492 1573-6776 |
| language | eng |
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| subjects | Applied Microbiology Bacteria Biochemistry Biomedical and Life Sciences Biotechnology Caldicellulosiruptor Caldicellulosiruptor saccharolyticus Carbohydrate Epimerases - chemistry Carbohydrate Epimerases - genetics Carbohydrate Epimerases - isolation & purification Carbohydrate Epimerases - metabolism Carbohydrates cellobiose Cellobiose - metabolism Dictyoglomus Enzyme Stability Enzymes Glucose half life Hydrogen-Ion Concentration Life Sciences Mannans - metabolism Mannose Microbiology Molecular Weight Monomers Original Research Paper Phylogeny Recombinant Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Ruminococcus Sequence Homology, Amino Acid Spirochaeta Spirochaeta - enzymology Spirochaeta - genetics Spirochaeta thermophila Substrate Specificity Sugar Sugars Temperature |
| title | Characterization of a recombinant mannobiose 2-epimerase from Spirochaeta thermophila that is suggested to be a cellobiose 2-epimerase |
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