Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass
An endo-1,4-β-xylanase gene, xylcg , was cloned from Chaetomium globosum and successfully expressed in Escherichia coli . The complete gene of 675 bp was amplified, cloned into the pET 28(a) vector, and expressed. The optimal conditions for the highest activity of the purified recombinant XylCg were...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2013-08, Vol.97 (16), p.7205-7214 |
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| creator | Singh, Raushan Kumar Tiwari, Manish Kumar Kim, Dongwook Kang, Yun Chan Ramachandran, Priyadharshini Lee, Jung-Kul |
| description | An endo-1,4-β-xylanase gene,
xylcg
, was cloned from
Chaetomium globosum
and successfully expressed in
Escherichia coli
. The complete gene of 675 bp was amplified, cloned into the pET 28(a) vector, and expressed. The optimal conditions for the highest activity of the purified recombinant XylCg were observed at a temperature of 40 °C and pH of 5.5. Using oat-spelt xylan, the determined
K
m
,
V
max
, and
k
cat
/
K
m
values were 0.243 mg ml
−1
, 4,530 U mg
−1
protein, and 7,640 ml s
−1
mg
−1
, respectively. A homology model and sequence analysis of XylCg, along with the biochemical properties, confirmed that XylCg belongs to the GH11 family. Rice straw pretreated with XylCg showed 30 % higher conversion yield than the rice straw pretreated with a commercial xylanase. Although xylanases have been characterized from fungal and bacterial sources,
C
.
globosum
XylCg is distinguished from other xylanases by its high catalytic efficiency and its effectiveness in the pretreatment of lignocellulosic biomass. |
| doi_str_mv | 10.1007/s00253-012-4577-z |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_1753537539</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A344279644</galeid><sourcerecordid>A344279644</sourcerecordid><originalsourceid>FETCH-LOGICAL-c576t-51c62ae7bb5a317f8e0b646422b5adeed8cec6352446d9e552053be026d5007f3</originalsourceid><addsrcrecordid>eNqNkl1rFDEYhQdR7Fr9Ad5IwJsKTs33zFyWRdtCRfDjOmQy72xTJsmaZKC7v8CfbdatHyuKEkjgzXMOnORU1VOCTwnGzauEMRWsxoTWXDRNvb1XLQhntMaS8PvVApNG1I3o2qPqUUo3uICtlA-rI8pIyynFi-rL2zCBmScdkZmCt36FtB-QudZRmwzRbnW2waMwIo3OLwhB4Idwu5m01wnQGINDy2sNOTg7O7SaQh_S7F5-c7E5oblQ1hfVduOKlUHrCDmCzg583tn2Njid0uPqwainBE_uzuPq05vXH5cX9dW788vl2VVtRCNzLYiRVEPT90Iz0owt4F5yWcKUwQAwtAaMZIJyLocOhKBYsB4wlYMoTzay4-pk77uO4fMMKStnk4GpBIIwJ1WejAlWtu7fKCcda1gnyP-gQnSdaGVBn_-G3oQ5-pJ5R9GWUNySn9RKT6CsH0MuH7IzVWeMc9p0kvNCnf6BKmsAZ03wMNoyPxC8OBAUJsNtXuk5JXX54f0hS_asiSGlCKNaR-t03CiC1a5_at8_VWqldv1T26J5dhdu7h0MPxTfC1cAugdSufIriL-k_6vrV2yr44A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1412812081</pqid></control><display><type>article</type><title>Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Singh, Raushan Kumar ; Tiwari, Manish Kumar ; Kim, Dongwook ; Kang, Yun Chan ; Ramachandran, Priyadharshini ; Lee, Jung-Kul</creator><creatorcontrib>Singh, Raushan Kumar ; Tiwari, Manish Kumar ; Kim, Dongwook ; Kang, Yun Chan ; Ramachandran, Priyadharshini ; Lee, Jung-Kul</creatorcontrib><description>An endo-1,4-β-xylanase gene,
xylcg
, was cloned from
Chaetomium globosum
and successfully expressed in
Escherichia coli
. The complete gene of 675 bp was amplified, cloned into the pET 28(a) vector, and expressed. The optimal conditions for the highest activity of the purified recombinant XylCg were observed at a temperature of 40 °C and pH of 5.5. Using oat-spelt xylan, the determined
K
m
,
V
max
, and
k
cat
/
K
m
values were 0.243 mg ml
−1
, 4,530 U mg
−1
protein, and 7,640 ml s
−1
mg
−1
, respectively. A homology model and sequence analysis of XylCg, along with the biochemical properties, confirmed that XylCg belongs to the GH11 family. Rice straw pretreated with XylCg showed 30 % higher conversion yield than the rice straw pretreated with a commercial xylanase. Although xylanases have been characterized from fungal and bacterial sources,
C
.
globosum
XylCg is distinguished from other xylanases by its high catalytic efficiency and its effectiveness in the pretreatment of lignocellulosic biomass.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-012-4577-z</identifier><identifier>PMID: 23184220</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Analysis ; Avena - chemistry ; Bacteria ; Biomass ; Biomedical and Life Sciences ; Biosynthesis ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Chaetomium - enzymology ; Chaetomium - genetics ; Chaetomium globosum ; Cloning ; Cloning, Molecular ; E coli ; Endo-1,4-beta Xylanases - chemistry ; Endo-1,4-beta Xylanases - genetics ; Endo-1,4-beta Xylanases - isolation & purification ; Endo-1,4-beta Xylanases - metabolism ; Enzyme Stability ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Fungi ; Gene Expression ; Genes ; Genetic aspects ; Genetic engineering ; Hydrogen-Ion Concentration ; Kinetics ; Life Sciences ; Lignin - metabolism ; Microbial Genetics and Genomics ; Microbiology ; Models, Molecular ; Oryza - chemistry ; Oryza sativa ; Plant Stems - chemistry ; Pretreatment ; Protein Conformation ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Rice ; Rice straw ; Straw ; Studies ; Temperature ; Xylanase ; Xylans - metabolism</subject><ispartof>Applied microbiology and biotechnology, 2013-08, Vol.97 (16), p.7205-7214</ispartof><rights>Springer-Verlag Berlin Heidelberg 2012</rights><rights>COPYRIGHT 2013 Springer</rights><rights>Springer-Verlag 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c576t-51c62ae7bb5a317f8e0b646422b5adeed8cec6352446d9e552053be026d5007f3</citedby><cites>FETCH-LOGICAL-c576t-51c62ae7bb5a317f8e0b646422b5adeed8cec6352446d9e552053be026d5007f3</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/s00253-012-4577-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-012-4577-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23184220$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Singh, Raushan Kumar</creatorcontrib><creatorcontrib>Tiwari, Manish Kumar</creatorcontrib><creatorcontrib>Kim, Dongwook</creatorcontrib><creatorcontrib>Kang, Yun Chan</creatorcontrib><creatorcontrib>Ramachandran, Priyadharshini</creatorcontrib><creatorcontrib>Lee, Jung-Kul</creatorcontrib><title>Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>An endo-1,4-β-xylanase gene,
xylcg
, was cloned from
Chaetomium globosum
and successfully expressed in
Escherichia coli
. The complete gene of 675 bp was amplified, cloned into the pET 28(a) vector, and expressed. The optimal conditions for the highest activity of the purified recombinant XylCg were observed at a temperature of 40 °C and pH of 5.5. Using oat-spelt xylan, the determined
K
m
,
V
max
, and
k
cat
/
K
m
values were 0.243 mg ml
−1
, 4,530 U mg
−1
protein, and 7,640 ml s
−1
mg
−1
, respectively. A homology model and sequence analysis of XylCg, along with the biochemical properties, confirmed that XylCg belongs to the GH11 family. Rice straw pretreated with XylCg showed 30 % higher conversion yield than the rice straw pretreated with a commercial xylanase. Although xylanases have been characterized from fungal and bacterial sources,
C
.
globosum
XylCg is distinguished from other xylanases by its high catalytic efficiency and its effectiveness in the pretreatment of lignocellulosic biomass.</description><subject>Analysis</subject><subject>Avena - chemistry</subject><subject>Bacteria</subject><subject>Biomass</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Chaetomium - enzymology</subject><subject>Chaetomium - genetics</subject><subject>Chaetomium globosum</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>E coli</subject><subject>Endo-1,4-beta Xylanases - chemistry</subject><subject>Endo-1,4-beta Xylanases - genetics</subject><subject>Endo-1,4-beta Xylanases - isolation & purification</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Fungi</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Genetic engineering</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Lignin - metabolism</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Oryza - chemistry</subject><subject>Oryza sativa</subject><subject>Plant Stems - chemistry</subject><subject>Pretreatment</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Rice</subject><subject>Rice straw</subject><subject>Straw</subject><subject>Studies</subject><subject>Temperature</subject><subject>Xylanase</subject><subject>Xylans - metabolism</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkl1rFDEYhQdR7Fr9Ad5IwJsKTs33zFyWRdtCRfDjOmQy72xTJsmaZKC7v8CfbdatHyuKEkjgzXMOnORU1VOCTwnGzauEMRWsxoTWXDRNvb1XLQhntMaS8PvVApNG1I3o2qPqUUo3uICtlA-rI8pIyynFi-rL2zCBmScdkZmCt36FtB-QudZRmwzRbnW2waMwIo3OLwhB4Idwu5m01wnQGINDy2sNOTg7O7SaQh_S7F5-c7E5oblQ1hfVduOKlUHrCDmCzg583tn2Njid0uPqwainBE_uzuPq05vXH5cX9dW788vl2VVtRCNzLYiRVEPT90Iz0owt4F5yWcKUwQAwtAaMZIJyLocOhKBYsB4wlYMoTzay4-pk77uO4fMMKStnk4GpBIIwJ1WejAlWtu7fKCcda1gnyP-gQnSdaGVBn_-G3oQ5-pJ5R9GWUNySn9RKT6CsH0MuH7IzVWeMc9p0kvNCnf6BKmsAZ03wMNoyPxC8OBAUJsNtXuk5JXX54f0hS_asiSGlCKNaR-t03CiC1a5_at8_VWqldv1T26J5dhdu7h0MPxTfC1cAugdSufIriL-k_6vrV2yr44A</recordid><startdate>20130801</startdate><enddate>20130801</enddate><creator>Singh, Raushan Kumar</creator><creator>Tiwari, Manish Kumar</creator><creator>Kim, Dongwook</creator><creator>Kang, Yun Chan</creator><creator>Ramachandran, Priyadharshini</creator><creator>Lee, Jung-Kul</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><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>7X8</scope><scope>7QO</scope><scope>7TB</scope><scope>7U5</scope><scope>F28</scope><scope>L7M</scope></search><sort><creationdate>20130801</creationdate><title>Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass</title><author>Singh, Raushan Kumar ; Tiwari, Manish Kumar ; Kim, Dongwook ; Kang, Yun Chan ; Ramachandran, Priyadharshini ; Lee, Jung-Kul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c576t-51c62ae7bb5a317f8e0b646422b5adeed8cec6352446d9e552053be026d5007f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Analysis</topic><topic>Avena - chemistry</topic><topic>Bacteria</topic><topic>Biomass</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Chaetomium - enzymology</topic><topic>Chaetomium - genetics</topic><topic>Chaetomium globosum</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>E coli</topic><topic>Endo-1,4-beta Xylanases - chemistry</topic><topic>Endo-1,4-beta Xylanases - genetics</topic><topic>Endo-1,4-beta Xylanases - isolation & purification</topic><topic>Endo-1,4-beta Xylanases - metabolism</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Fungi</topic><topic>Gene Expression</topic><topic>Genes</topic><topic>Genetic aspects</topic><topic>Genetic engineering</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Lignin - metabolism</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Oryza - chemistry</topic><topic>Oryza sativa</topic><topic>Plant Stems - chemistry</topic><topic>Pretreatment</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Rice</topic><topic>Rice straw</topic><topic>Straw</topic><topic>Studies</topic><topic>Temperature</topic><topic>Xylanase</topic><topic>Xylans - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Singh, Raushan Kumar</creatorcontrib><creatorcontrib>Tiwari, Manish Kumar</creatorcontrib><creatorcontrib>Kim, Dongwook</creatorcontrib><creatorcontrib>Kang, Yun Chan</creatorcontrib><creatorcontrib>Ramachandran, Priyadharshini</creatorcontrib><creatorcontrib>Lee, Jung-Kul</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</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 One Sustainability</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>One Business (ProQuest)</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>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Singh, Raushan Kumar</au><au>Tiwari, Manish Kumar</au><au>Kim, Dongwook</au><au>Kang, Yun Chan</au><au>Ramachandran, Priyadharshini</au><au>Lee, Jung-Kul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2013-08-01</date><risdate>2013</risdate><volume>97</volume><issue>16</issue><spage>7205</spage><epage>7214</epage><pages>7205-7214</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>An endo-1,4-β-xylanase gene,
xylcg
, was cloned from
Chaetomium globosum
and successfully expressed in
Escherichia coli
. The complete gene of 675 bp was amplified, cloned into the pET 28(a) vector, and expressed. The optimal conditions for the highest activity of the purified recombinant XylCg were observed at a temperature of 40 °C and pH of 5.5. Using oat-spelt xylan, the determined
K
m
,
V
max
, and
k
cat
/
K
m
values were 0.243 mg ml
−1
, 4,530 U mg
−1
protein, and 7,640 ml s
−1
mg
−1
, respectively. A homology model and sequence analysis of XylCg, along with the biochemical properties, confirmed that XylCg belongs to the GH11 family. Rice straw pretreated with XylCg showed 30 % higher conversion yield than the rice straw pretreated with a commercial xylanase. Although xylanases have been characterized from fungal and bacterial sources,
C
.
globosum
XylCg is distinguished from other xylanases by its high catalytic efficiency and its effectiveness in the pretreatment of lignocellulosic biomass.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>23184220</pmid><doi>10.1007/s00253-012-4577-z</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2013-08, Vol.97 (16), p.7205-7214 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1753537539 |
| source | MEDLINE; SpringerLink Journals |
| subjects | Analysis Avena - chemistry Bacteria Biomass Biomedical and Life Sciences Biosynthesis Biotechnologically Relevant Enzymes and Proteins Biotechnology Chaetomium - enzymology Chaetomium - genetics Chaetomium globosum Cloning Cloning, Molecular E coli Endo-1,4-beta Xylanases - chemistry Endo-1,4-beta Xylanases - genetics Endo-1,4-beta Xylanases - isolation & purification Endo-1,4-beta Xylanases - metabolism Enzyme Stability Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Fungi Gene Expression Genes Genetic aspects Genetic engineering Hydrogen-Ion Concentration Kinetics Life Sciences Lignin - metabolism Microbial Genetics and Genomics Microbiology Models, Molecular Oryza - chemistry Oryza sativa Plant Stems - chemistry Pretreatment Protein Conformation Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Rice Rice straw Straw Studies Temperature Xylanase Xylans - metabolism |
| title | Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass |
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