Cloning of a xylanase gene xyn2A from rumen fungus Neocallimastix sp. GMLF2 in Escherichia coli and its partial characterization
Anaerobic fungi belonging to the family Neocallimastigaceae are native inhabitants in the rumen of the most herbivores, such as cattle, sheep and goats. A member of this unique group, Neocallimastix sp. GMLF2 was isolated from cattle feces and screened for its xylanase encoding gene using polymerase...
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| Veröffentlicht in: | Biológia 2009-08, Vol.64 (4), p.664-670 |
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| creator | Akyol, Ismail Ugur Comlekcioglu Bulent Kar M. Ekinci Emin Ozkose |
| description | Anaerobic fungi belonging to the family Neocallimastigaceae are native inhabitants in the rumen of the most herbivores, such as cattle, sheep and goats. A member of this unique group, Neocallimastix sp. GMLF2 was isolated from cattle feces and screened for its xylanase encoding gene using polymerase chain reaction. The gene coding for a xylanase (xyn2A) was cloned in Escherichia coli and expression was monitored. To determine the enzyme activity, assays were conducted for both fungal xylanase and cloned xylanase (Xyl2A) for supernatant and cell-associated activities. Optimum pH and temperature of the enzyme were found to be 6.5 and 50°C, respectively. The enzyme was stable at 40°C and 50°C for 20 min but lost most of its activity when temperature reached 60°C for 5-min incubation time. Rumen fungal xylanase was mainly released to the supernatant of culture, while cloned xylanase activity was found as cell-associated. Multiple alignment of the amino acid sequences of Xyl2A with published xylanases from various organisms suggested that Xyl2A belongs to glycoside hydrolase family 11. |
| doi_str_mv | 10.2478/s11756-009-0140-5 |
| format | Article |
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Optimum pH and temperature of the enzyme were found to be 6.5 and 50°C, respectively. The enzyme was stable at 40°C and 50°C for 20 min but lost most of its activity when temperature reached 60°C for 5-min incubation time. Rumen fungal xylanase was mainly released to the supernatant of culture, while cloned xylanase activity was found as cell-associated. Multiple alignment of the amino acid sequences of Xyl2A with published xylanases from various organisms suggested that Xyl2A belongs to glycoside hydrolase family 11.</description><identifier>ISSN: 1336-9563</identifier><identifier>ISSN: 0006-3088</identifier><identifier>EISSN: 1336-9563</identifier><identifier>DOI: 10.2478/s11756-009-0140-5</identifier><language>eng</language><publisher>Heidelberg: Versita</publisher><subject>amino acid sequences ; anaerobes ; Biomedical and Life Sciences ; cattle ; Cell Biology ; Cell culture ; Cloning ; E. coli ; enzyme activity ; enzyme stability ; Enzymes ; Escherichia coli ; Feces ; Fungi ; gene expression ; genes ; glycoside hydrolase ; glycosides ; goats ; Herbivores ; Life Sciences ; Microbiology ; Neocallimastigaceae ; Neocallimastix ; pH effects ; Plant Sciences ; Polymerase chain reaction ; Rumen ; rumen fungi ; sheep ; temperature ; Temperature effects ; Xylan endo-1,3-b-xylosidase ; xylanase ; xylanases ; Zoology</subject><ispartof>Biológia, 2009-08, Vol.64 (4), p.664-670</ispartof><rights>Versita Warsaw and Springer-Verlag Berlin Heidelberg 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-787da9f8baaa9a4c5c7b3c4cd646ea14a1423b10b6a966cd05df8d4f4a97c1a93</citedby><cites>FETCH-LOGICAL-c399t-787da9f8baaa9a4c5c7b3c4cd646ea14a1423b10b6a966cd05df8d4f4a97c1a93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.2478/s11756-009-0140-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.2478/s11756-009-0140-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids></links><search><creatorcontrib>Akyol, Ismail</creatorcontrib><creatorcontrib>Ugur Comlekcioglu</creatorcontrib><creatorcontrib>Bulent Kar</creatorcontrib><creatorcontrib>M. Ekinci</creatorcontrib><creatorcontrib>Emin Ozkose</creatorcontrib><title>Cloning of a xylanase gene xyn2A from rumen fungus Neocallimastix sp. GMLF2 in Escherichia coli and its partial characterization</title><title>Biológia</title><addtitle>Biologia</addtitle><description>Anaerobic fungi belonging to the family Neocallimastigaceae are native inhabitants in the rumen of the most herbivores, such as cattle, sheep and goats. A member of this unique group, Neocallimastix sp. GMLF2 was isolated from cattle feces and screened for its xylanase encoding gene using polymerase chain reaction. The gene coding for a xylanase (xyn2A) was cloned in Escherichia coli and expression was monitored. To determine the enzyme activity, assays were conducted for both fungal xylanase and cloned xylanase (Xyl2A) for supernatant and cell-associated activities. Optimum pH and temperature of the enzyme were found to be 6.5 and 50°C, respectively. The enzyme was stable at 40°C and 50°C for 20 min but lost most of its activity when temperature reached 60°C for 5-min incubation time. Rumen fungal xylanase was mainly released to the supernatant of culture, while cloned xylanase activity was found as cell-associated. Multiple alignment of the amino acid sequences of Xyl2A with published xylanases from various organisms suggested that Xyl2A belongs to glycoside hydrolase family 11.</description><subject>amino acid sequences</subject><subject>anaerobes</subject><subject>Biomedical and Life Sciences</subject><subject>cattle</subject><subject>Cell Biology</subject><subject>Cell culture</subject><subject>Cloning</subject><subject>E. coli</subject><subject>enzyme activity</subject><subject>enzyme stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Feces</subject><subject>Fungi</subject><subject>gene expression</subject><subject>genes</subject><subject>glycoside hydrolase</subject><subject>glycosides</subject><subject>goats</subject><subject>Herbivores</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Neocallimastigaceae</subject><subject>Neocallimastix</subject><subject>pH effects</subject><subject>Plant Sciences</subject><subject>Polymerase chain reaction</subject><subject>Rumen</subject><subject>rumen fungi</subject><subject>sheep</subject><subject>temperature</subject><subject>Temperature effects</subject><subject>Xylan endo-1,3-b-xylosidase</subject><subject>xylanase</subject><subject>xylanases</subject><subject>Zoology</subject><issn>1336-9563</issn><issn>0006-3088</issn><issn>1336-9563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqNkEFv3CAQha0qlZqk_QE9dU65OQWDsTlV0SpJK23bQ5szmsXgJWJhA7aSzak_vazcQy6VIiEYpPe90XtV9ZGSy4Z3_edMadeKmhBZE8pJ3b6pTiljopatYCcv5nfVWc73hPCuJfS0-rPyMbgwQrSA8HTwGDAbGE0w5ReaK7Ap7iDNOxPAzmGcM_wwUaP3bod5ck-Q95dw-31904ALcJ311iSntw5BR-8AwwBuyrDHNDn0oLeYUE9F84yTi-F99daiz-bDv_e8uru5_r36Wq9_3n5bXa1rzaSc6q7vBpS23yCiRK5b3W2Y5noQXBikvJyGbSjZCJRC6IG0g-0HbjnKTlOU7Ly6WHz3KT7MJk9q57I2vgQ2cc6qIR1p--YopItQp5hzMlbtU4maDooSdexaLV2r0rU6dq3awnxZmEf0JdpgxjQfyqDu45xCifV_VnAuBC8OzeKQy7Ywvgot0KcFshgVjslldferIVQQUm7GBfsLvDqg3Q</recordid><startdate>20090801</startdate><enddate>20090801</enddate><creator>Akyol, Ismail</creator><creator>Ugur Comlekcioglu</creator><creator>Bulent Kar</creator><creator>M. Ekinci</creator><creator>Emin Ozkose</creator><general>Versita</general><general>SP Versita</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20090801</creationdate><title>Cloning of a xylanase gene xyn2A from rumen fungus Neocallimastix sp. GMLF2 in Escherichia coli and its partial characterization</title><author>Akyol, Ismail ; Ugur Comlekcioglu ; Bulent Kar ; M. Ekinci ; Emin Ozkose</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-787da9f8baaa9a4c5c7b3c4cd646ea14a1423b10b6a966cd05df8d4f4a97c1a93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>amino acid sequences</topic><topic>anaerobes</topic><topic>Biomedical and Life Sciences</topic><topic>cattle</topic><topic>Cell Biology</topic><topic>Cell culture</topic><topic>Cloning</topic><topic>E. coli</topic><topic>enzyme activity</topic><topic>enzyme stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Feces</topic><topic>Fungi</topic><topic>gene expression</topic><topic>genes</topic><topic>glycoside hydrolase</topic><topic>glycosides</topic><topic>goats</topic><topic>Herbivores</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Neocallimastigaceae</topic><topic>Neocallimastix</topic><topic>pH effects</topic><topic>Plant Sciences</topic><topic>Polymerase chain reaction</topic><topic>Rumen</topic><topic>rumen fungi</topic><topic>sheep</topic><topic>temperature</topic><topic>Temperature effects</topic><topic>Xylan endo-1,3-b-xylosidase</topic><topic>xylanase</topic><topic>xylanases</topic><topic>Zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Akyol, Ismail</creatorcontrib><creatorcontrib>Ugur Comlekcioglu</creatorcontrib><creatorcontrib>Bulent Kar</creatorcontrib><creatorcontrib>M. 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The enzyme was stable at 40°C and 50°C for 20 min but lost most of its activity when temperature reached 60°C for 5-min incubation time. Rumen fungal xylanase was mainly released to the supernatant of culture, while cloned xylanase activity was found as cell-associated. Multiple alignment of the amino acid sequences of Xyl2A with published xylanases from various organisms suggested that Xyl2A belongs to glycoside hydrolase family 11.</abstract><cop>Heidelberg</cop><pub>Versita</pub><doi>10.2478/s11756-009-0140-5</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | amino acid sequences anaerobes Biomedical and Life Sciences cattle Cell Biology Cell culture Cloning E. coli enzyme activity enzyme stability Enzymes Escherichia coli Feces Fungi gene expression genes glycoside hydrolase glycosides goats Herbivores Life Sciences Microbiology Neocallimastigaceae Neocallimastix pH effects Plant Sciences Polymerase chain reaction Rumen rumen fungi sheep temperature Temperature effects Xylan endo-1,3-b-xylosidase xylanase xylanases Zoology |
| title | Cloning of a xylanase gene xyn2A from rumen fungus Neocallimastix sp. GMLF2 in Escherichia coli and its partial characterization |
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