Characterization of the multiple forms of beta-xylanase produced by a Streptomyces sp. growing on lignocellulose
Streptomyces sp. strain EC10 degraded efficiently the hemicellulose fraction of wheat straw. Three forms of beta -xylanases detected in the culture filtrate were purified by precipitation with ammonium sulphate, chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. The three pur...
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| Veröffentlicht in: | Applied microbiology and biotechnology 1992-01, Vol.36 (6), p.733-738 |
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| container_title | Applied microbiology and biotechnology |
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| creator | Lumba, F.L Penninckx, M.J |
| description | Streptomyces sp. strain EC10 degraded efficiently the hemicellulose fraction of wheat straw. Three forms of beta -xylanases detected in the culture filtrate were purified by precipitation with ammonium sulphate, chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. The three purified enzymes (X sub(IA), X sub(IB) and X' sub(II)) were homogeneous by polyacrylamide gel electrophoresis. The enzymes were typical non-debranching endo- beta -xylanases (1,4- beta -D-xylan xylanohydrolases; E.C.3.2.1.8) with respective relative molecular weights of 32,000, 22,000, 21,000 and isoelectric points of 6.8, 8.9 and 5.2. The enzymes were highly specific for xylans and showed optimal activity at pH 7.0-8.0 and 60 degree C. |
| doi_str_mv | 10.1007/BF00172184 |
| format | Article |
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Three forms of beta -xylanases detected in the culture filtrate were purified by precipitation with ammonium sulphate, chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. The three purified enzymes (X sub(IA), X sub(IB) and X' sub(II)) were homogeneous by polyacrylamide gel electrophoresis. The enzymes were typical non-debranching endo- beta -xylanases (1,4- beta -D-xylan xylanohydrolases; E.C.3.2.1.8) with respective relative molecular weights of 32,000, 22,000, 21,000 and isoelectric points of 6.8, 8.9 and 5.2. 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Three forms of beta -xylanases detected in the culture filtrate were purified by precipitation with ammonium sulphate, chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. The three purified enzymes (X sub(IA), X sub(IB) and X' sub(II)) were homogeneous by polyacrylamide gel electrophoresis. The enzymes were typical non-debranching endo- beta -xylanases (1,4- beta -D-xylan xylanohydrolases; E.C.3.2.1.8) with respective relative molecular weights of 32,000, 22,000, 21,000 and isoelectric points of 6.8, 8.9 and 5.2. The enzymes were highly specific for xylans and showed optimal activity at pH 7.0-8.0 and 60 degree C.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>endo-1,4- beta -xylanase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>lignocellulose</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Streptomyces</subject><subject>wheat straw</subject><subject>xylan 1,4-beta-xylosidase</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNotkE1LxDAYhIMouH5c_APmIN6qSd9m0x518QsED-q5vM2-WStpU5MUXX-9ET0NDA_DzDB2IsWFFEJfXt8KIXUp62qHLWQFZSGWstpli-yqQqum3mcHMb5nqqyXywWbVm8Y0CQK_Tem3o_cW57eiA-zS_3kiFsfhvjrdpSw-No6HDESn4Jfz4bWvNty5M8p0JT8sDUUeZwu-Cb4z37c8Bzo-s3oDTk3Ox_piO1ZdJGO__WQvd7evKzui8enu4fV1WNhSw2p6KTSjUEotQGqO7luFNgOK1h3uhFWEGkpO02gazR5p2oqBOhqsgLImBIO2flfbi76MVNM7dDH3xY4kp9jK5dSSdVABs_-QYwGnQ04mj62U-gHDNtW5Rc1VBk7_cMs-hY3ISOvz6WQkJ-tKwUAP6f-c_c</recordid><startdate>19920101</startdate><enddate>19920101</enddate><creator>Lumba, F.L</creator><creator>Penninckx, M.J</creator><general>Springer</general><scope>FBQ</scope><scope>IQODW</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19920101</creationdate><title>Characterization of the multiple forms of beta-xylanase produced by a Streptomyces sp. growing on lignocellulose</title><author>Lumba, F.L ; Penninckx, M.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f273t-b1579ca327c3e8b1d953fba43db790f0ee711b7e378ac432594a33b8ef03ecc23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>endo-1,4- beta -xylanase</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>lignocellulose</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Streptomyces</topic><topic>wheat straw</topic><topic>xylan 1,4-beta-xylosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lumba, F.L</creatorcontrib><creatorcontrib>Penninckx, M.J</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lumba, F.L</au><au>Penninckx, M.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the multiple forms of beta-xylanase produced by a Streptomyces sp. growing on lignocellulose</atitle><jtitle>Applied microbiology and biotechnology</jtitle><date>1992-01-01</date><risdate>1992</risdate><volume>36</volume><issue>6</issue><spage>733</spage><epage>738</epage><pages>733-738</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>Streptomyces sp. strain EC10 degraded efficiently the hemicellulose fraction of wheat straw. Three forms of beta -xylanases detected in the culture filtrate were purified by precipitation with ammonium sulphate, chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-100. The three purified enzymes (X sub(IA), X sub(IB) and X' sub(II)) were homogeneous by polyacrylamide gel electrophoresis. The enzymes were typical non-debranching endo- beta -xylanases (1,4- beta -D-xylan xylanohydrolases; E.C.3.2.1.8) with respective relative molecular weights of 32,000, 22,000, 21,000 and isoelectric points of 6.8, 8.9 and 5.2. The enzymes were highly specific for xylans and showed optimal activity at pH 7.0-8.0 and 60 degree C.</abstract><cop>Berlin</cop><pub>Springer</pub><doi>10.1007/BF00172184</doi><tpages>6</tpages></addata></record> |
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| ispartof | Applied microbiology and biotechnology, 1992-01, Vol.36 (6), p.733-738 |
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| subjects | Bacteriology Biological and medical sciences endo-1,4- beta -xylanase Fundamental and applied biological sciences. Psychology lignocellulose Metabolism. Enzymes Microbiology Streptomyces wheat straw xylan 1,4-beta-xylosidase |
| title | Characterization of the multiple forms of beta-xylanase produced by a Streptomyces sp. growing on lignocellulose |
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