Purification and characterization of two d-xylanases from Trichoderma harzianum
Two endo-1,4-β- d-xylanases (1,4-β- d-xylan xylanohydrolase, EC 3.2.1.8) from Trichoderma harzianum E58 have been purified by ultrafiltration and chromatography on carboxymethyl-Sepharose, phenyl-Sepharose and Sephadex G-75. The d-xylanases were shown to be homogeneous by the criteria of dodecyl sul...
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| Veröffentlicht in: | Enzyme and microbial technology 1985, Vol.7 (9), p.425-430 |
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| creator | Tan, L.U.L. Wong, K.K.Y. Yu, E.K.C. Saddler, J.N. |
| description | Two endo-1,4-β-
d-xylanases (1,4-β-
d-xylan xylanohydrolase, EC 3.2.1.8) from
Trichoderma harzianum
E58 have been purified by ultrafiltration and chromatography on carboxymethyl-Sepharose, phenyl-Sepharose and Sephadex G-75. The
d-xylanases were shown to be homogeneous by the criteria of dodecyl sulphate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weights were estimated to be 20 000 and 29 000, with pl values of 9.4 and 9.5, respectively. Typically, 456 mg of the 20 000 dalton and 1.9 mg of the 29 000 dalton
d-xylanases were purified from 4.2 litre of culture filtrate with specific activities of 370 and 75 U mg
−1,
respectively. Optimum
d-xylanase activities were obtained when the enzymes were incubated at pH 5, 50°C, for the 20 000 dalton protein and pH 5, 60°C for the 29 000 dalton protein
. |
| doi_str_mv | 10.1016/0141-0229(85)90041-9 |
| format | Article |
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d-xylanases (1,4-β-
d-xylan xylanohydrolase, EC 3.2.1.8) from
Trichoderma harzianum
E58 have been purified by ultrafiltration and chromatography on carboxymethyl-Sepharose, phenyl-Sepharose and Sephadex G-75. The
d-xylanases were shown to be homogeneous by the criteria of dodecyl sulphate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weights were estimated to be 20 000 and 29 000, with pl values of 9.4 and 9.5, respectively. Typically, 456 mg of the 20 000 dalton and 1.9 mg of the 29 000 dalton
d-xylanases were purified from 4.2 litre of culture filtrate with specific activities of 370 and 75 U mg
−1,
respectively. Optimum
d-xylanase activities were obtained when the enzymes were incubated at pH 5, 50°C, for the 20 000 dalton protein and pH 5, 60°C for the 29 000 dalton protein
.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/0141-0229(85)90041-9</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Biological and medical sciences ; Biotechnology ; cellulase ; Cellulose ; chromatographies ; d-xylanases ; endo-1,4- beta -D-xylosidase ; Enzyme engineering ; Food industries ; Fundamental and applied biological sciences. Psychology ; Improved methods for extraction and purification of enzymes ; Methods. Procedures. Technologies ; purification ; Trichoderma harzianum ; ultrafiltration ; Use and upgrading of agricultural and food by-products. Biotechnology</subject><ispartof>Enzyme and microbial technology, 1985, Vol.7 (9), p.425-430</ispartof><rights>1985</rights><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c308t-1d22a2a2ab15fbd83fa240992f21f839ffdd353eb1522bed62df35307956dd693</citedby><cites>FETCH-LOGICAL-c308t-1d22a2a2ab15fbd83fa240992f21f839ffdd353eb1522bed62df35307956dd693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0141022985900419$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9187644$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9238252$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Tan, L.U.L.</creatorcontrib><creatorcontrib>Wong, K.K.Y.</creatorcontrib><creatorcontrib>Yu, E.K.C.</creatorcontrib><creatorcontrib>Saddler, J.N.</creatorcontrib><title>Purification and characterization of two d-xylanases from Trichoderma harzianum</title><title>Enzyme and microbial technology</title><description>Two endo-1,4-β-
d-xylanases (1,4-β-
d-xylan xylanohydrolase, EC 3.2.1.8) from
Trichoderma harzianum
E58 have been purified by ultrafiltration and chromatography on carboxymethyl-Sepharose, phenyl-Sepharose and Sephadex G-75. The
d-xylanases were shown to be homogeneous by the criteria of dodecyl sulphate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weights were estimated to be 20 000 and 29 000, with pl values of 9.4 and 9.5, respectively. Typically, 456 mg of the 20 000 dalton and 1.9 mg of the 29 000 dalton
d-xylanases were purified from 4.2 litre of culture filtrate with specific activities of 370 and 75 U mg
−1,
respectively. Optimum
d-xylanase activities were obtained when the enzymes were incubated at pH 5, 50°C, for the 20 000 dalton protein and pH 5, 60°C for the 29 000 dalton protein
.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>cellulase</subject><subject>Cellulose</subject><subject>chromatographies</subject><subject>d-xylanases</subject><subject>endo-1,4- beta -D-xylosidase</subject><subject>Enzyme engineering</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Improved methods for extraction and purification of enzymes</subject><subject>Methods. Procedures. Technologies</subject><subject>purification</subject><subject>Trichoderma harzianum</subject><subject>ultrafiltration</subject><subject>Use and upgrading of agricultural and food by-products. Biotechnology</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><recordid>eNqFkctOwzAQRS0EEqXwByyyQAgWAXucpPEGCVW8pEplUdaW64dqlMTFToD263FI1SXIC2vGZ67uXCN0TvANwaS4xSQjKQZgV2V-zTCOFTtAI1JOWIoZZodotEeO0UkI7xjHRoZHaP7aeWusFK11TSIalciV8EK22tvt0HQmab9cotLvTSUaEXRIjHd1svBWrpzSvhZJnNla0XT1KToyogr6bHeP0dvjw2L6nM7mTy_T-1kqKS7blCgA0Z8lyc1SldQIyDBjYICYkjJjlKI51fEZYKlVAcrEGk9YXihVMDpGl4Pu2ruPToeW1zZIXUWH2nWBx-3oBCCPYDaA0rsQvDZ87W0t_IYTzPv0eB8N76PhZc5_0-O9_sVOXwQpKuNFI23YzzKgJeTwLxa_oIhOxuhuwHSM5NNqz4O0upFaWa9ly5Wzf9v5AdgQkFk</recordid><startdate>1985</startdate><enddate>1985</enddate><creator>Tan, L.U.L.</creator><creator>Wong, K.K.Y.</creator><creator>Yu, E.K.C.</creator><creator>Saddler, J.N.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope></search><sort><creationdate>1985</creationdate><title>Purification and characterization of two d-xylanases from Trichoderma harzianum</title><author>Tan, L.U.L. ; Wong, K.K.Y. ; Yu, E.K.C. ; Saddler, J.N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c308t-1d22a2a2ab15fbd83fa240992f21f839ffdd353eb1522bed62df35307956dd693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>cellulase</topic><topic>Cellulose</topic><topic>chromatographies</topic><topic>d-xylanases</topic><topic>endo-1,4- beta -D-xylosidase</topic><topic>Enzyme engineering</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Improved methods for extraction and purification of enzymes</topic><topic>Methods. Procedures. Technologies</topic><topic>purification</topic><topic>Trichoderma harzianum</topic><topic>ultrafiltration</topic><topic>Use and upgrading of agricultural and food by-products. Biotechnology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tan, L.U.L.</creatorcontrib><creatorcontrib>Wong, K.K.Y.</creatorcontrib><creatorcontrib>Yu, E.K.C.</creatorcontrib><creatorcontrib>Saddler, J.N.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tan, L.U.L.</au><au>Wong, K.K.Y.</au><au>Yu, E.K.C.</au><au>Saddler, J.N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of two d-xylanases from Trichoderma harzianum</atitle><jtitle>Enzyme and microbial technology</jtitle><date>1985</date><risdate>1985</risdate><volume>7</volume><issue>9</issue><spage>425</spage><epage>430</epage><pages>425-430</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>Two endo-1,4-β-
d-xylanases (1,4-β-
d-xylan xylanohydrolase, EC 3.2.1.8) from
Trichoderma harzianum
E58 have been purified by ultrafiltration and chromatography on carboxymethyl-Sepharose, phenyl-Sepharose and Sephadex G-75. The
d-xylanases were shown to be homogeneous by the criteria of dodecyl sulphate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weights were estimated to be 20 000 and 29 000, with pl values of 9.4 and 9.5, respectively. Typically, 456 mg of the 20 000 dalton and 1.9 mg of the 29 000 dalton
d-xylanases were purified from 4.2 litre of culture filtrate with specific activities of 370 and 75 U mg
−1,
respectively. Optimum
d-xylanase activities were obtained when the enzymes were incubated at pH 5, 50°C, for the 20 000 dalton protein and pH 5, 60°C for the 29 000 dalton protein
.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/0141-0229(85)90041-9</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-0229 |
| ispartof | Enzyme and microbial technology, 1985, Vol.7 (9), p.425-430 |
| issn | 0141-0229 1879-0909 |
| language | eng |
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| source | Elsevier ScienceDirect Journals |
| subjects | Biological and medical sciences Biotechnology cellulase Cellulose chromatographies d-xylanases endo-1,4- beta -D-xylosidase Enzyme engineering Food industries Fundamental and applied biological sciences. Psychology Improved methods for extraction and purification of enzymes Methods. Procedures. Technologies purification Trichoderma harzianum ultrafiltration Use and upgrading of agricultural and food by-products. Biotechnology |
| title | Purification and characterization of two d-xylanases from Trichoderma harzianum |
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