Soluble and immobilized laccase as catalysts for the transformation of substituted phenols
The ability of a laccase from the fungus Rhizoctonia praticola to transform 15 phenolic substrates has been examined. Substrates tested included chlorophenols, methylphenols (cresols) and methoxyphenols. The amount of substrate removed was dependent on the substituent group and position of substitut...
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| Veröffentlicht in: | Enzyme and microbial technology 1986, Vol.8 (3), p.171-177 |
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| creator | Shuttleworth, Kay L. Bollag, Jean-Marc |
| description | The ability of a laccase from the fungus Rhizoctonia praticola
to transform 15 phenolic substrates has been examined. Substrates tested included chlorophenols, methylphenols (cresols) and methoxyphenols. The amount of substrate removed was dependent on the substituent group and position of substitution. Virtually 100% of each of the methoxyphenols was transformed, whereas less than 10% of any of the chlorophenols was transformed. The Rhizoctonia
laccase was immobilized by covalent coupling to Celite. Syringic acid and 2,6-dimethoxyphenol were completely removed by the immobilized enzyme both initially and after several repeated incubations. The addition of syringic acid enhanced the transformation of 2,4-dichlorophenol with free and immobilized laccase. There were no substantial differences in the relative activities of the free and immobilized enzyme. |
| doi_str_mv | 10.1016/0141-0229(86)90108-0 |
| format | Article |
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laccase was immobilized by covalent coupling to Celite. Syringic acid and 2,6-dimethoxyphenol were completely removed by the immobilized enzyme both initially and after several repeated incubations. The addition of syringic acid enhanced the transformation of 2,4-dichlorophenol with free and immobilized laccase. There were no substantial differences in the relative activities of the free and immobilized enzyme.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/0141-0229(86)90108-0</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>biodegradation ; Biological and medical sciences ; Biological treatment of waters ; Biotechnology ; Environment and pollution ; Fundamental and applied biological sciences. Psychology ; immobilized enzyme ; immobilized enzymes ; Industrial applications and implications. Economical aspects ; Laccase ; phenolic pollutants ; phenols ; Rhizoctonia praticola ; soil enzymes</subject><ispartof>Enzyme and microbial technology, 1986, Vol.8 (3), p.171-177</ispartof><rights>1986</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-2ea64d63096b6134481b60898b2a6c01db2cacf3d3d6a7d166cf3147618fad253</citedby><cites>FETCH-LOGICAL-c400t-2ea64d63096b6134481b60898b2a6c01db2cacf3d3d6a7d166cf3147618fad253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0141-0229(86)90108-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8708020$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Shuttleworth, Kay L.</creatorcontrib><creatorcontrib>Bollag, Jean-Marc</creatorcontrib><title>Soluble and immobilized laccase as catalysts for the transformation of substituted phenols</title><title>Enzyme and microbial technology</title><description>The ability of a laccase from the fungus Rhizoctonia praticola
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laccase was immobilized by covalent coupling to Celite. Syringic acid and 2,6-dimethoxyphenol were completely removed by the immobilized enzyme both initially and after several repeated incubations. The addition of syringic acid enhanced the transformation of 2,4-dichlorophenol with free and immobilized laccase. There were no substantial differences in the relative activities of the free and immobilized enzyme.</description><subject>biodegradation</subject><subject>Biological and medical sciences</subject><subject>Biological treatment of waters</subject><subject>Biotechnology</subject><subject>Environment and pollution</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>immobilized enzyme</subject><subject>immobilized enzymes</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Laccase</subject><subject>phenolic pollutants</subject><subject>phenols</subject><subject>Rhizoctonia praticola</subject><subject>soil enzymes</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><recordid>eNp9kEFv1DAQhS1UJJaFf8DBB4TgEBgnxutcKlVVaStV4gBcuFgT29EaOfHicSotvx6nW_XY0-iNvjej9xh7J-CzAKG-gJCigbbtP2r1qQcBuoEXbCP0rm-gh_6MbZ6QV-w10R-AupCwYb9_pLgM0XOcHQ_TlIYQwz_veERrkeqeuMWC8UiF-JgyL3vPS8aZqpiwhDTzNHJaBiqhLKVaD3s_p0hv2MsRI_m3j3PLfn27-nl509x9v769vLhrrAQoTetRSac66NWgRCelFoMC3euhRWVBuKG1aMfOdU7hzgmlqhByp4Qe0bVfuy37cLp7yOnv4qmYKZD1MeLs00KmBu2UFCsoT6DNiSj70RxymDAfjQCzFmnWlszaktHKPBRpoNreP95HshjHmt0GevLqHWhoV-z8hPma9T74bMgGP1vvQva2GJfC83_-A_pUh4M</recordid><startdate>1986</startdate><enddate>1986</enddate><creator>Shuttleworth, Kay L.</creator><creator>Bollag, Jean-Marc</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>1986</creationdate><title>Soluble and immobilized laccase as catalysts for the transformation of substituted phenols</title><author>Shuttleworth, Kay L. ; Bollag, Jean-Marc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-2ea64d63096b6134481b60898b2a6c01db2cacf3d3d6a7d166cf3147618fad253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>biodegradation</topic><topic>Biological and medical sciences</topic><topic>Biological treatment of waters</topic><topic>Biotechnology</topic><topic>Environment and pollution</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>immobilized enzyme</topic><topic>immobilized enzymes</topic><topic>Industrial applications and implications. Economical aspects</topic><topic>Laccase</topic><topic>phenolic pollutants</topic><topic>phenols</topic><topic>Rhizoctonia praticola</topic><topic>soil enzymes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shuttleworth, Kay L.</creatorcontrib><creatorcontrib>Bollag, Jean-Marc</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>Shuttleworth, Kay L.</au><au>Bollag, Jean-Marc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Soluble and immobilized laccase as catalysts for the transformation of substituted phenols</atitle><jtitle>Enzyme and microbial technology</jtitle><date>1986</date><risdate>1986</risdate><volume>8</volume><issue>3</issue><spage>171</spage><epage>177</epage><pages>171-177</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>The ability of a laccase from the fungus Rhizoctonia praticola
to transform 15 phenolic substrates has been examined. Substrates tested included chlorophenols, methylphenols (cresols) and methoxyphenols. The amount of substrate removed was dependent on the substituent group and position of substitution. Virtually 100% of each of the methoxyphenols was transformed, whereas less than 10% of any of the chlorophenols was transformed. The Rhizoctonia
laccase was immobilized by covalent coupling to Celite. Syringic acid and 2,6-dimethoxyphenol were completely removed by the immobilized enzyme both initially and after several repeated incubations. The addition of syringic acid enhanced the transformation of 2,4-dichlorophenol with free and immobilized laccase. There were no substantial differences in the relative activities of the free and immobilized enzyme.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/0141-0229(86)90108-0</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-0229 |
| ispartof | Enzyme and microbial technology, 1986, Vol.8 (3), p.171-177 |
| issn | 0141-0229 1879-0909 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_14436415 |
| source | Access via ScienceDirect (Elsevier) |
| subjects | biodegradation Biological and medical sciences Biological treatment of waters Biotechnology Environment and pollution Fundamental and applied biological sciences. Psychology immobilized enzyme immobilized enzymes Industrial applications and implications. Economical aspects Laccase phenolic pollutants phenols Rhizoctonia praticola soil enzymes |
| title | Soluble and immobilized laccase as catalysts for the transformation of substituted phenols |
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