Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase
Laccase from the white rot fungus Coriolus versicolor was immobilized on Celite R-637 by covalent binding with glutaraldehyde. After a sharp primary decline in activity (up to 50%), the retained enzyme activity was stable over a storage period of 33 days at 4 degrees C. A comparative study of solubl...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2001-10, Vol.57 (1/2), p.85-91 |
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| creator | Leontievsky, A.A Myasoedova, N.M Baskunov, B.P Golovleva, L.A Bucke, C Evans, C.S |
| description | Laccase from the white rot fungus Coriolus versicolor was immobilized on Celite R-637 by covalent binding with glutaraldehyde. After a sharp primary decline in activity (up to 50%), the retained enzyme activity was stable over a storage period of 33 days at 4 degrees C. A comparative study of soluble and immobilized laccases revealed the increased resistance of immobilized enzyme to the unfavourable effects of alkaline pH, high temperature and the action of inhibitors. A combination of these properties of immobilized laccase resulted in the ability to oxidize 2,4,6-trichlorophenol (2,4,6-TCP) at 50 degrees C at pH 7.0. The reactions of soluble and immobilized laccase with 2,4,6-TCP were examined in the presence and absence of redox mediators. 3,5-Dichlorocatechol, 2,6-dichloro-1,4-benzoquinone and 2,6-dichloro-1,4-hydroquinone were found to be the primary products of 2,4,6-TCP oxidation by laccase; oligo- and polymeric compounds were also found. |
| doi_str_mv | 10.1007/s002530100756 |
| format | Article |
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After a sharp primary decline in activity (up to 50%), the retained enzyme activity was stable over a storage period of 33 days at 4 degrees C. A comparative study of soluble and immobilized laccases revealed the increased resistance of immobilized enzyme to the unfavourable effects of alkaline pH, high temperature and the action of inhibitors. A combination of these properties of immobilized laccase resulted in the ability to oxidize 2,4,6-trichlorophenol (2,4,6-TCP) at 50 degrees C at pH 7.0. The reactions of soluble and immobilized laccase with 2,4,6-TCP were examined in the presence and absence of redox mediators. 3,5-Dichlorocatechol, 2,6-dichloro-1,4-benzoquinone and 2,6-dichloro-1,4-hydroquinone were found to be the primary products of 2,4,6-TCP oxidation by laccase; oligo- and polymeric compounds were also found.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s002530100756</identifier><identifier>PMID: 11693939</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>2,4,6-trichlorophenol ; 2,6-dichloro-1,4-benzoquinone ; 2,6-dichloro-1,4-hydroquinone ; 3,5-dichlorocatechol ; Basidiomycota - enzymology ; Biotransformation ; Chlorophenols - pharmacokinetics ; Comparative studies ; Coriolus versicolor ; Enzymatic activity ; enzyme activity ; Enzymes ; Enzymes, Immobilized - metabolism ; glutaraldehyde ; High temperature ; immobilized enzymes ; Laccase ; oxidation ; Oxidoreductases - metabolism ; Solubility ; storage time ; temperature ; white-rot fungi</subject><ispartof>Applied microbiology and biotechnology, 2001-10, Vol.57 (1/2), p.85-91</ispartof><rights>Springer-Verlag 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-baec67865b24aec88036e97605a86e8344a51109da2a177a907fb799c1fb226f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11693939$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leontievsky, A.A</creatorcontrib><creatorcontrib>Myasoedova, N.M</creatorcontrib><creatorcontrib>Baskunov, B.P</creatorcontrib><creatorcontrib>Golovleva, L.A</creatorcontrib><creatorcontrib>Bucke, C</creatorcontrib><creatorcontrib>Evans, C.S</creatorcontrib><title>Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><description>Laccase from the white rot fungus Coriolus versicolor was immobilized on Celite R-637 by covalent binding with glutaraldehyde. After a sharp primary decline in activity (up to 50%), the retained enzyme activity was stable over a storage period of 33 days at 4 degrees C. A comparative study of soluble and immobilized laccases revealed the increased resistance of immobilized enzyme to the unfavourable effects of alkaline pH, high temperature and the action of inhibitors. A combination of these properties of immobilized laccase resulted in the ability to oxidize 2,4,6-trichlorophenol (2,4,6-TCP) at 50 degrees C at pH 7.0. The reactions of soluble and immobilized laccase with 2,4,6-TCP were examined in the presence and absence of redox mediators. 3,5-Dichlorocatechol, 2,6-dichloro-1,4-benzoquinone and 2,6-dichloro-1,4-hydroquinone were found to be the primary products of 2,4,6-TCP oxidation by laccase; oligo- and polymeric compounds were also found.</description><subject>2,4,6-trichlorophenol</subject><subject>2,6-dichloro-1,4-benzoquinone</subject><subject>2,6-dichloro-1,4-hydroquinone</subject><subject>3,5-dichlorocatechol</subject><subject>Basidiomycota - enzymology</subject><subject>Biotransformation</subject><subject>Chlorophenols - pharmacokinetics</subject><subject>Comparative studies</subject><subject>Coriolus versicolor</subject><subject>Enzymatic activity</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>glutaraldehyde</subject><subject>High temperature</subject><subject>immobilized enzymes</subject><subject>Laccase</subject><subject>oxidation</subject><subject>Oxidoreductases - metabolism</subject><subject>Solubility</subject><subject>storage time</subject><subject>temperature</subject><subject>white-rot 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glutaraldehyde. After a sharp primary decline in activity (up to 50%), the retained enzyme activity was stable over a storage period of 33 days at 4 degrees C. A comparative study of soluble and immobilized laccases revealed the increased resistance of immobilized enzyme to the unfavourable effects of alkaline pH, high temperature and the action of inhibitors. A combination of these properties of immobilized laccase resulted in the ability to oxidize 2,4,6-trichlorophenol (2,4,6-TCP) at 50 degrees C at pH 7.0. The reactions of soluble and immobilized laccase with 2,4,6-TCP were examined in the presence and absence of redox mediators. 3,5-Dichlorocatechol, 2,6-dichloro-1,4-benzoquinone and 2,6-dichloro-1,4-hydroquinone were found to be the primary products of 2,4,6-TCP oxidation by laccase; oligo- and polymeric compounds were also found.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>11693939</pmid><doi>10.1007/s002530100756</doi><tpages>7</tpages></addata></record> |
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| ispartof | Applied microbiology and biotechnology, 2001-10, Vol.57 (1/2), p.85-91 |
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| subjects | 2,4,6-trichlorophenol 2,6-dichloro-1,4-benzoquinone 2,6-dichloro-1,4-hydroquinone 3,5-dichlorocatechol Basidiomycota - enzymology Biotransformation Chlorophenols - pharmacokinetics Comparative studies Coriolus versicolor Enzymatic activity enzyme activity Enzymes Enzymes, Immobilized - metabolism glutaraldehyde High temperature immobilized enzymes Laccase oxidation Oxidoreductases - metabolism Solubility storage time temperature white-rot fungi |
| title | Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase |
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