Laccases: blue enzymes for green chemistry
Laccases are oxidoreductases belonging to the multinuclear copper-containing oxidases; they catalyse the monoelectronic oxidation of substrates at the expense of molecular oxygen. Interest in these essentially ‘eco-friendly’ enzymes – they work with air and produce water as the only by-product – has...
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description | Laccases are oxidoreductases belonging to the multinuclear copper-containing oxidases; they catalyse the monoelectronic oxidation of substrates at the expense of molecular oxygen. Interest in these essentially ‘eco-friendly’ enzymes – they work with air and produce water as the only by-product – has grown significantly in recent years: their uses span from the textile to the pulp and paper industries, and from food applications to bioremediation processes. Laccases also have uses in organic synthesis, where their typical substrates are phenols and amines, and the reaction products are dimers and oligomers derived from the coupling of reactive radical intermediates. Here, we provide a brief discussion of this interesting group of enzymes, increased knowledge of which will promote laccase-based industrial processes in the future. |
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Interest in these essentially ‘eco-friendly’ enzymes – they work with air and produce water as the only by-product – has grown significantly in recent years: their uses span from the textile to the pulp and paper industries, and from food applications to bioremediation processes. Laccases also have uses in organic synthesis, where their typical substrates are phenols and amines, and the reaction products are dimers and oligomers derived from the coupling of reactive radical intermediates. Here, we provide a brief discussion of this interesting group of enzymes, increased knowledge of which will promote laccase-based industrial processes in the future.</description><identifier>ISSN: 0167-7799</identifier><identifier>EISSN: 1879-3096</identifier><identifier>DOI: 10.1016/j.tibtech.2006.03.006</identifier><identifier>PMID: 16574262</identifier><identifier>CODEN: TRBIDM</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amines ; Aqueous solutions ; Biocatalysts ; Biological and medical sciences ; Bioremediation ; Biotechnology ; Biotechnology - methods ; Biotechnology - trends ; Chemical Industry - methods ; Chemical Industry - trends ; Copper ; Enzyme Activation ; enzyme activity ; Enzymes ; Fruit juices ; Fundamental and applied biological sciences. 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Interest in these essentially ‘eco-friendly’ enzymes – they work with air and produce water as the only by-product – has grown significantly in recent years: their uses span from the textile to the pulp and paper industries, and from food applications to bioremediation processes. Laccases also have uses in organic synthesis, where their typical substrates are phenols and amines, and the reaction products are dimers and oligomers derived from the coupling of reactive radical intermediates. 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Psychology</subject><subject>Green chemistry</subject><subject>industrial applications</subject><subject>laccase</subject><subject>Laccase - chemistry</subject><subject>Laccase - classification</subject><subject>Laccase - metabolism</subject><subject>Lignin</subject><subject>literature reviews</subject><subject>Phenols</subject><subject>Pulp & paper industry</subject><subject>Substrate Specificity</subject><issn>0167-7799</issn><issn>1879-3096</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0U1r3DAQBmBRGpptmp-Q1FDSQ8COxvqycikh9AsWemhzFrI0Srx47VSyC9tfXy1rCPSyp7k8M9LMS8gF0AooyJtNNXXthO6pqimVFWVVLq_IChqlS0a1fE1W2alSKa1PyduUNpRSpjS8IacgheK1rFfkem2dswnTbdH2MxY4_N1tMRVhjMVjRBwK94TbLk1x946cBNsnPF_qGXn48vnX_bdy_ePr9_u7dekE51MZmA9MedEIr7VwilOgngbgDFvkyqEGaCWr21YG8FZ6lEExEEIF0QRG2Rn5eJj7HMffM6bJ5Pcd9r0dcJyTkUpzIZvjsNaMKyGOQ1CgmZCQ4Yf_4Gac45C3NSCoYCAbzrMSB-XimFLEYJ5jt7VxZ4CafThmY5ZwzD4cQ5nJJfddLtPndov-pWtJI4OrBdjkbB-iHVyXXpxSXDZKZPf-4IIdjX2M2Tz8rCmwfOoG6nq_8aeDwBzUnw6jSa7DwaHvIrrJ-LE78tl_SYe16A</recordid><startdate>20060501</startdate><enddate>20060501</enddate><creator>Riva, Sergio</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><general>Elsevier Limited</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QF</scope><scope>7QO</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88C</scope><scope>88E</scope><scope>8AO</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0S</scope><scope>M0T</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20060501</creationdate><title>Laccases: blue enzymes for green chemistry</title><author>Riva, Sergio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-f3df37d585d995c74010d0f143ebe47ce911b632bb6f1da6de6f731557f58f303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amines</topic><topic>Aqueous solutions</topic><topic>Biocatalysts</topic><topic>Biological and medical sciences</topic><topic>Bioremediation</topic><topic>Biotechnology</topic><topic>Biotechnology - methods</topic><topic>Biotechnology - trends</topic><topic>Chemical Industry - methods</topic><topic>Chemical Industry - trends</topic><topic>Copper</topic><topic>Enzyme Activation</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Fruit juices</topic><topic>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Trends in biotechnology (Regular ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Riva, Sergio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Laccases: blue enzymes for green chemistry</atitle><jtitle>Trends in biotechnology (Regular ed.)</jtitle><addtitle>Trends Biotechnol</addtitle><date>2006-05-01</date><risdate>2006</risdate><volume>24</volume><issue>5</issue><spage>219</spage><epage>226</epage><pages>219-226</pages><issn>0167-7799</issn><eissn>1879-3096</eissn><coden>TRBIDM</coden><abstract>Laccases are oxidoreductases belonging to the multinuclear copper-containing oxidases; they catalyse the monoelectronic oxidation of substrates at the expense of molecular oxygen. Interest in these essentially ‘eco-friendly’ enzymes – they work with air and produce water as the only by-product – has grown significantly in recent years: their uses span from the textile to the pulp and paper industries, and from food applications to bioremediation processes. Laccases also have uses in organic synthesis, where their typical substrates are phenols and amines, and the reaction products are dimers and oligomers derived from the coupling of reactive radical intermediates. Here, we provide a brief discussion of this interesting group of enzymes, increased knowledge of which will promote laccase-based industrial processes in the future.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>16574262</pmid><doi>10.1016/j.tibtech.2006.03.006</doi><tpages>8</tpages></addata></record> |
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subjects | Amines Aqueous solutions Biocatalysts Biological and medical sciences Bioremediation Biotechnology Biotechnology - methods Biotechnology - trends Chemical Industry - methods Chemical Industry - trends Copper Enzyme Activation enzyme activity Enzymes Fruit juices Fundamental and applied biological sciences. Psychology Green chemistry industrial applications laccase Laccase - chemistry Laccase - classification Laccase - metabolism Lignin literature reviews Phenols Pulp & paper industry Substrate Specificity |
title | Laccases: blue enzymes for green chemistry |
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