dc.creatorDuran N.
dc.creatorRosa M.A.
dc.creatorD'Annibale A.
dc.creatorGianfreda L.
dc.date2002
dc.date2015-06-30T16:40:25Z
dc.date2015-11-26T15:31:32Z
dc.date2015-06-30T16:40:25Z
dc.date2015-11-26T15:31:32Z
dc.date.accessioned2018-03-28T22:39:58Z
dc.date.available2018-03-28T22:39:58Z
dc.identifier
dc.identifierEnzyme And Microbial Technology. , v. 31, n. 7, p. 907 - 931, 2002.
dc.identifier1410229
dc.identifier10.1016/S0141-0229(02)00214-4
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0037010857&partnerID=40&md5=4aa180d216781be9a404e701b5b591ca
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/101488
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/101488
dc.identifier2-s2.0-0037010857
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1262249
dc.descriptionThis review summarizes all the research efforts that have been spent to immobilize laccase and tyrosinase for various applications, including synthetic and analytical purposes, bioremediation, wastewater treatment, and must and wine stabilization. All immobilization procedures used in these areas are discussed. Considerations on the efficacy of immobilized copper oxidases and products, in addition to their kinetic parameters are also discussed. The available data indicate that the immobilization of laccase into cationic polymer cross-linked with epichlorohydrin appears to be a promising procedure for industrial applications. The development of laccase and tyrosinase-based biosensors to monitor a wide range of compounds appears to be at a mature stage of technology. © 2002 Elsevier Science Inc. All rights reserved.
dc.description31
dc.description7
dc.description907
dc.description931
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dc.languageen
dc.publisher
dc.relationEnzyme and Microbial Technology
dc.rightsfechado
dc.sourceScopus
dc.titleApplications Of Laccases And Tyrosinases (phenoloxidases) Immobilized On Different Supports: A Review
dc.typeArtículos de revistas


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