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dc.contributor.authorJegan Roy, J-
dc.contributor.authorEmilia Abraham, T-
dc.contributor.authorAbhijith, K S-
dc.contributor.authorSujith Kumar, P V-
dc.contributor.authorThakur, M S-
dc.date.accessioned2015-08-05T11:27:21Z-
dc.date.available2015-08-05T11:27:21Z-
dc.date.issued2005-
dc.identifier.citationBiosensors and Bioelectronics 21(1):206–211; Jul 2005en_US
dc.identifier.issn0956-5663-
dc.identifier.urihttp://ir.niist.res.in:8080/jspui/handle/123456789/1894-
dc.description.abstractCross-linked enzyme crystals (CLECs) are a versatile form of biocatalyst that can also be used for biosensor application. Laccase from Trametes versicolor (E.C.1.10.3.2) was crystallized, cross-linked and lyophilized with beta-cyclodextrin. The CLEC laccase was found to be highly active towards phenols like 2-amino phenol, guaiacol, catechol, pyrogallol, catechin and ABTS (non-phenolic). The CLEC laccase was embedded in 30% polyvinylpropylidone (PVP) gel and mounted into an electrode to make the sensor. The biosensor was used to detect the phenols in 50-1000 mu mol concentration level. Phenols with lower molecular weight such as 2-amino phenol, catechol and pyrogallol gave a short response time where as the higher molecular weight substrates like catechin and ABTS had comparatively a long response time. The optimum pH of the analyte was 5.5-6.0 when catechol was used as substrate. The CLEC laccase retained good activity for over 3 months.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectCLECen_US
dc.subjectLaccaseen_US
dc.subjectBiosensoren_US
dc.subjectCross-linkingen_US
dc.subjectGlutaraldehydeen_US
dc.titleBiosensor for the determination of phenols based on Cross-Linked Enzyme Crystals (CLEC) of laccaseen_US
dc.typeArticleen_US
Appears in Collections:2005

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