Properties of horseradish peroxidase immobilised onto polyaniline

dc.creatorFernandes, KF
dc.creatorLima, CS
dc.creatorLopes, FM
dc.creatorCollins, CH
dc.date2004
dc.dateAPR 30
dc.date2014-11-16T15:34:24Z
dc.date2015-11-26T16:23:36Z
dc.date2014-11-16T15:34:24Z
dc.date2015-11-26T16:23:36Z
dc.date.accessioned2018-03-28T23:04:46Z
dc.date.available2018-03-28T23:04:46Z
dc.identifierProcess Biochemistry. Elsevier Sci Ltd, v. 39, n. 8, n. 957, n. 962, 2004.
dc.identifier1359-5113
dc.identifierWOS:000221135900007
dc.identifier10.1016/S0032-9592(03)00211-5
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/70547
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/70547
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/70547
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1268281
dc.descriptionChemically synthesised polyaniline was used for horseradish peroxidase (HRP) immobilisation after activation with glutaraldehyde. The immobilised enzyme showed better performance than free enzyme when submitted to concentrations of organic solvents (ethanol, acetone and acetonitrile) above 10% (v/v). The immobilised HR-P (PANIG-HRP) also presented a better performance than free enzyme when submitted to heat treatment, with a plateau of activity in the range from 30 to 60degreesC. The pH profile of the immobilised and free enzyme revealed a similar behaviour, although PANIG-HRP exhibited higher activity in the alkaline range (from pH 9.0 to 11.0) and optimum pH displacement of two units towards acidic range. In the best storage conditions the PANIG-HRP was 100% stable for 70 days. A difference in the kinetic parameters K-m, K-cat, K-m.app and K-cat.app were observed; immobilised enzyme presenting a K-m.app of 5.20 mmol 1(-1) and free enzyme 9.58 mmol 1(-1) with pyrogallol as substrate. (C) 2003 Elsevier Ltd. All rights reserved.
dc.description39
dc.description8
dc.description957
dc.description962
dc.languageen
dc.publisherElsevier Sci Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationProcess Biochemistry
dc.relationProcess Biochem.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectpolyaniline
dc.subjecthorseradish peroxidase
dc.subjectimmobilisation
dc.subjectstability
dc.subjectkinetic parameters
dc.subjectFlow-injection Analysis
dc.subjectWater-insoluble Derivatives
dc.subjectEnzyme Reactors
dc.subjectGlucose-oxidase
dc.subjectAlpha-amylase
dc.subjectTrypsin
dc.subjectProteins
dc.subjectSupports
dc.subjectCarrier
dc.subjectDesign
dc.titleProperties of horseradish peroxidase immobilised onto polyaniline
dc.typeArtículos de revistas


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