Immobilization of tyrosinase on chitosan-clay composite beads

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dc.contributor.authorDinçer A.
dc.contributor.authorBecerik S.
dc.contributor.authorAydemir T.
dc.date.accessioned2024-07-22T08:19:30Z
dc.date.available2024-07-22T08:19:30Z
dc.date.issued2012
dc.description.abstractTyrosinase was immobilized on glutaraldehyde crosslinked chitosan-clay composite beads and used for phenol removal. Immobilization yield, loading efficiency and activity of tyrosinase immobilized beads were found as 67%, 25% and 1400U/g beads respectively. Optimum pH of the free and immobilized enzyme was found as pH 7.0. Optimum temperature of the free and immobilized enzyme was determined as 25-30°C and 25°C respectively. The kinetic parameters of free and immobilized tyrosinase were calculated using l-catechol as a substrate and Km value for free and immobilized tyrosinase were found as 0.93mM and 1.7mM respectively. After seven times of repeated tests, each over 150min, the efficiency of phenol removal using same immobilized tyrosinase beads were decreased to 43%. © 2011 Elsevier B.V.
dc.identifier.DOI-ID10.1016/j.ijbiomac.2011.11.020
dc.identifier.issn01418130
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/17708
dc.language.isoEnglish
dc.publisherElsevier B.V.
dc.subjectchitosan
dc.subjectglutaraldehyde
dc.subjectmonophenol monooxygenase
dc.subjectphenol
dc.subjectadsorption
dc.subjectaqueous solution
dc.subjectarticle
dc.subjectcross linking
dc.subjectenzyme activity
dc.subjectenzyme immobilization
dc.subjectenzyme kinetics
dc.subjectoxidation
dc.subjectpH
dc.subjectprotein stability
dc.subjectscanning electron microscopy
dc.subjecttemperature
dc.subjectthermostability
dc.titleImmobilization of tyrosinase on chitosan-clay composite beads
dc.typeArticle

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