Başak E.Aydemir T.2024-07-222024-07-2220132169141Xhttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/17173Bovine liver catalase was covalently immobilized onto amino acid-modified chitosan beads. The beads were characterized with SEM, FTIR, TGA and the effects of immobilization on optimum pH and temperature, thermostability, reusability were evaluated. Immobilized catalase showed the maximal enzyme activity at pH 7.0 at 30°C. The kinetic parameters, Km and Vmax, for immobilized catalase on alanine-chitosan beads and lysine-chitosan beads were estimated to be 25.67 mM, 27 mM and 201.39 μmol H2O 2/min, 197.50 μmol H2O2/min, respectively. The activity of the immobilized catalase on Ala-CB and Lys-CB retained 40% of its high initial activity after 100 times of reuse. © 2013 Informa Healthcare USA, Inc.EnglishAlanineAnimalsCatalaseCattleChitosanEnzyme StabilityEnzymes, ImmobilizedFood IndustryGlutaralKineticsLysineMicrospheresTemperatureAcidsChitosanRadioactive waste vitrificationReusabilityalanineamino acidcatalasechitosanlysinenanobeadAminoBovine liver catalaseCatalaseChitosan beadsFTIRInitial activityModificationOptimum pHarticlechemical modificationenzyme activityenzyme immobilizationenzyme kineticsinfrared spectroscopypHscanning electron microscopytemperaturethermostabilityAmino acidsArticle10.3109/10731199.2012.742095