Zaidan U.H.Rahman M.B.A.Basri M.Othman S.S.Rahman R.N.Z.R.A.Salleh A.B.2024-05-282024-05-282010169131710.1016/j.clay.2009.11.0042-s2.0-75349090073https://www.scopus.com/inward/record.uri?eid=2-s2.0-75349090073&doi=10.1016%2fj.clay.2009.11.004&partnerID=40&md5=ae1334d7ce19f1d38ca814bbd26a21dehttps://oarep.usim.edu.my/handle/123456789/8893Mica was modified either by acid treatment, grafting with aminopropyl-, octyl-, vinyl-, mercapto- and glycidoxy-triethoxysilanes, and activation of pre-treated support with glutaraldehyde (Glu). The derivatives were characterized by X-ray diffraction (XRD), infra-red spectroscopy (FTIR), surface area and porosity analysis, scanning electron microscopy coupled with energy dispersive X-ray (SEM-EDX) and transmission electron microscopy (TEM) techniques. The modified micas were used for immobilization of lipase from Candida rugosa (CRL). Activity of the lipase was determined by esterification and exhibited the improved activity than the free enzyme following the order; Amino-CRL > Glu-Amino-CRL > Octyl-CRL > Vinyl-CRL > Glycidoxy-CRL > Mercapto-CRL > Mica-CRL. Lipase immobilized mica showed enhanced protein loading (up to 8.22 mg protein/g support) and immobilization (up to 78%) compared to the free lipase and unmodified mica. � 2009 Elsevier B.V. All rights reserved.en-USCandida rugosa lipaseEsterificationImmobilizationMicaSilanizationAcid treatmentsAminopropylCandida rugosa lipaseEnergy dispersive x-rayFree enzymeFTIRGlutaraldehydesLipase from Candida rugosaLipase immobilizationProtein loadingsSEM-EDXSilanizationsSilylationsSurface areaTEMAldehydesEnzyme activityEnzyme immobilizationEsterificationEstersFourier transform infrared spectroscopyMicaScanning electron microscopyTransmission electron microscopyX ray diffractionX ray diffraction analysisSilicate mineralscatalystchemical reactionenzyme activityesterimmobilizationmicaproteinCandida rugosaMicasArticle2762824743924ACLSE