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Silylation of mica for lipase immobilization as biocatalysts in esterification

Zaidan, Uswatun Hasanah and Abdul Rahman , Mohd Basyaruddin and Basri, Mahiran and Othman, Siti Salhah and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar (2010) Silylation of mica for lipase immobilization as biocatalysts in esterification. Applied Clay Science, 47 . pp. 276-282. ISSN 0169-1317

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Abstract

Mica 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-CRLNGlu-Amino-CRLNOctyl-CRLNVinyl-CRLNGlycidoxy CRLNMercapto-CRLNMica-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.

Item Type:Article
Keyword:Mica; Silanization; Immobilization; Candida rugosa lipase; Esterification
Subject:Mica
Subject:Lipase
Subject:Biotechnology - Use of - Enzymes
Faculty or Institute:Faculty of Biotechnology and Biomolecular Sciences
Publisher:Elsevier B.V.
DOI Number:10.1016/j.clay.2009.11.004
Altmetrics:http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1016/j.clay.2009.11.004
ID Code:16712
Deposited By: Nida Hidayati Ghazali
Deposited On:16 Jul 2012 03:51
Last Modified:31 Oct 2012 03:01

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