Silylation of mica for lipase immobilization as biocatalysts in esterification

• Main Authors: Uswatun Hasanah, Zaidan, Mohd Basyaruddin, Abdul Rahman, Mahiran, Basri, Siti Salhah, Othman, Raja Noor Zaliha, Raja Abdul Rahman, Abu Bakar, Salleh
• Format: Article
• Language: English
• Published: Elsevier Science Bv 2015
• Subjects: Mica; Silanization; Immobilization; Candida rugosa lipase; Esterification
• Online Access: http://ddms.usim.edu.my/handle/123456789/8405

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-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. (C) 2009 Elsevier B.V. All rights reserved.