Silylation of mica for lipase immobilization as biocatalysts in esterification

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 are...

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Main Authors: Zaidan, Uswatun Hasanah, Abdul Rahman, Mohd Basyaruddin, Basri, Mahiran, Othman, Siti Salhah, Raja Abdul Rahman, Raja Noor Zaliha, Salleh, Abu Bakar
Format: Article
Language:English
Published: Elsevier 2010
Online Access:http://psasir.upm.edu.my/id/eprint/16712/
http://psasir.upm.edu.my/id/eprint/16712/1/Silylation%20of%20mica%20for%20lipase%20immobilization%20as%20biocatalysts%20in%20esterification.pdf
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author Zaidan, Uswatun Hasanah
Abdul Rahman, Mohd Basyaruddin
Basri, Mahiran
Othman, Siti Salhah
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
author_facet Zaidan, Uswatun Hasanah
Abdul Rahman, Mohd Basyaruddin
Basri, Mahiran
Othman, Siti Salhah
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
author_sort Zaidan, Uswatun Hasanah
building UPM Institutional Repository
collection Online Access
description 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.
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spelling upm-167122016-09-02T04:50:06Z http://psasir.upm.edu.my/id/eprint/16712/ Silylation of mica for lipase immobilization as biocatalysts in esterification Zaidan, Uswatun Hasanah Abdul Rahman, Mohd Basyaruddin Basri, Mahiran Othman, Siti Salhah Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar 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. Elsevier 2010 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/16712/1/Silylation%20of%20mica%20for%20lipase%20immobilization%20as%20biocatalysts%20in%20esterification.pdf 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 (3-4). pp. 276-282. ISSN 0169-1317; ESSN: 1872-9053 10.1016/j.clay.2009.11.004
spellingShingle Zaidan, Uswatun Hasanah
Abdul Rahman, Mohd Basyaruddin
Basri, Mahiran
Othman, Siti Salhah
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Silylation of mica for lipase immobilization as biocatalysts in esterification
title Silylation of mica for lipase immobilization as biocatalysts in esterification
title_full Silylation of mica for lipase immobilization as biocatalysts in esterification
title_fullStr Silylation of mica for lipase immobilization as biocatalysts in esterification
title_full_unstemmed Silylation of mica for lipase immobilization as biocatalysts in esterification
title_short Silylation of mica for lipase immobilization as biocatalysts in esterification
title_sort silylation of mica for lipase immobilization as biocatalysts in esterification
url http://psasir.upm.edu.my/id/eprint/16712/
http://psasir.upm.edu.my/id/eprint/16712/
http://psasir.upm.edu.my/id/eprint/16712/1/Silylation%20of%20mica%20for%20lipase%20immobilization%20as%20biocatalysts%20in%20esterification.pdf