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Application of natural kaolin as support for the immobilization of lipase from Candida rugosa as biocatalsyt for effective esterification


Citation

Abdul Rahman, Mohd Basyaruddin and Md Tajudin, Safarini and Hussein, Mohd Zobir and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar and Basri, Mahiran (2005) Application of natural kaolin as support for the immobilization of lipase from Candida rugosa as biocatalsyt for effective esterification. Applied Clay Science, 29 (2). pp. 111-116. ISSN 0169-1317; ESSN: 1872-9053

Abstract / Synopsis

Lipase from Candida rugosa was immobilized onto natural kaolin by physical adsorption method. About 77% of protein content was immobilized onto the support. The activities of the immobilized lipase were determined by the esterification activities using oleic acid and 1-butanol as substrates and hexane as reaction medium. The effects of reaction temperature, thermostability, stability in organic solvent, leaching and storage studies of immobilized lipase were investigated. Kaolin-immobilized lipase exhibited activities higher by fourfolds than the native lipase after thermal stability test at 70 °C. Immobilized lipase was found to be stable in hexane at room temperature up to 12 days and also showed higher stability than native lipase in the storage study. Leaching studies showed that the immobilized lipase remained full activity even after being washed by 20 ml of solvent. The experimental results showed that physical adsorption is suitable for the attachment of enzyme onto kaolin.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science and Environmental Studies
DOI Number: https://doi.org/10.1016/j.clay.2004.12.001
Publisher: Elsevier
Keywords: Clay; Kaolin; Immobilized enzyme; Lipase; Esterification
Depositing User: Nabilah Mustapa
Date Deposited: 17 Sep 2015 14:02
Last Modified: 26 Sep 2016 16:13
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1016/j.clay.2004.12.001
URI: http://psasir.upm.edu.my/id/eprint/40335
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