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Enzymatic synthesis of methyl adipate ester using lipase from Candida rugosa immobilised on Mg, Zn and Ni of layered double hydroxides (LDHs)


Citation

Abdul Rahman, Mohd Basyaruddin and Zaidan, Uswatun Hasanah and Basri, Mahiran and Hussein, Mohd Zobir and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar (2008) Enzymatic synthesis of methyl adipate ester using lipase from Candida rugosa immobilised on Mg, Zn and Ni of layered double hydroxides (LDHs). Journal of Molecular Catalysis B: Enzymatic, 50 (1). pp. 33-39. ISSN 1381-1177; ESSN: 1873-3158

Abstract / Synopsis

The enzymatic synthesis of methyl adipate via green esterification of adipic acid and methanol in hexane has been studied. Lipase from Candida rugosa immobilised onto various layered double hydroxides (LDHs) by a reproducible and simple method of physical adsorption was used as biocatalyst with promising result. Mg/Al–NO3−, Zn/Al–NO3 − and Ni/Al–NO3− of LDHs with molar ratio of M2+/M3+ = 4:1 were synthesised by co-precipitation method with continuous agitation. The percentages of protein loading on Mg/Al–NO3 −, Zn/Al–NO − and Ni/Al–NO3 − were 71%, 67% and 58%, respectively, due to the larger surface area, porosity and basal spacing of the supports. Parameter studies of reaction time,reaction temperature, water activity, thermostability, storage, leaching and reusability were investigated and optimised. Optimum conditions to produce adipate ester upto 80 % were reaction time; 2.5 h, temperature; 50 ◦C, and water activity; 0.53, respectively. Increased in optimisation conditions and enhanced stability properties were found after immobilisation compared to the native lipase.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Faculty of Science
DOI Number: 10.1016/j.molcatb.2007.09.020
Publisher: Elsevier
Keywords: Adipate; Lipase; Immobilisation; Layered double hydroxides; Biocatalyst
Depositing User: Najwani Amir Sariffudin
Date Deposited: 04 May 2010 16:05
Last Modified: 28 Sep 2016 09:44
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1016/j.molcatb.2007.09.020
URI: http://psasir.upm.edu.my/id/eprint/5822
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