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Reductive alkylation of lipase: experimental and molecular modeling approaches


Raja Abdul Rahman, Raja Noor Zaliha and Tejo, Bimo Ario and Basri, Mahiran and Abdul Rahman, Mohd Basyaruddin and Khan, Farid and Md Zain, Sharifuddin and Siahaan, Teruna J. and Salleh, Abu Bakar (2004) Reductive alkylation of lipase: experimental and molecular modeling approaches. Applied Biochemistry and Biotechnology, 118 (1-3). pp. 11-20. ISSN 0273-2289; ESSN: 1559-0291


Candida rugosa lipase was modified via reductive alkylation to increase its hydrophobicity to work better in organic solvents. The free amino group of lysines was alkylated using propionaldehyde with different degrees of modification obtained (49 and 86%). Far-ultraviolet circular dichroism (CD) spectroscopy of the lipase in aqueous solvent showed that such chemical modifications at the enzyme surface caused a loss in secondary and tertiary structure that is attributed to the enzyme unfolding. Using molecular modeling, we propose that in an aqueous environment the loss in protein structure of the modified lipase is owing to disruption of stabilizing salt bridges, particularly of surface lysines. Indeed, molecular modeling and simulation of a salt bridge formed by Lys-75 to Asp-79, in a nonpolar environment, suggests the adoption of a more flexible alkylated lysine that may explain higher lipase activity in organic solvents on alkylation.

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Additional Metadata

Item Type: Article
Divisions: Faculty of Science and Environmental Studies
Institute of Bioscience
DOI Number: https://doi.org/10.1385/ABAB:118:1-3:011
Publisher: Humana Press
Keywords: Candida rugosa; Circular dichroism; Enzyme modification; Lipase; Molecular modeling
Depositing User: Nabilah Mustapa
Date Deposited: 04 Jul 2017 03:03
Last Modified: 04 Jul 2017 03:03
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1385/ABAB:118:1-3:011
URI: http://psasir.upm.edu.my/id/eprint/56252
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