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Amidination of lipase with hydrophobic imidoesters


Citation

Basri, M. and Ampon, K. and Yunus, W. M. Z. and Razak, C. N. A. and Salleh, A. B. (1992) Amidination of lipase with hydrophobic imidoesters. Journal of the American Oil Chemists' Society, 69 (6). pp. 579-583. ISSN 0003-021X; eISSN: 1558-9331

Abstract

Lipase from Candida rugosa was chemically modified by amidination with imidoester hydrochlorides of different hydrophobicity. The modified enzyme showed a higher ester synthesis activity but a lower ester hydrolysis activity compared with the native enzyme. The maximum specific activity of the modified enzyme depended on its degree of derivatization. Benzene was found to be the best solvent for the synthesis reaction. The optimal temperature for the reaction was not affected by modification of the lipase. The modified lipase was more thermostable and solvent-stable than the native enzyme. When fatty acids of different carbon chainlength were tested as substrates in the synthesis of esters with the modified lipase, the highest activity was observed with myristic acid and propanol.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science and Environmental Studies
Universiti Pertanian Malaysia
DOI Number: https://doi.org/10.1007/bf02636112
Publisher: Wiley
Keywords: Amidination; Ester hydrolysis; Ester synthesis; Lipase
Depositing User: Ms. Zaimah Saiful Yazan
Date Deposited: 10 Jan 2025 07:46
Last Modified: 10 Jan 2025 07:46
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1007/bf02636112
URI: http://psasir.upm.edu.my/id/eprint/113042
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