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Amidination of lipase with hydrophobic imidoesters

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 modif...

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Main Authors: Basri, M., Ampon, K., Yunus, W. M. Z., Razak, C. N. A., Salleh, A. B.
Format: Article
Published: Wiley 1992
Online Access:http://psasir.upm.edu.my/id/eprint/113042/
https://aocs.onlinelibrary.wiley.com/doi/10.1007/BF02636112
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spelling my.upm.eprints.1130422025-01-10T07:46:25Z http://psasir.upm.edu.my/id/eprint/113042/ Amidination of lipase with hydrophobic imidoesters Basri, M. Ampon, K. Yunus, W. M. Z. Razak, C. N. A. Salleh, A. B. 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. Wiley 1992 Article PeerReviewed 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 https://aocs.onlinelibrary.wiley.com/doi/10.1007/BF02636112 10.1007/bf02636112
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description 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.
format Article
author Basri, M.
Ampon, K.
Yunus, W. M. Z.
Razak, C. N. A.
Salleh, A. B.
spellingShingle Basri, M.
Ampon, K.
Yunus, W. M. Z.
Razak, C. N. A.
Salleh, A. B.
Amidination of lipase with hydrophobic imidoesters
author_facet Basri, M.
Ampon, K.
Yunus, W. M. Z.
Razak, C. N. A.
Salleh, A. B.
author_sort Basri, M.
title Amidination of lipase with hydrophobic imidoesters
title_short Amidination of lipase with hydrophobic imidoesters
title_full Amidination of lipase with hydrophobic imidoesters
title_fullStr Amidination of lipase with hydrophobic imidoesters
title_full_unstemmed Amidination of lipase with hydrophobic imidoesters
title_sort amidination of lipase with hydrophobic imidoesters
publisher Wiley
publishDate 1992
url http://psasir.upm.edu.my/id/eprint/113042/
https://aocs.onlinelibrary.wiley.com/doi/10.1007/BF02636112
_version_ 1821003742765383680
score 13.235796

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