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...
| Main Authors: | , , , , |
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| Format: | Article |
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Wiley
1992
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| Online Access: | http://psasir.upm.edu.my/id/eprint/113042/ |
| _version_ | 1848866109463199744 |
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| author | Basri, M. Ampon, K. Yunus, W. M. Z. Razak, C. N. A. Salleh, A. B. |
| author_facet | Basri, M. Ampon, K. Yunus, W. M. Z. Razak, C. N. A. Salleh, A. B. |
| author_sort | Basri, M. |
| building | UPM Institutional Repository |
| collection | Online Access |
| 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. |
| first_indexed | 2025-11-15T14:15:23Z |
| format | Article |
| id | upm-113042 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:15:23Z |
| publishDate | 1992 |
| publisher | Wiley |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-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 |
| spellingShingle | Basri, M. Ampon, K. Yunus, W. M. Z. Razak, C. N. A. Salleh, A. B. Amidination of lipase with hydrophobic imidoesters |
| title | 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_short | Amidination of lipase with hydrophobic imidoesters |
| title_sort | amidination of lipase with hydrophobic imidoesters |
| url | http://psasir.upm.edu.my/id/eprint/113042/ http://psasir.upm.edu.my/id/eprint/113042/ http://psasir.upm.edu.my/id/eprint/113042/ |