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Stability of hydrophobic lipase derivatives immobilized on organic polymer beads

Lipase from Candida rugosa was immobilized by attaching various hydrophobic groups to the enzyme molecule and adsorbing these hydrophobic lipase derivatives on several organic polymer beads. The immobilized enzymes were more thermostable in organic solvents compared to the native and modified Upases...

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Main Authors: Basri, M., Ampon, K., Wan Yunus, W.M.Z., A. Razak, C.N.
Format: Article
Language:English
Published: Humana Press 1994
Online Access:http://psasir.upm.edu.my/id/eprint/114810/1/114810.pdf
http://psasir.upm.edu.my/id/eprint/114810/
https://link.springer.com/article/10.1007/BF02788740?error=cookies_not_supported&code=0f51ffbe-4fd5-4b76-8185-9c1b123c2738
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spelling my.upm.eprints.1148102025-02-03T04:17:09Z http://psasir.upm.edu.my/id/eprint/114810/ Stability of hydrophobic lipase derivatives immobilized on organic polymer beads Basri, M. Ampon, K. Wan Yunus, W.M.Z. A. Razak, C.N. Lipase from Candida rugosa was immobilized by attaching various hydrophobic groups to the enzyme molecule and adsorbing these hydrophobic lipase derivatives on several organic polymer beads. The immobilized enzymes were more thermostable in organic solvents compared to the native and modified Upases. Thermostability was highest with ΧAD2 beads, followed by ΧAD7 and RCOOH. Initially modifying the enzyme with hydrophobic modifiers did not have any effect on the enzyme thermostability. The best conditions for storing these enzyme preparations were at very low temperature in the lyophilized form and in a solution containing the reaction substrate. Interestingly, PEG-lipase immobilized on ΧAD7 beads showed increased operational stability when used in a stirred-tank reactor. The operational stability was further increased by a mild glutaraldehyde treatment of the enzyme preparation. © 1994 Humana Press Inc. Humana Press 1994 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/114810/1/114810.pdf Basri, M. and Ampon, K. and Wan Yunus, W.M.Z. and A. Razak, C.N. (1994) Stability of hydrophobic lipase derivatives immobilized on organic polymer beads. Applied Biochemistry and Biotechnology, 48 (3). pp. 173-183. ISSN 1559-0291; eISSN: 0273-2289 https://link.springer.com/article/10.1007/BF02788740?error=cookies_not_supported&code=0f51ffbe-4fd5-4b76-8185-9c1b123c2738 10.1007/BF02788740
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/
language English
description Lipase from Candida rugosa was immobilized by attaching various hydrophobic groups to the enzyme molecule and adsorbing these hydrophobic lipase derivatives on several organic polymer beads. The immobilized enzymes were more thermostable in organic solvents compared to the native and modified Upases. Thermostability was highest with ΧAD2 beads, followed by ΧAD7 and RCOOH. Initially modifying the enzyme with hydrophobic modifiers did not have any effect on the enzyme thermostability. The best conditions for storing these enzyme preparations were at very low temperature in the lyophilized form and in a solution containing the reaction substrate. Interestingly, PEG-lipase immobilized on ΧAD7 beads showed increased operational stability when used in a stirred-tank reactor. The operational stability was further increased by a mild glutaraldehyde treatment of the enzyme preparation. © 1994 Humana Press Inc.
format Article
author Basri, M.
Ampon, K.
Wan Yunus, W.M.Z.
A. Razak, C.N.
spellingShingle Basri, M.
Ampon, K.
Wan Yunus, W.M.Z.
A. Razak, C.N.
Stability of hydrophobic lipase derivatives immobilized on organic polymer beads
author_facet Basri, M.
Ampon, K.
Wan Yunus, W.M.Z.
A. Razak, C.N.
author_sort Basri, M.
title Stability of hydrophobic lipase derivatives immobilized on organic polymer beads
title_short Stability of hydrophobic lipase derivatives immobilized on organic polymer beads
title_full Stability of hydrophobic lipase derivatives immobilized on organic polymer beads
title_fullStr Stability of hydrophobic lipase derivatives immobilized on organic polymer beads
title_full_unstemmed Stability of hydrophobic lipase derivatives immobilized on organic polymer beads
title_sort stability of hydrophobic lipase derivatives immobilized on organic polymer beads
publisher Humana Press
publishDate 1994
url http://psasir.upm.edu.my/id/eprint/114810/1/114810.pdf
http://psasir.upm.edu.my/id/eprint/114810/
https://link.springer.com/article/10.1007/BF02788740?error=cookies_not_supported&code=0f51ffbe-4fd5-4b76-8185-9c1b123c2738
_version_ 1823093281941094400
score 13.239859

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