Immobilization of hydrophobic lipase derivatives on to organic polymer beads
A simple and effective method of lipase immobilization is described. Lipase from Candida rugosa was first modified with several hydrophobic modifiers before being adsorbed on to organic polymer beads. The soluble hydrophobic lipase derivatives adsorbed more strongly on to the various polymers as com...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Society of Chemical Industry
1994
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| Online Access: | http://psasir.upm.edu.my/id/eprint/22571/ http://psasir.upm.edu.my/id/eprint/22571/1/Immobilization%20of%20hydrophobic%20lipase%20derivatives%20on%20to%20organic%20polymer%20beads.pdf |
| _version_ | 1848844520878243840 |
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| author | Basri, Mahiran Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Abdul Razak, Che Nyonya Salleh, Abu Bakar |
| author_facet | Basri, Mahiran Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Abdul Razak, Che Nyonya Salleh, Abu Bakar |
| author_sort | Basri, Mahiran |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | A simple and effective method of lipase immobilization is described. Lipase from Candida rugosa was first modified with several hydrophobic modifiers before being adsorbed on to organic polymer beads. The soluble hydrophobic lipase derivatives adsorbed more strongly on to the various polymers as compared with the native lipase. The optimal adsorption temperature of the native and modified lipases on all the polymers was 40°C. The optimal pH of adsorption was between 6 and 7. Lipase immobilized in this manner produced high catalytic recoveries which were affected by the type of modifiers, degree of modification and type of supports used. Monomethoxypolyethylene glycol (1900) activated with p-nitrophenyl chloroformate was found to be the best modifier of the enzyme at 95% modification, for adsorption to the polymers. Increasing the degree of modification of the enzyme increased the activity which was immobilized. Generally, both native and hydrophobic lipase derivatives showed higher specific activities when immobilized on polar polymers compared with non-polar polymers. |
| first_indexed | 2025-11-15T08:32:14Z |
| format | Article |
| id | upm-22571 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T08:32:14Z |
| publishDate | 1994 |
| publisher | Society of Chemical Industry |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-225712016-02-02T04:04:31Z http://psasir.upm.edu.my/id/eprint/22571/ Immobilization of hydrophobic lipase derivatives on to organic polymer beads Basri, Mahiran Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Abdul Razak, Che Nyonya Salleh, Abu Bakar A simple and effective method of lipase immobilization is described. Lipase from Candida rugosa was first modified with several hydrophobic modifiers before being adsorbed on to organic polymer beads. The soluble hydrophobic lipase derivatives adsorbed more strongly on to the various polymers as compared with the native lipase. The optimal adsorption temperature of the native and modified lipases on all the polymers was 40°C. The optimal pH of adsorption was between 6 and 7. Lipase immobilized in this manner produced high catalytic recoveries which were affected by the type of modifiers, degree of modification and type of supports used. Monomethoxypolyethylene glycol (1900) activated with p-nitrophenyl chloroformate was found to be the best modifier of the enzyme at 95% modification, for adsorption to the polymers. Increasing the degree of modification of the enzyme increased the activity which was immobilized. Generally, both native and hydrophobic lipase derivatives showed higher specific activities when immobilized on polar polymers compared with non-polar polymers. Society of Chemical Industry 1994-01 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22571/1/Immobilization%20of%20hydrophobic%20lipase%20derivatives%20on%20to%20organic%20polymer%20beads.pdf Basri, Mahiran and Ampon, Kamaruzaman and Wan Yunus, Wan Md. Zin and Abdul Razak, Che Nyonya and Salleh, Abu Bakar (1994) Immobilization of hydrophobic lipase derivatives on to organic polymer beads. Journal of Chemical Technology and Biotechnology, 59 (1). pp. 37-44. ISSN 0268-2575; ESSN: 1097-4660 http://onlinelibrary.wiley.com/doi/10.1002/jctb.280590107/abstract 10.1002/jctb.280590107 |
| spellingShingle | Basri, Mahiran Ampon, Kamaruzaman Wan Yunus, Wan Md. Zin Abdul Razak, Che Nyonya Salleh, Abu Bakar Immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| title | Immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| title_full | Immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| title_fullStr | Immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| title_full_unstemmed | Immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| title_short | Immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| title_sort | immobilization of hydrophobic lipase derivatives on to organic polymer beads |
| url | http://psasir.upm.edu.my/id/eprint/22571/ http://psasir.upm.edu.my/id/eprint/22571/ http://psasir.upm.edu.my/id/eprint/22571/ http://psasir.upm.edu.my/id/eprint/22571/1/Immobilization%20of%20hydrophobic%20lipase%20derivatives%20on%20to%20organic%20polymer%20beads.pdf |