Thermostable L2 lipase: enzyme properties and rational design
Thennostable lipase L2 was originally produced extracellularly by thermophilic Bacillus sp. L2, isolated from a hot spring in Perak, Malaysia. The recombinant L2 lipase has been expressed in Escherichia coli system and later purified by using affinity chromatography. The optimum pH and temperature w...
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| Format: | Conference or Workshop Item |
| Language: | English |
| Published: |
2012
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| Online Access: | http://psasir.upm.edu.my/id/eprint/25909/1/ID%2025909.pdf |
| _version_ | 1796970841941999616 |
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| author | Raja Abdul Rahman, Raja Noor Zaliha |
| author_facet | Raja Abdul Rahman, Raja Noor Zaliha |
| author_sort | Raja Abdul Rahman, Raja Noor Zaliha |
| collection | UPM |
| description | Thennostable lipase L2 was originally produced extracellularly by thermophilic Bacillus sp. L2, isolated from a hot spring in Perak, Malaysia. The recombinant L2 lipase has been expressed in Escherichia coli system and later purified by using affinity chromatography. The optimum pH and temperature were 9.0 and 70°C, respectively. The structure of L2 lipase was successfully elucidated. To understand the function of amino acid residue at lipase N-terminal end, rational design was conducted by substitution of the second amino acid in L2 lipase. Result showed that the N-terminal residues of L2 lipase actually play a very important role of maintaining the integrity of the protein. |
| first_indexed | 2024-03-06T08:04:05Z |
| format | Conference or Workshop Item |
| id | upm.eprints-25909 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T08:04:05Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | upm.eprints-259092016-09-27T01:25:22Z http://psasir.upm.edu.my/id/eprint/25909/ Thermostable L2 lipase: enzyme properties and rational design Raja Abdul Rahman, Raja Noor Zaliha Thennostable lipase L2 was originally produced extracellularly by thermophilic Bacillus sp. L2, isolated from a hot spring in Perak, Malaysia. The recombinant L2 lipase has been expressed in Escherichia coli system and later purified by using affinity chromatography. The optimum pH and temperature were 9.0 and 70°C, respectively. The structure of L2 lipase was successfully elucidated. To understand the function of amino acid residue at lipase N-terminal end, rational design was conducted by substitution of the second amino acid in L2 lipase. Result showed that the N-terminal residues of L2 lipase actually play a very important role of maintaining the integrity of the protein. 2012 Conference or Workshop Item NonPeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/25909/1/ID%2025909.pdf Raja Abdul Rahman, Raja Noor Zaliha (2012) Thermostable L2 lipase: enzyme properties and rational design. In: 7th International Symposium of the Protein Society of Thailand, 29-31 Aug. 2012 . |
| spellingShingle | Raja Abdul Rahman, Raja Noor Zaliha Thermostable L2 lipase: enzyme properties and rational design |
| title | Thermostable L2 lipase: enzyme properties and rational design |
| title_full | Thermostable L2 lipase: enzyme properties and rational design |
| title_fullStr | Thermostable L2 lipase: enzyme properties and rational design |
| title_full_unstemmed | Thermostable L2 lipase: enzyme properties and rational design |
| title_short | Thermostable L2 lipase: enzyme properties and rational design |
| title_sort | thermostable l2 lipase enzyme properties and rational design |
| url | http://psasir.upm.edu.my/id/eprint/25909/1/ID%2025909.pdf |
| work_keys_str_mv | AT rajaabdulrahmanrajanoorzaliha thermostablel2lipaseenzymepropertiesandrationaldesign |