Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri
Phospholipase A₂ is a lipolytic enzyme that specifically hydrolyze sn-2 fatty acyl ester bond of phospholipids to yield free fatty acids and lysophospholipids. It was widely use in the several industry including pharmaceutical, food and biotechnology. Therefore, this study was done to purify the pho...
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2009
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my-uitm-ir.1054142024-12-04T14:27:42Z Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri 2009 Mohamed Sukri, Noor Akma Pharmaceutical industry Pharmaceutical chemistry Phospholipase A₂ is a lipolytic enzyme that specifically hydrolyze sn-2 fatty acyl ester bond of phospholipids to yield free fatty acids and lysophospholipids. It was widely use in the several industry including pharmaceutical, food and biotechnology. Therefore, this study was done to purify the phospholipas A₂ enzyme by using hybrid protocol. This method consist of two combination method which is denaturing and native protocol and has ability to purified and retained biological activity of the desired protein. There were two clones involved in the study which is pBADTOPO pla, clone 5 and pBADTOPO pla, clone 8. They were purified at the 37 °C. Result indicated, only small amount of bioactive protein were recovered. Poor recovery of bioactive protein from inclusion bodies may result from the loss of secondary structure during solubilization procedure and interaction among the denatured protein molecules during refolding. 2009 Thesis https://ir.uitm.edu.my/id/eprint/105414/ https://ir.uitm.edu.my/id/eprint/105414/1/105414.PDF text en public degree Universiti Teknologi MARA (Kampus Puncak Alam) Faculty of Pharmacy Ramasamy, Kalavathy |
| institution |
Universiti Teknologi MARA |
| collection |
UiTM Institutional Repository |
| language |
English |
| advisor |
Ramasamy, Kalavathy |
| topic |
Pharmaceutical industry Pharmaceutical chemistry |
| spellingShingle |
Pharmaceutical industry Pharmaceutical chemistry Mohamed Sukri, Noor Akma Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri |
| description |
Phospholipase A₂ is a lipolytic enzyme that specifically hydrolyze sn-2 fatty acyl ester bond of phospholipids to yield free fatty acids and lysophospholipids. It was widely use in the several industry including pharmaceutical, food and biotechnology. Therefore, this study was done to purify the phospholipas A₂ enzyme by using hybrid protocol. This method consist of two combination method which is denaturing and native protocol and has ability to purified and retained biological activity of the desired protein. There were two clones involved in the study which is pBADTOPO pla, clone 5 and pBADTOPO pla, clone 8. They were purified at the 37 °C. Result indicated, only small amount of bioactive protein were recovered. Poor recovery of bioactive protein from inclusion bodies may result from the loss of secondary structure during solubilization procedure and interaction among the denatured protein molecules during refolding. |
| format |
Thesis |
| qualification_level |
Bachelor degree |
| author |
Mohamed Sukri, Noor Akma |
| author_facet |
Mohamed Sukri, Noor Akma |
| author_sort |
Mohamed Sukri, Noor Akma |
| title |
Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri |
| title_short |
Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri |
| title_full |
Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri |
| title_fullStr |
Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri |
| title_full_unstemmed |
Purification of recombinant phospholipase A₂ enzyme in escherichia coli / Noor Akma Mohamed Sukri |
| title_sort |
purification of recombinant phospholipase a₂ enzyme in escherichia coli / noor akma mohamed sukri |
| granting_institution |
Universiti Teknologi MARA (Kampus Puncak Alam) |
| granting_department |
Faculty of Pharmacy |
| publishDate |
2009 |
| url |
https://ir.uitm.edu.my/id/eprint/105414/1/105414.PDF |
| _version_ |
1818588148826898432 |