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| Content Provider | PubMed Central |
|---|---|
| Author | Lan, Dong-ming Yang, Ning Wang, Wen-kai Shen, Yan-fei Yang, Bo Wang, Yong-hua |
| Copyright Year | 2011 |
| Abstract | A novel lipase gene lip5 from the yeast Candida albicans was cloned and sequenced. Alignment of amino acid sequences revealed that 86–34% identity exists with lipases from other Candida species. The lipase and its mutants were expressed in the yeast Pichia pastoris, where alternative codon usage caused the mistranslation of 154-Ser and 293-Ser as leucine. 154-Ser to leucine resulted in loss of expression of Lip5, and 293-Ser to leucine caused a marked reduction in the lipase activity. Lip5-DM, which has double mutations that revert 154 and 293 to serine residues, showed good lipase activity, and was overexpressed and purified by (NH4)2SO4 precipitation and ion-exchange chromatography. The pure Lip5-DM was stable at low temperatures ranging from 15–35 °C and pH 5–9, with the optimal conditions being 15–25 °C and pH 5–6. The activation energy of recombinant lipase was 8.5 Kcal/mol between 5 and 25 °C, suggesting that Lip5-DM was a cold–active lipase. Its activity was found to increase in the presence of Zn2+, but it was strongly inhibited by Fe2+, Fe3+, Hg2+ and some surfactants. In addition, the Lip5-DM could not tolerate water-miscible organic solvents. Lip5-DM exhibited a preference for the short-and medium-chain length p-nitrophenyl (C4 and C8 acyl group) esters rather than the long chain length p-nitrophenyl esters (C12, C16 and C18 acyl group) with highest activity observed with the C8 derivatives. The recombinant enzyme displayed activity toward triacylglycerols, such as olive oil and safflower oil. |
| Related Links | http://dx.doi.org/10.3390/ijms12063950 |
| Ending Page | 3965 |
| Page Count | 16 |
| Starting Page | 3950 |
| File Format | |
| ISSN | 14220067 |
| e-ISSN | 14220067 |
| Journal | International Journal of Molecular Sciences |
| Issue Number | 6 |
| Volume Number | 12 |
| Language | English |
| Publisher | Molecular Diversity Preservation International (MDPI) |
| Publisher Date | 2011-06-01 |
| Access Restriction | Open |
| Rights Holder | Molecular Diversity Preservation International (MDPI) |
| Subject Keyword | Physical and Theoretical Chemistry Inorganic Chemistry Organic Chemistry Spectroscopy Molecular Biology Catalysis Computer Science Applications Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Organic Chemistry Medicine Molecular Biology Physical and Theoretical Chemistry Catalysis Inorganic Chemistry Computer Science Applications |
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