Abstract
We have cloned a novel lipase gene, lip2, from Aspergillus niger and expressed it in Escherichia coli. Upon purification of the recombinant Lip2 protein, its properties were characterized. In comparison with a previously identified lipase Lip1, both enzymes are acid lipases (optimal pH <6.5), Ca2+-dependent and PMSF-sensitive, but have different molecular weights (35 and 43 kDa), optimal substrate spectra (C10 and C8), optimal reaction temperatures (45 and 50°C) and thermal stability. Circular dichroism spectroscopy revealed that Lip2 contains a typical Ca2+-active site. This first report on the cloning of the Lip2 gene and its enzymatic characteristics may greatly facilitate its potential industrial application.
Original language | English |
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Pages (from-to) | 951-956 |
Number of pages | 6 |
Journal | Biotechnology Letters |
Volume | 32 |
Issue number | 7 |
Early online date | 8 Mar 2010 |
DOIs | |
Publication status | Published - Jul 2010 |
User-Defined Keywords
- Aspergillus niger
- Lip1 Lip2 genes
- Lipase