AI Article Synopsis
- Researchers used different ABC protein exporters from various bacteria to enhance the secretion of lipase (TliA) in E. coli.
- The study tested the effects of different gene clusters and various growth temperatures (20 to 35 °C) on TliA secretion levels.
- The results showed that E. coli with S. marcescens lipBCD genes at 25 °C achieved the highest secretion of lipase, indicating that both the choice of exporter and temperature are critical for optimizing extracellular production.
Article Abstract
Heterologous ABC protein exporters, the apparatus of type I secretion pathway in Gram-negative bacteria, were used for extracellular production of Pseudomonas fluorescens lipase (TliA) in recombinant Escherichia coli. The effect of the expression of different ABC protein exporter gene clusters (P. fluorescens tliDEF, Pseudomonas aeruginosa aprDEF, Erwinia chrysanthemi prtDEF, and Serratia marcescens lipBCD genes) was examined on the secretion of TliA at growth temperatures of 20, 25, 30 and 35 °C. TliA secretion in recombinant E. coli XL10-Gold varied depending upon type of ABC protein exporter and culture temperature. E. coli expressing S. marcescens lipBCD genes showed the highest secretion level of TliA (122.8 U ml(-1)) when cultured at 25 °C. Thus, optimized culture conditions for efficient extracellular production of lipase in recombinant E. coli can be designed by changing the type of ABC protein exporter and the growth temperature.
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| http://dx.doi.org/10.1007/s10529-014-1567-5 | DOI Listing |
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