Production of squalene by squalene synthases and their truncated mutants in Escherichia coli.
Squalene is a precursor of thousands of bioactive triterpenoids and also has industrial value as a lubricant, health-promoting agent, and/or drop-in biofuel. To establish an efficient Escherichia coli-based system for squalene production, we tested two different squalene synthases and their mutants in combination with precursor pathways. By co-expressing a chimeric mevalonate pathway with human or Thermosynechococcus squalene synthase, E. coli accumulated squalene up to 230 mg/L or 55 mg/g-DCW in flask culture. We also determined that a significant truncation of squalene synthase at the C-terminus retains partial cellular activity. The squalene-producing strain described herein represents a convenient platform for gene discovery and the construction of the pathway toward natural and non-natural hopanoids/steroids.
['Katabami|Akinori|A|', 'Li|Ling|L|', 'Iwasaki|Miki|M|', 'Furubayashi|Maiko|M|', 'Saito|Kyoichi|K|', 'Umeno|Daisuke|D|']
D002851:Chromatography, High Pressure Liquid D000458:Cyanobacteria D004926:Escherichia coli D013186:Farnesyl-Diphosphate Farnesyltransferase D006801:Humans D008798:Mevalonic Acid D050505:Mutant Proteins D009154:Mutation D013185:Squalene D013696:Temperature
Squalene synthase Triterpenoid Mevalonate pathway Bacterial production Carotenoid