A mutant of Magnetospirillum gryphiswaldense, NPHB, was obtained from a conjugation experiment. An aberrant recombination occurred between a putative elongation factor-G gene (fus-like) of the bacterial chromosome and the chloramphenicol resistant gene (cat) of a suicide vector, pSUP202. Complementary experiments and transcription analysis of genes around the recombinant site showed that the cat promoter enhanced the expression of adenosine triphosphatase gene downstream. Adenosine triphosphate hydrolyzing activity in NPHB was 35% higher than in the wild-type strain (M. gryphiswaldense MSR-1). NPHB accumulated 71% less poly-β-hydroxybutyrate and consumed 56% more oxygen and 40% more lactate than MSR-1. The magnetosome content of NPHB was 69% higher than MSR-1 in flask culture. NPHB cultured in a 7.5-L bioreactor gave a maximum yield of 58.4 ± 6.4 mg magnetosomes per liter.
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This work was supported by Chinese High Technology Research and Development Program (Grant no. 2006AA02Z233 and 2007AA021805) and Chinese National Science Foundation (Grant no. 30570023).
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Liu, J., Ding, Y., Jiang, W. et al. A mutation upstream of an ATPase gene significantly increases magnetosome production in Magnetospirillum gryphiswaldense . Appl Microbiol Biotechnol 81, 551–558 (2008). https://doi.org/10.1007/s00253-008-1665-1
- Magnetospirillum gryphiswaldense
- PHB production
- ATPase activity
- Magnetosome production
- Oxygen consumption