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Purification and characterization of an extracellular lipase from Clostridium tetanomorphum

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The strictly anaerobic bacterium Clostridium tetanomorphum formed an extracellular lipase when the growth medium contained glycerol in addition to fermentable substrates such as l-glutamate or glucose. The lipase was purified from the concentrated culture supernatant and exhibited a final specific activity of 900 U/mg. The purified lipase had a Stokes’ radius of 5.0 nm and a sedimentation coefficient of 5.7S. The native molecular mass calculated from these values was 118,000 Da, which is considerably higher than the molecular mass calculated by PAGE (70,000 Da). With p-nitrophenyl esters of different fatty acids as substrates enzyme activity was highest when the acyl chain was short (C2). The purified lipase showed no protease or thioesterase activity.

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We thank Prof. G. Gottschalk for generous support.

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Correspondence to Rolf Daniel.

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Petersen, M., Daniel, R. Purification and characterization of an extracellular lipase from Clostridium tetanomorphum . World J Microbiol Biotechnol 22, 431–435 (2006).

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  • Clostridium tetanomorphum
  • enzyme purification
  • extracellular enzymes
  • lipase
  • triolein