[Production of lecithinase by Bacillus thuringiensis].

The activity of lecithaniase was determined in 24 strains of Bacillus thuringiensis on four growth media. The highest accumulation of lecithinase was found on the Hottinger medium containing 0.5% of glucose and 0.56% of sodium bicarbonate. Lecithinase appears at the logarithmic growth phase, and its activity is maximal after 10 hours of growth (at the beginning of the stationary phase). Biosynthesis and accumulation of lecithinase occur at pH 6.0 to 9.0. Lecithinase was purified by salting out with ammonium sulphate (75% saturation). Lecithinase is a thermolabile protein; it is stable within pH range of 3.0 to 9.0 and is resistant to the action of trypsin and 8M urea.