Partial Purification and Some Properties of a Phospholipase C from Pseudomonas sp. Strain KS3.2
An extracellular phospholipase C was partially purified from <I>Pseudomonas</I> sp. strain KS3.2. The enzyme was composed of an approximately 18-kDa peptide. Maximal enzyme activity was found at pH 7.2 and 50 °C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 °C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activity toward other phospholipids.
- Bioscience, biotechnology, and biochemistry
Bioscience, biotechnology, and biochemistry 70(2), 535-537, 2006-02-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry