Partial purification and some properties of a phospholipase C from Pseudomonas sp. strain KS3.2.
An extracellular phospholipase C was partially purified from Pseudomonas 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 degrees C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 degrees C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activity toward other phospholipids.
Department of Chemistry and Biology Engineering, Fukui National College of Technology, Japan. sugimori@sss.fukushima-u.ac.jp
Daisuke
D
Sugimori
Masatoshi
M
Nakamura
D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D011549:Pseudomonas / Q000145:classification* / Q000201:enzymology*; D013696:Temperature; D010738:Type C Phospholipases / Q000302:isolation & purification* / Q000378:metabolism*
D010738:Type C Phospholipases