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.
Sugimori
Daisuke
D
Department of Chemistry and Biology Engineering, Fukui National College of Technology, Japan. sugimori@sss.fukushima-u.ac.jp
Nakamura
Masatoshi
M
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