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Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Partial purification and some properties of a phospholipase C from Pseudomonas sp. strain KS3.2
Daisuke Sugimori1, Masatoshi Nakamura
1Department of Chemistry and Biology Engineering, Fukui National College of Technology, Japan. sugimori@sss.fukushima-u.ac.jp
Bioscience, Biotechnology, and Biochemistry
|February 24, 2006
Abstract:
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.

