Partial Purification and Some Properties of a Phospholipase C from Pseudomonas sp. Strain KS3.2

• SUGIMORI Daisuke

  Department of Chemistry and Biology Engineering, Fukui National College of Technology

• NAKAMURA Masatoshi

  Department of Chemistry and Biology Engineering, Fukui National College of Technology

Bibliographic Information

Other Title

• Partial Purification and Some Properties of a Phospholipase C from<i>Pseudomonas</i>sp. Strain KS3.2

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 °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.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 70 (2), 535-537, 2006

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• phospholipase C
• metalloenzyme
• serine hydrolase
• <I>Pseudomonas</I> sp.

Details

• CRID: 1390001206475786112
• NII Article ID: 10018534703
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.70.535
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 7833729
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I7833729
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.70.535
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed