4.4 Article

Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete

Journal

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 73, Issue 9, Pages 2136-2137

Publisher

TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90323

Keywords

marine; phosphatidylcholine; phospholipase C; sodium ion; Streptomyces

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A novel extracellular phospholipase C (PLC) was purified from a marine streptomycete. It had a molecular mass of 28 kDa as estimated by SDS-polyacrylamide gel electrophoresis. Its enzyme activity was optimal at pH 8.0 at 45 degrees C. The PLC hydrolyzed only phosphatidylcholine. Its activity was enhanced 300% by Na+ (200 mm), suggesting that the purified PLC is a typical marine-type enzyme.

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