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

SangJoon MO; Jae-heon KIM; Ki Woong CHO

doi:10.1271/bbb.90323

Biochemistry & Molecular Biology Notes

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

SangJoon MO, Jae-heon KIM, Ki Woong CHO

著者情報

キーワード: marine, phosphatidylcholine, phospholipase C, sodium ion, Streptomyces

ジャーナルフリー

2009 年 73 巻 9 号 p. 2136-2137

DOI https://doi.org/10.1271/bbb.90323

View "Advance Publication" version (September 7, 2009).

詳細

抄録

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 °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.

責任著者(Corresponding author)

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