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A novel extracellular phospholipase C purified from a marine bacterium, Pseudoalteromonas sp. J937

Title
A novel extracellular phospholipase C purified from a marine bacterium, Pseudoalteromonas sp. J937
Authors
Mo S.Kim J.-H.Cho K.W.
Ewha Authors
모상준
Issue Date
2009
Journal Title
Biotechnology Letters
ISSN
0141-5492JCR Link
Citation
vol. 31, no. 1, pp. 89 - 94
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Marine bacterial isolates were screened for phospholipase C (PLC) activity on PCY agar plates containing phosphatidylcholine (PC) as substrate. The strain that showed the highest activity on a PCY screening agar plate and a thin-layer chromatography was identified as a strain of Pseudoalteromonas and subsequently designated Pseudoalteromonas sp. J937. The extracellular PLC of the strain J937 was purified to a specific activity of 33 U mg-1 protein by serial ion exchange and gel filtration column chromatography. It had a molecular mass of 32 kDa estimated by SDS-PAGE. The optimal pH and temperature of the enzyme were about pH 8 and 45°C, respectively. The PLC hydrolyzed phosphatidylethanolamine as well as PC but not other glycerophospholipids. Its activity was enhanced by 150% with Ca2+ (200 mM) and by 180% with Na+ (500 mM), suggesting that the purified PLC is a marine-type enzyme. © 2008 Springer Science+Business Media B.V.
DOI
10.1007/s10529-008-9833-z
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연구기관 > 나노·바이오기술연구소 > Journal papers
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