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

Content Provider	Springer Nature Link
Author	Mo, SangJoon Kim, Jae heon Cho, Ki Woong
Copyright Year	2008
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.
Starting Page	89
Ending Page	94
Page Count	6
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	31
Issue Number	1
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2008-09-11
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Glycerophospholipid Marine Phospholipase C Pseudoalteromonas Biochemistry Applied Microbiology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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