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Title 

Purification and characterization of phospholipase D from actinomycetes KF923

 

방선균 KF923이 생산하는 phospholipase D의 정제 및 특성

Authors 

B Y KwakS H YoonChang-Jin KimD H Shon

Publisher 

The Korean Society for Applied Microbiology and Biotechnology

Issue Date 

2003

Citation 

Korean Journal of Microbiology & Biotechnology, vol. 31, no. 4, pp. 389-394

Keywords 

actinomycetescharacteristicsphospholipase Dpurificationsodium ioncontrolled studyculture mediumhydrolysisprotein purification

Abstract 

In order to screen microorganisms producing phopholipase D (PLD) had high transphosphatidylation activity, about 1,000 Actinomycetes strains were isolated from the 63 soil samples, collected over 6 local area in Korea. When the hydrolytic activity in the supernatant was determined, 131 strains produced PLD more than 0.3 U/ml. Among 131 culture broths tested, 23 ones had transphosphatidylation activity higher than 20% and finally one strain (Actinomycetes KF 923), which had highest hydrolytic and transphophadylation activity, was selected. Actinomycetes KF923 showed the highest hydrolytic activity (13 U/ml) and phosphatidylation activity (95%) after 48 h fermentation using the P medium (yeast extract 1%, peptone 1%, glucose 1.5%, glycerol 1%, CaCO3 0.4%, pH 7.2). PLD was purified from the culture broth of Actinomycetes KF923 and the specific activity of purified PLD was 567 U/mg. The molecular weight of PLD was about 55 kD and the optimum pH and temperature were 6.0 and 60°C, respectively. The stability of PLD toward pH and temperature were high around pH 8.0 and below 40°C. Special metal ions were not necessary to the PLD activity.

ISSN 

0257-2389

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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