|
KMID : 0613820080180010084
|
|
Journal of Life Science
2008 Volume.18 No. 1 p.84 ~ p.90
|
|
|
Characterization of Pseudomonas sp. MN5 and Purification of Manganese Oxidizing Protein
|
|
Lee Seung-Hui
Park Kyeong-Ryang
|
|
|
Abstract
|
|
|
|
Bacterial colonies which were able to oxidize the manganese were isolated from six soil samples in Byungchon area. Among them, one bacterial strain was selected for this study based on its high manganese oxidation activity. This selected bacterial strain was identified as Pseudomonas sp. MN5 through physiological-biochemical test and analysis of its 16s rRNA sequence. This selected bacterial strain was able to utilize fructose and maltose, but they doesn’t utilizing various carbohydrates as a sole carbon source. Pseudomonas sp. MN5 showed a very sensitive to antibiotics such as kanamycin, chloramphenicol, streptomycin and tetracycline, but a high resistance up to mg/ml unit to heavy metals such as lithium, manganese and barium. Optimal manganese oxidation condition of Pseudomonas sp. MN5 was pH 7.5 and manganese oxidation activity was inhibited by proteinase K and boiling treatment. The manganese oxidizing protein produced by Pseudomonas sp. MN5 was purified by ammonium sulfate precipitation, HiTrap Q FF anion exchange chromatography and G3000sw XL gel filtration chromatography. By sodium dodecyl sulfate polyacrylamide gel electrophoresis, three manganese oxidizing protein with estimated molecular weights of 15 kDa, 46.7 kDa and 63.5 kDa were detected. Also, it was estimated that manganese oxidizing protein produced by Pseudomonas sp. MN5 were a kind of porin proteins through internal sequence and N-terminal sequence analysis.
|
|
|
KEYWORD
|
|
|
Manganese oxidizing protein, porin, Pseudomonas, purification
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|
|