• YAKHAK HOEJI
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• v.38 no.3
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• pp.274-280
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• 1994

A strain of actinomycetes producing extracellular adenosine deaminase inhibitor, strain V-8, was isolated from soil. Strain V-8 was gam positive and its cell wall chemotype was decided as cell wall chemotype I from analysis of diaminopimelic acid isomers and sugar pattern. This strain had a wide range of sugar utilization as carbon sources. The optimal pH and temperature for growth were $6.8{\sim}7.0$ and $28{\sim}30^{\circ}C$, respectively. From the morphological, chemotaxonomical characteristics and analysis of various physiological characteristics, the strain V-8 was identified Streptomyces sp.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.83-89
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• 1990

Two strains of actinomycetes producing extracellular adenosine deaminase, strain J-845S and strain J-326TK, were isolated from soil. Strain J-845S was gram-positive and non-acid-fast. This strain formed whitish, rod-shaped, smooth and non-motile spores on the aerial mycelium, and the spore chain was spiral. The hyphae of the mycelium branched abundantly. Cell wall chemotypes of the strain were of type I containing LL-diaminopimelic acids, and of phospholipid type II, and then strain J-845S was designated as Streptomyces sp.. Strain J-326TK was gram-positive and non-acid-fast. The hyphae of primary and aerial mycelium fragmented into irregular rod of coccus-like elements. The aerial mycelium either did not branch or sparsely branched. Cell wall composition was of type I and phospholipid type I. Thus, strain J-326TK was identified as Nocardioides sp.

• Microbiology and Biotechnology Letters
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• v.15 no.5
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• pp.306-311
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• 1987

After series of purification by means of ammonium sulfate fractionation, the 1st and 2nd DEAE-Cellulose, DEAE-Sephadex A-50, and Sephacryl S-200 superfine gel filtration, the activity of extracellular adenine deaminase from Streptomyces sp. J-350P increased 1764 fold and the yield was 0.3% of original activity. The enzyme was stable at the pH range 6.5 to 8.5 and at up to 5$0^{\circ}C$. The optimum pH and temperature of the enzyme were around 6.5 and 35$^{\circ}C$. The molecular weight ol the enzyme was estimated as 36, 000 by calibrated Sephacryl S-200 superfine column chromatography.

• Proceedings of the KSME Conference
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• 2008.11a
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• pp.1687-1689
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• 2008

In the detection of pathogenic microorganisms ATP-bioluminescence reaction is a fascinating method. ATP(adenosine triphosphate) is an energy source of all kinds of living organism and ATP-bioluminescence reaction uses this ATP. However, ATP exists not only in the cells but also outside the cells. Therefore ATP-bioluminescence reaction only with intracellular ATP is very important in pathogenic microorganism detection. Because of that reason we developed a microfluidic channel containing Dielectrophoretic zone which capture microorganisms and eliminating and washing extracellular ATP with ATP-degarading enzymes, adenosine phosphate deaminase and apyrase. Microorganisms are captured by pDEP force at the DEP electrode zone and only extracellular ATPs are washed and eliminated outside the zone.