Purification and Characterization of Extracellular Adenosine Deaminase from Streptomyces sp. J-350P

Streptomyces sp. J-350P가 생산하는 세포외 Adenine Deaminase의 부분정제 및 성질

  • 박정혜 (부산대학교 자연과학대학 미생물학과) ;
  • 전홍기 (부산대학교 자연과학대학 미생물학과)
  • Published : 1987.10.01


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.


Extracellular adenine deaminase;purification