Food and Fermentation Industries

Purification and Characterization of Glutaminase from Pseudomonas nitroreducens

  • Yang Cheng ,
  • Zhang Tao ,
  • Jiang Bo ,
  • Miao Ming ,
  • Mu Wan-meng ,
  • Ma Ya-jun ,
  • Zhang Wei
Expand

Online published: 2012-12-25

Abstract

Glutaminase from Pseudomonas nitroreducens SK16.004 was purified by ion-exchange and gel filtration chromatography.The characteristics and Km of the enzyme were studied.The result showed that the optimal reaction temperature and pH of purified glutaminase were 55℃ and 9.0,respectively.It was stable within range of pH value from 5.0 to 11.0 under 37℃ to 60℃.The enzyme was greatly activated by Cu2+ and partly inhibited by Fe3+.It exhibited the highest affinity to glutamine and its Km and Vmax were 0.72 mmol/L and 0.55 μmol/(min·mL),respectively.

Cite this article

Yang Cheng , Zhang Tao , Jiang Bo , Miao Ming , Mu Wan-meng , Ma Ya-jun , Zhang Wei . Purification and Characterization of Glutaminase from Pseudomonas nitroreducens[J]. Food and Fermentation Industries, 2012 , 38(12) : 16 -21 . DOI: 10.13995/j.cnki.11-1802/ts.2012.12.015

Outlines

/