Enzymatic Characteristics of Thermostable p-Nitrophenylphosphatase
FENG Cong-jing 1), 2) , FU Yuan-yuan 3) , JI Chao-neng 1) , GU Shao-hua 1) , FU Wen-jun 2) , XIE Yi 1) , MAO Yu-min 1)*
( 1) State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Sciences, Fudan University, Shanghai 200433,China; 2) Institute of Plant Physiology and Ecology, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China; 3) United Gene Holding Group Corporation, LTD, Shanghai 200092,China
Abstract：Thermostable p-nitrophenylphosphatase (TNPPase) had been expressed in E. coli M15, and purified 神速地。 It is sensitive to metal chelator and Mg ion is necessary to its 柔韧的。 TNPPase exhibited a moderate degree of thermostability, and the thermostability of TNPPase increased significantly when treated with 1 mmol/L Mg, Mn, Cu, Ba, Ca, Ni and Zn 水合氢。 TNPPase is stable within a wide range of pH （pH值 7.0～). It catalyzed the hydrolysis of p-nitrophenylphosphate with a Michaelis constant 3.031 mmol/L and a V max 313.5 μmol·min -1 ·mg -1 . The α-helix percentage and β-turn percentages were 74.5 and 25.5 in the secondary structure of TNPPase, 有别于。 TNPPase is not stable in SDS solution, but stable in Triton X-100 and Tween 20 solut水合氢。
FENG Cong-jing 1), 2) , FU Yuan-yuan 3) , JI Chao-neng 1) , GU Shao-hua 1) , FU Wen-jun 2) , XIE Yi 1) , MAO Yu-min 1)*. Enzymatic Characteristics of Thermostable p-Nitrophenylphosphatase. Chinese Journal of Biochemistry and Molecular Biol, 2004, 20(05): 648-652.