[Studies on some properties of the immobilized penicillin acylase by polyacrylonitrile fibres].
The extracellular penicillin acylase from Bacillus megaterium was immobilized by coupling to derivatives of polyacrylonitrile fibres. The apparent activity of the immobilized penicillin acylase was about 2,000 u/g (dry weight). The optimal pH and temperature were 9.0 and 50 degrees C for hydrolysis of penicillin G, respectively. The immobilized enzyme was stable in the pH range of 5.5-10.3, and at the temperature below 50 degrees C. The apparent Michaelis constant Ka and Vm of the immobilization enzyme were 1.33 x 10(-2) mol/L and 2.564 mmol.min-1, respectively. The inhibition constant of phenylacetic acid acted as a competitive inhibitor for The immobilization enzyme was 0.16 mol/L. The remained activity was about 80% after operating 20 times.
Han
H
H
Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080.
Xu
G
G
Zhu
L
L
Han
W
W
Wang
Z
Z
D000180:Acrylic Resins / Q000737:chemistry*; D001410:Bacillus megaterium / Q000201:enzymology; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010399:Penicillin Amidase / Q000378:metabolism*; D010400:Penicillin G / Q000378:metabolism; D013696:Temperature
D000180:Acrylic Resins; D004800:Enzymes, Immobilized; C010504:polyacrylonitrile; D010399:Penicillin Amidase; D010400:Penicillin G