Jp. Cardoso, PURIFICATION OF PENICILLIN-G AMIDASE USING QUATERNARY AMMONIUM-SALTS AND EFFECT ON THE ACTIVITY OF THE IMMOBILIZED ENZYMES, Bioprocess engineering, 16(4), 1997, pp. 209-218
This paper describes the purification of Penicillin G Amidase (EC 3.5.
1.11) using quaternary ammonium salts with the aim of increasing the a
ctivity of immobilised enzymes prepared from the purified solutions. T
wo different quaternary ammonium salts were tested with different solu
tions of the enzyme. It was concluded that the quaternary ammonium sal
ts used selectively precipitated the non-enzymatic protein leaving in
solution practically all the enzyme resulting in a high yield of purif
ication. Optimal conditions for purification using the two types of qu
aternary ammonium salts were determined. Immobilisation studies were p
erformed from various purified enzyme solutions, using different amoun
ts of a quaternary ammonium salt. The immobilised enzymes so obtained
showed a much higher activity than the immobilised enzyme obtained fro
m non-purified enzyme solutions.