Immobilization of permeabilized Escherichia coli cells with penicillin acylase activity.
Escherichia coli cells with penicillin acylase activity were sequentially treated at pH 7.8 with aqueous solutions of N-cetyl-N,N,N-trimethylammonium bromide and glutaraldehyde and then immobilized within porous polyacrylamide beads. The immobilized whole cells showed enhanced hydrolysis rates in the conversion of benzylpenicillin to 6-aminopenicillanic acid (6-APA) compared to untreated cells immobilized and used under identical conditions. The immobilized system showed no apparent loss in enzyme activity when used repeatedly over 90 cycles for 6-APA production from 4% benzylpenicillin.
Prabhune
A A
AA
Biochemical Sciences Division, National Chemical Laboratory, Pune, India.
Rao
B S
BS
Pundle
A V
AV
SivaRaman
H
H
D002463:Cell Membrane Permeability; D000077286:Cetrimonium; D002593:Cetrimonium Compounds / Q000494:pharmacology; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D005976:Glutaral / Q000494:pharmacology; D007700:Kinetics; D010399:Penicillin Amidase / Q000378:metabolism*
D002593:Cetrimonium Compounds; D004800:Enzymes, Immobilized; D010399:Penicillin Amidase; D005976:Glutaral; D000077286:Cetrimonium