Adsorption and expression of penicillin G acylase immobilized onto methacrylate polymers generated with varying pore generating solvent volume.
Adsorption and expression of penicillin G acylase was studied on macroporous methacrylate polymer beads of differing pore volume, generated with kerosene. The absorption and expression of the penicillin G acylase was dependent on pore volume. Maximum expression of 57% of adsorbed enzyme was obtained on beads synthesized with 40 mL of kerosene, indicating minimum pore-diffusion limitations.
Kotha
A
A
Chemical Engineering Division, National Chemical Laboratory, Pune, India.
Selvaraj
L
L
Rajan
C R
CR
Ponrathnam
S
S
Kumar
K K
KK
Ambekar
G R
GR
Shewale
J G
JG
D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007648:Kerosene; D010399:Penicillin Amidase / Q000378:metabolism*; D011109:Polymethacrylic Acids; D016062:Porosity
D004800:Enzymes, Immobilized; D007648:Kerosene; D011109:Polymethacrylic Acids; D010399:Penicillin Amidase