Single-Step purification and immobilization of penicillin acylase using hydrophobic ligands.
Five different hydrophobic ligands immobilized on 4% (4XL) and 6% (6XL) crosslinked agarose were used to study the single-step purification of penicillin acylase from cell lysate. The 4XL gels showed relatively higher specific activity and recovery than the 6XL gels. In single-step purification, highly active enzyme (42 U/mg) was obtained using moderately hydrophobic ligand (octyl). The crude enzyme immobilized on octyl gel by adsorption showed significant operational stability over a period of 30 d at room temperature. Reactor studies demonstrated the feasibility of hydrophobic ligands as a medium for immobilization.
Adikane
H V
HV
Chemical Engineering Division, National Chemical Laboratory, Pune, India. hva@che.ncl.res.in
Singh
R K
RK
Thakar
D M
DM
Nene
S N
SN
D000327:Adsorption; D019149:Bioreactors; D002845:Chromatography / Q000379:methods*; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000201:enzymology; D008024:Ligands; D010399:Penicillin Amidase / Q000737:chemistry* / Q000302:isolation & purification*; D012492:Salts / Q000494:pharmacology; D012685:Sepharose / Q000737:chemistry*; D013696:Temperature; D013997:Time Factors
D008024:Ligands; D012492:Salts; D012685:Sepharose; D010399:Penicillin Amidase