Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde.
The activity of penicillin G acylase from Alcaligenes faecalis increased 7.5-fold when cells were permeabilized with 0.3% (w/v) CTAB. The treated cells were entrapped by polyvinyl alcohol crosslinked with boric acid, and crosslinked with 2% (v/v) glutaraldehyde to increase the stability. The conversion yield of penicillin G to 6-aminopenicillanic acid was 75% by immobilized system in batch reaction. No activity was lost after 15 cycles and about 65% enzyme activity was retained at the end of the 31th cycle.
Cheng
Shiwei
S
State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, PR China.
Wei
Dongzhi
D
Song
Qingxun
Q
Zhao
Xiangguo
X
D018929:Cell Culture Techniques / Q000379:methods*; D000077286:Cetrimonium; D002593:Cetrimonium Compounds / Q000494:pharmacology*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D005976:Glutaral / Q000737:chemistry*; D010399:Penicillin Amidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D010539:Permeability; D016062:Porosity; D014462:Ultrafiltration / Q000295:instrumentation / Q000379:methods*
D002593:Cetrimonium Compounds; D004800:Enzymes, Immobilized; D010399:Penicillin Amidase; D005976:Glutaral; D000077286:Cetrimonium