Immobilization of Alcaligenes faecalis penicillin G acylase on epoxy-type supports.
Alcaligenes faecalis penicillin G acylase has several desired features over other penicillin G acylases and its use in industry requires immobilization. In this work, two novel supports ZH-EP (epoxy-type) and ZH-HA (epoxy-amino type) were used to immobilize Alcaligenes faecalis penicillin G acylase (AfPGA) with Eupergit C as reference. The saturation of immobilized protein on ZH-EP (269 mg/g, 116 h) and ZH-HA (296 mg/g, 15 h) was obtained more rapidly than Eupergit C (197 mg/g, 260 h). And the activity of immobilized AfPGA on ZH-EP (520 U/g) and ZH-HA (2200 U/g) was higher than that on Eupergit C (310 U/g). The properties of three immobilized enzymes were compared and no obvious difference was observed, which indicated that ZH-EP and ZH-HA were promised in industry.
Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China. dicp402@mail.dlptt.ln.cn
J
J
Sun
Y
Y
Zhou
Z
Z
Yuan
G
G
Xu
D042481:Alcaligenes faecalis / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D004852:Epoxy Compounds / Q000737:chemistry*; D010399:Penicillin Amidase / Q000737:chemistry*
D004800:Enzymes, Immobilized; D004852:Epoxy Compounds; D010399:Penicillin Amidase