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- W2005476581 abstract "Permeabilization of the cells of E. coli with N-cetyl-N, N, N-trimethylammoniumbromide (CTAB) showed 40% increase in penicillin G acylase activity. The treated cells were immobilized in porous beads of gelatin cross-linked with glutaraldehyde. Upon entrapment the catalytic properties of enzyme were changed as compared to non-immobilized form. Hydrolysis of penicillin G by immobilized system showed 60% conversion of substrate to 6-aminopenicillanic acid in batch system, whereas in continuous system, the conversion rate was 85%. The immobilized form of whole cell penicillin acylase showed low Km toward penicillin G as a substrate." @default.
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- W2005476581 date "2002-01-01" @default.
- W2005476581 modified "2023-09-25" @default.
- W2005476581 title "Immobilization of whole cell penicillin G acylase in open pore gelatin matrix" @default.
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- W2005476581 doi "https://doi.org/10.1016/s0141-0229(01)00445-8" @default.
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