Process of penicillin G hydrolysis catalyzed by penicillin acylase immobilized on acylic carrier
β Scribed by A. Noworyta; J. Bryjak
- Publisher
- Springer
- Year
- 1993
- Tongue
- English
- Weight
- 334 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1615-7605
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## Abstract The kinetic parameters for penicillin G hydrolysis in systems with penicillin G acylase from __Escherichia coli__ (free and immobilized on activated chitosan microbeads produced by electrostatic extrusion) were determined. The obtained kinetic results indicated that both systems (free a
Penicillin acylase obtained from E. Coli (E. C. 3.5.1.11) was covalently bound via glutaric aldehyde to acrylic carriers crosslinked with divinylbenzene or ethylene glycol dimethacrylate. The best enzymatic preparation was obtained by using ethyl acrylate/ ethylene glycol dimethacrylate copolymer. I
The possibility of using the multicompartment immobilized enzyme reactor (MIER) in presence of a charged substrate is here explored. Penicillin G acylase is used to convert penicillin G (a free acid, with a pK of 2.6) into two charged products: phenyl acetic acid (PAA, with a pK of 4.2) and 6-aminop
The usefulness of Lilly's kinetic equation to describe penicillin G hydrolysis performed by immobilized penicillin acylase onto the acrylic carrier has been shown. Based on the experimental results characteristic kinetic constants have been estimated. The effect of noncompetitive inhibition of 6-ami