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
Immobilization of penicillin acylase on acrylic carriers
โ Scribed by J. Bryjak; A. Trochimczuk; A. Noworyta
- Publisher
- Springer
- Year
- 1989
- Tongue
- English
- Weight
- 409 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1615-7605
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โฆ Synopsis
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 cm 3 of the carrier bound 6.4 mg of protein, having 72% activity in relation to the native enzyme. The preparation lost only 10% of its initial activity after 100 d of storage at 4~ A negligible effect of immobilization on the enzyme activity at different temperatures or pH as well as significant increase of the stability of the immobilized enzyme at elevated temperatures were observed.
Abbreviations
BA AE PA 6-APA EGDMA DVB butyl acrylate ethyl acrylate penicillin acylase 6-aminopenicillanic acid ethylene glycol dimethacrylate divinylbenzene
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## Abstract Penicillin acylase has been immobilized to carboxymethylcellulose and to the resin Amberlite XAD7. The reaction kinetics of the enzyme were affected by both intrinsic (molecular) and microenvironmental effects. The Michaelis constant for the enzyme increased after immobilization as a re