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Kinetic behavior of penicillin acylase immobilized on acrylic carrier

โœ Scribed by J. Bryjak; A. Noworyta


Publisher
Springer
Year
1993
Tongue
English
Weight
487 KB
Volume
9
Category
Article
ISSN
1615-7605

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โœฆ Synopsis


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-amino penicillanic acid has not been found. Five components of reaction resistance have been defined. These components were also estimated for the reaction of the native enzyme as well as the Boehringer preparation.

List of symbols

C E g/m 3 Cp, CQ mol/m 3 Cs mol/m 3 Cso mol/m 3 KA mol/m 3 Kis mol/m 3 Kip mol/m 3 KiQ mol/m 3 k 3 mol/g/min R(1) R(2) R(3) R(4) R(5) enzyme concentration product concentrations substrate concentration initial substrate concentration constant which defines the affinity of a substrate to the enzyme substrate inhibitory constant PhAA inhibitory constant 6-APA inhibitory constant constant rate of dissociation of the active complex concentrational component of reaction resistance resistance component derived from substrate affinity resistance component due to the inhibition of the enzyme by substrate resistance component due to the inhibition of the enzyme by PhAA resistance component due to inhibition of the enzyme by 6-APA r= --dCs/dt mol/m 3min rate of reaction t min reaction time ~(i) relative resistance of reaction


๐Ÿ“œ SIMILAR VOLUMES


Immobilization of penicillin acylase on
โœ J. Bryjak; A. Trochimczuk; A. Noworyta ๐Ÿ“‚ Article ๐Ÿ“… 1989 ๐Ÿ› Springer ๐ŸŒ English โš– 409 KB

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

Kinetic behavior of immobilized Penicill
โœ S. W. Carleysmith; P. Dunnill; M. D. Lilly ๐Ÿ“‚ Article ๐Ÿ“… 1980 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 1003 KB

## 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