๐”– Bobbio Scriptorium
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Structural studies of penicillin acylase

โœ Scribed by James A. Brannigan; Guy G. Dodson; Sarah H. Done; Lorraine Hewitt; Colin E. McVey; Keith S. Wilson


Book ID
111635129
Publisher
Springer-Verlag
Year
2000
Tongue
English
Weight
218 KB
Volume
88
Category
Article
ISSN
0273-2289

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Penicillin acylase from Bacillus rneg~terj~lln was purified 5.22 fold using ultrafiltration followed bp ammonium sulphate precipitation and gel filtration chromatography using Sephades G-100. The final specific activity was 2.62 Uimg protein and was free from interfering proteases.

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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