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Penicillin amidase

About: Penicillin amidase is a research topic. Over the lifetime, 576 publications have been published within this topic receiving 15563 citations. The topic is also known as: penicillin amidohydrolase & ampicillin acylase.


Papers
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Journal ArticleDOI
TL;DR: The results suggest that the adsorption of proteins on supports bearing almost neutral charge is not driven by the existence of opposite charges between the adsorbent and the biomacromolecule but just by the possibility of forming a high number of enzyme-support ionic bonds.

39 citations

Journal ArticleDOI
TL;DR: Immobilization of the enzyme in polyelectrolyte complex particles leads to the appearance of new properties of the biocatalyst; immobilized penicillin amidase can be reversibly converted to the insoluble state with a slight change in pH and ionic strength of the solution.

39 citations

Journal ArticleDOI
TL;DR: Immobilisation of both native and modified enzymes resulted in the thermostabilisation of the penicillin amidase, and good relative activity of the enzymes was obtained after insolubilisation.

39 citations

Journal ArticleDOI
TL;DR: Permeabilization of the cells of E. coli with N-cetyl-N, N, N-trimethylammoniumbromide (CTAB) showed 40% increase in penicillin G acylase activity, whereas in continuous system, the conversion rate was 85%.

39 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20234
20222
20183
20175
20165
20153