The kinetics of penicillin-V deacylation on an immobilized enzyme

An immobilized Penicillin‐V‐acylase (commercial name, Novozym 217) with high specificity for the phenoxyacetyl‐(V)‐ side chain was investigated in a recycle reactor and in a batch reactor to find the enzymatic reaction rate as a function of conversion, x, substrate concentration, c A0 and pH. The re...

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Veröffentlicht in:Biotechnology and bioengineering 1983-07, Vol.25 (7), p.1873-1895
Hauptverfasser: Haagensen, P., Karlsen, L. G., Petersen, J., Villadsen, J.
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Sprache:eng
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Zusammenfassung:An immobilized Penicillin‐V‐acylase (commercial name, Novozym 217) with high specificity for the phenoxyacetyl‐(V)‐ side chain was investigated in a recycle reactor and in a batch reactor to find the enzymatic reaction rate as a function of conversion, x, substrate concentration, c A0 and pH. The reaction rate depends strongly on pH, and both products, phenoxy‐acetic acid and 6‐APA, inhibit the reaction. Nonspecific side reactions amount to only a few per cent when c A0
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.260250715