Gel-entrapped penicillin G acylase optimized by an enzyme thermistor

Direct activity determination by a flow-through microcalorimetry in the enzyme thermistor system was employed for a fast comparison of (poly)acrylamide gel-entrapped penicillin G acylase preparations. Composition of the pre-polymerization cocktail and both the storage and operational stabilities of...

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Veröffentlicht in:Biotechnology techniques 1993-10, Vol.7 (11), p.809-814
Hauptverfasser: WELWARDOVA, A, GEMEINER, P, MICHALKOVA, E, WELWARD, L, JAKUBOVA, A
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Sprache:eng
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Zusammenfassung:Direct activity determination by a flow-through microcalorimetry in the enzyme thermistor system was employed for a fast comparison of (poly)acrylamide gel-entrapped penicillin G acylase preparations. Composition of the pre-polymerization cocktail and both the storage and operational stabilities of optimal gel-entrapped enzyme preparations isolated from the Escherichia coli industrial strain were optimized by this method. The validity of the results was corroborated by spectrophotometric measurements.
ISSN:0951-208X
1573-6784
DOI:10.1007/BF00153750