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 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
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. |
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ISSN: | 0951-208X 1573-6784 |
DOI: | 10.1007/BF00153750 |