The possibility of using the multicompartment immobilized enzyme reactor (MIER) in presence of a charged substrate is here explored. Penicillin G acylase is used to convert penicillin G (a free acid, with a pK of 2.6) into two charged products: phenyl acetic acid (PAA, with a pK of 4.2) and 6-aminop
Enzyme flow microcalorimetry—a useful tool for screening of immobilized penicillin G acylase
✍ Scribed by Alica Vikartovská-Welwardová; Eva Michalková; Peter Gemeiner
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1998
- Tongue
- English
- Weight
- 209 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0268-2575
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✦ Synopsis
Screening of a representative series of immobilized penicillin G acylase biocatalysts (enzyme, cells) using enzyme Ñow microcalorimetry is described. Immobilized penicillin G acylase biocatalysts were either prepared in the laboratory by various techniques or obtained from four commercial manufacturers. An industrial strain of Escherichia coli was entrapped in (poly)acrylamide gel or hardened calcium pectate gel. Semi-puriÐed enzyme was immobilized in various waysÈeither by covalent binding to oxirane-acrylic beads or chlorotriazine bead cellulose or by entrapment in (poly)acrylamide gel. The validity of the enzyme Ñow microcalorimetry results was corroborated by a pH-stat method, showing enzyme Ñow microcalorimetry to be a suitable method for rapid screening of immobilized biocatalysts regardless of the immobilization technique, carrier type or the biocatalyst source.
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