An Industrial View on Enzymes for the Cleavage of Cephalosporin C
Due to the compensation for low operational stability by low costs of preparation, cell immobilization of Trigonopsis variabilis seems an economically attractive and technically feasible way to prepare D-amino acid oxidase (EC 220.127.116.11). However, the application of immobilized cells is restricted to large-volume products, since it involves extensive development and characterization work.
For glutaryl-7-ACA acylase (EC 18.104.22.168), expressed in Escherichia coli, isolation and immobilization of the enzyme on a commercial carrier seems more attractive from a regulatory point of view. The immobilized enzyme shows very high operational stability, which may compensate for the costs of the carrier.
Despite its lower stability, cephalosporin G acetylesterase (EC 22.214.171.124), expressed in E. coli, was also immobilized on a commercial carrier for regulatory reasons. Moreover, extensive development of immobilized whole cells seemed economically not acceptable for this low-volume product.
A mathematical model for the enzymatic cleavage showed limitations of a combined application of two biocatalysts in a stirred tank reactor, e.g., in terms of product yield.
Document Type: Research Article
Publication date: December 1, 1999
International Journal for Chemistry and Official Membership Journal of the Swiss Chemical Society (SCS) and its Divisions
CHIMIA, a scientific journal for chemistry in the broadest sense, is published 10 times a year and covers the interests of a wide and diverse readership. Contributions from all fields of chemistry and related areas are considered for publication in the form of Review Articles and Notes. A characteristic feature of CHIMIA are the thematic issues, each devoted to an area of great current significance.
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