Immobilization of enzymes with polyaziridine: II. D-amino acid oxidase
โ Scribed by Carrington S. Cobbs; Leon Lantz; Louis L. Wood; Gary J. Calton
- Publisher
- Springer-Verlag
- Year
- 1990
- Tongue
- English
- Weight
- 345 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0951-208X
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โฆ Synopsis
A novel method of enzyme immobilization using a tri-functional aziridine to immobilize enzymes was used to immobilize D-amino acid oxidase (DAAO) with good retention of enzymatic activity (62%-89%). The stability of the immobilized DAAO in a fixed bed reactor with continuous operation using D-phenylalanine as substrate yielded a projected half-life of 69 days which is far superior to other methods of immobilization of DAAO.
๐ SIMILAR VOLUMES
## Background Immobilization of __Trigonopsis variabilis__ D-amino acid oxidase (__Tv__DAO) on solid support is the key to a reasonably stable performance of this enzyme in the industrial process for the conversion of cephalosporin C as well as in other biocatalytic applications. ## Results To pr
## Abstract A oneโstep procedure of immobilizing soluble and aggregated preparations of Dโamino acid oxidase from __Trigonopsis variabilis__ (__Tv__DAO) is reported where carrierโfree enzyme was entrapped in semipermeable microcapsules produced from the polycation poly(methyleneโcoโguanidine) in co
The preparation of flavin adenine dinucleotide-aftinity columns employing glucose oxidase and D-amino acid oxidase covalently linked to Sepharose-4B is described. Both immobilized enzymes have very good long-term stabilities, retaining at least half of their original flavin adenine dinucleotide-bind