## 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
D-amino acid oxidase fromTrigonopsis variabilis: Comparison of enzyme specificity “in vivo” and “in vitro”
✍ Scribed by Eva M. Kubicek-Pranz; Max Röhr
- Publisher
- Springer Netherlands
- Year
- 1985
- Tongue
- English
- Weight
- 227 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0141-5492
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## Abstract A one‐step procedure of immobilizing soluble and aggregated preparations of D‐amino acid oxidase from __Trigonopsis variabilis__ (__Tv__DAO) is reported where carrier‐free enzyme was entrapped in semipermeable microcapsules produced from the polycation poly(methylene‐co‐guanidine) in co
## Abstract The inhibition of D‐amino acid oxidase contained in permeabilized cells of the yeast __Trigonopsis variabilis__ by α‐keto acids (pyruvic acid, phenylpyruvic acid and 4‐methylthio‐2‐oxobutanoic acid), products of the transformation of the corresponding D‐amino acids, was studied. In all
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