Purification of d-amino acid oxidase from Trigonopsis variabilis
✍ Scribed by Clarence P. Berg; Frank A. Rodden
- Publisher
- Elsevier Science
- Year
- 1976
- Tongue
- English
- Weight
- 573 KB
- Volume
- 71
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract __Trigonopsis variabilis__ D‐amino acid oxidase (__Tv__DAO) is a long‐known flavoenzyme whose most important biocatalytic application is currently the industrial production of 7‐amino‐cephalosporanic acid (7‐ACA) from cephalosporin C. Lacking mechanistic foundation, rational stabilizati
## 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
The industrial importance of Trigonopsis variabilisd-amino acid oxidase (TvDAAO) is represented by its biocatalytic oxidative deamination of cephalosporin C (CPC) to yield glutaryl-7-aminocephalosporanic acid (GL-7-ACA). The process has been incorporated into a two-step bioconversion to produce 7-am
## 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