Gentisate dioxygenase activity in immobilized cell-free extracts prepared fromSalmonella typhimurium
โ Scribed by Frederick E. Goetz; Jeonghui Joo
- Book ID
- 104650383
- Publisher
- Springer-Verlag
- Year
- 1990
- Tongue
- English
- Weight
- 260 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0951-208X
No coin nor oath required. For personal study only.
โฆ Synopsis
Cell-free extracts of Salmonella typhimurium containing gentisate dioxygenase were immobilized by entrapment in carrageenan and polyacrylamide and adsorption to polyester filters. Carrageenan gels were very porous, and the enzyme was slowly inactivated in polyacrylamide. When adsorbed on polyester the enzyme could be lyophilized and reactivated. Batch reactors charged with the immobilized enzyme converted gentisate to maleylpyruvate with yields of 10-90%.
๐ SIMILAR VOLUMES
In order to better understand the high plasmid stability in immobilized recombinant E. coli cells, the effects of dilution rate on the pTG201 plasmid stability, the copy number, and the catechol 2,3-dioxygenase (encoded by XyIE gene) production were, at first, studied in free E. coli W3101 continuou
Wheat embryo extracts are commonly used in cell-free protein synthesis studies. Soluble inhibitor(s) that diminish aminoacylation of tRNA exist in such extracts. These inhibitors can be effectively removed by prolonged dialysis, provided that proper salt conditions are maintained to ensure stability