Streptomycete 2-nitropropane dioxyenase gene and its application
A technology of dioxygenase and nitropropane, applied in application, genetic engineering, oxidoreductase and other directions, can solve the problem of not many structural genes, and achieve the effect of improving the environment
- Summary
- Abstract
- Description
- Claims
- Application Information
AI Technical Summary
Problems solved by technology
Method used
Image
Examples
Embodiment 1
[0025] Example 1: Cloning and expression of npD gene
[0026] 1. Cloning of npD gene
[0027] 1.1 Preparation of probes
[0028] In the cloned Streptomyces coelicolor A3 (2) development and differentiation promoter pTH270 upstream part of the gene inside there is a SmaI restriction site, using SmaI and HindIII on the multiple cloning site for plasmid pIJ4478 [Tan H & Chater K.J.Bacteriol .1993, 175 (4): 933-940] (the gene sequence containing pTH270 and its upstream and downstream partial sequences) to perform double enzyme digestion to obtain a DNA fragment of about 320bp.
[0029] Take 10ng-3μg DNA to denature in boiling water for 10 minutes, immediately put it in ice / NaCl for 3 minutes; add 2μl hexanucleotide mixture, 2μl dNTP mixture containing digoxigernin-11-dUTP, add distilled water to 19μl, finally add 1μl Klenow enzyme After incubation at 37°C for 20 hours, 2 μl of 0.2M EDTA (pH 8.0) was added to terminate the reaction. Then add 2.5 μl 4M LiCl, 75 μl pre-cooled abso...
Embodiment 2
[0056] Embodiment 2: Separation, purification and biological activity of 2-nitropropane dioxygenase
[0057] The obtained cell fragments were subjected to Sephadex column chromatography, eluted with 0.01M phosphate buffer (pH 7.0), the active fractions were combined, and subjected to DEAE Sepharose Fast Flow column chromatography. Wash with 2-3 column volumes of 0.2M and 0.3M sodium chloride, and finally elute with 0.4M sodium chloride. The active part is subjected to repeated column chromatography on DEAE Sepharose Fast Flow, and the purity is detected by SDS-PAGE . The results showed that after the above purification process, the target protein NPD with good purity and activity was obtained.
[0058] After mixing 0.05 μg of enzyme solution, 100 μl of 0.4 mM substrate and 800 μl of 0.2M phosphate buffer (pH 7.0), they were reacted at 37° C. for 5 minutes, and the reaction was terminated with 200 μl of 5 mM copper sulfate. Add 0.5ml of p-aminobenzenesulfonic acid (0.33%) and...
PUM
Login to View More Abstract
Description
Claims
Application Information
Login to View More 


