A scalable overexpression of a thermostable recombinant poly-histidine tag carboxyl esterase under lambda promoter: purification, characterization, and protein modelling
Nadia A. Soliman, Safaa M. Ali, Mahmoud E. A. Duab, Yasser R. Abdel-Fattah · 2023
Read A scalable overexpression of a thermostable recombinant poly-histidine tag carboxyl esterase under lambda promoter: purification, characterization, and protein modelling by Nadia A. Soliman, Safaa M. Ali, Mahmoud E. A. Duab, Yasser R. Abdel-Fattah (2023) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-10716096.txt.
Description
Nadia Soliman and three co-workers built germs to mass make a heat proof enzyme for trade use. Esterases are workhorse agents used in drugs, skin creams, foods, soaps, and waste clean up. The team took a gene for one such agent from a Geobacillus type and added a tag to purify it in one step. Escherichia coli germs then made the gene's protein with a lambda switch. The 2023 study scaled the work up to a seven litre stirred tank.
The protein ran to 499 amino acids. It held the shared code mark that is the norm for its enzyme clan. Its guessed shape matched a known kin at near 95 percent likeness. The team cleaned the enzyme, probed its traits, and built a model of its shape. A broad supply of a heat proof esterase suits trade steps that run hot.
Catalog record
| CREATOR | Nadia A. Soliman, Safaa M. Ali, Mahmoud E. A. Duab, Yasser R. Abdel-Fattah |
|---|---|
| YEAR | 2023 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 31 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |