Ionic liquids (ILs) are known to provide stability to biomolecules. ILs are also widely used in the fields of chemical engineering, biological engineering, chemistry, and biochemistry because they facilitate enzyme catalyzed reactions and enhance their conversion rate. In this work, we have evaluated the influence of alkyl chain substitution of ammonium ILs such as diethylammonium dihydrogen phosphate (DEAP) and triethylammonium hydrogen phosphate (TEAP) for the stability and activity of the tobacco etch virus (TEV) protease. Further, we performed molecular dynamics (MD) simulations to calculate the RMSD (root mean square deviation) for TEV and TEV + ILs. Experimental and simulations results show that TEV is more stable in the presence of TEAP than DEAP. Whereas, TEV protease activity for the cleavage of fusion proteins is preserved in the presence of DEAP while lost in the presence of TEAP. Hence, DEAP IL can serve as alternative solvents for the stability of the TEV protease with preserved activity. To the best of our knowledge, this is first study to show that ILs can stabilize and maintain the TEV protease cleavage activity.
|Number of pages||8|
|Journal||International Journal of Biological Macromolecules|
|Publication status||Published - 2020 Jul 15|
Bibliographical noteFunding Information:
This work was supported by several grants ( 2019M3A9F6021810 , NRF-2017M3A9F6029753 , NRF-2019M3E5D6063903 to W. Lee) from the Ministry of Future Creation and Science (MFCS) of Korea. This work was also supported by JSPS -KAKENHI 19H05462 and 16H03895 to PA and MS.
This work was supported by several grants (2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee) from the Ministry of Future Creation and Science (MFCS) of Korea. This work was also supported by JSPS-KAKENHI 19H05462 and 16H03895 to PA and MS.
© 2020 Elsevier B.V.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Economics and Econometrics