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Understanding Thermal and Organic Solvent Stability of Thermoalkalophilic Lipases: Insights from Computational Predictions and Experiments

preprint
submitted on 16.12.2019 and posted on 20.12.2019 by Mohamed Shehata, Emel Timucin, Alessandro Venturini, Osman Ugur Sezerman
The study enclosed herein reports computational and experimental findings on the active and inactive conformations of the lipase from the family I.5. Given their high stability under extreme conditions, this lipase family, also called thermoalkalophilic liapses, are of high potential for industrial reactions. To this end, this study investigated the structural impact of 5 different organic solvents that are commonly used in industrial reactions, on the active and inactive conformations in silico. These findings were validated by the experiments which recruited the recombinant enzyme and analyzed organic solvent stability at different temperatures.

Funding

This work supported by The Scientific and Technological Research Council of Turkey and The National Research Council of Italy (TUBITAK grant no. 215Z712). The numerical calculations reported in this paper were partially performed at TUBITAK ULAKBIM, High Performance and Grid Computing Center (TRUBA resources).

History

Email Address of Submitting Author

mohamed.gyte@gmail.com

Institution

Acibadem University

Country

Turkey

ORCID For Submitting Author

0000-0003-0841-4577

Declaration of Conflict of Interest

The authors declare no competing interests.

Version Notes

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