Thermophilic Carboxylesterases from Hydrothermal Vents of the Volcanic Island of Ischia Active on Synthetic and Biobased Polymers and Mycotoxins
Marco A. Distaso, Tatyana N. Chernikova, Rafael Bargiela, Cristina Coscolín, P.J. Stogios, José L. González-Alfonso, Sofia Lemak, Anna N. Khusnutdinova, Francisco J. Plou, E. Evdokimova, Alexei Savchenko, Evgenii A. Lunev, Michail M. Yakimov, Olga V. Golyshina, Manuel Ferrer, Alexander F. Yakunin, Peter N. Golyshin
Abstract
and showed low sequence similarity to known carboxylesterases. Active sites of IS10 and IS12 had the largest effective volumes among the characterized prokaryotic carboxylesterases and exhibited high substrate promiscuity, including hydrolysis of polyesters and mycotoxin T-2 (IS12). Though less promiscuous than IS10 and IS12, IS11 had a higher thermostability with a high temperature optimum (80 to 90°C) for activity and hydrolyzed polyesters, and its crystal structure revealed an unusual lipocalin domain likely involved in substrate binding. The polyesterase activity of these enzymes makes them attractive candidates for further optimization and potential application in plastics recycling.