@misc{10481/103445,
year = {2025},
month = {3},
url = {https://hdl.handle.net/10481/103445},
abstract = {Oxalate decarboxylase (OxDC) from Bacillus subtilis is a Mn-dependent hexameric enzyme that converts oxalate to carbon dioxide and formate. Recently, OxDC has attracted the interest of the scientific community due to its biotechnological and medical applications for the treatment of hyperoxaluria, a group of pathologic conditions associated with excessive oxalate urinary excretion caused by either increased endogenous production or increased exogenous absorption. The fact that OxDC displays optimum pH in the acidic range represents a big limitation for most biotechnological applications involving processes occurring at neutral pH, where the activity and stability of the enzyme are remarkably reduced. Here, through bioinformatics-guided protein engineering followed by combinatorial mutagenesis and analyses of activity and thermal stability, we identified a double mutant of OxDC endowed with enhanced catalytic efficiency and stability under physiological conditions. The obtained engineered form of OxDC offers a potential tool for improved intestinal oxalate degradation in hyperoxaluria patients.},
organization = {Italian Ministry of University
and Research (SIR project RBSI148BK3)},
organization = {Okinawa Institute of Science and Technology
Graduate University (OIST)},
organization = {Cabinet Office, Government of Japan},
organization = {Japan Society for the Promotion of Science
(JSPS) for the KAKENHI Early Career Scientist N. 22K15065},
publisher = {American Chemical Society},
title = {Engineered Oxalate Decarboxylase Boosts Activity and Stability for Biological Applications},
author = {Dindo, Mirco and Conter, Carolina and Uechi, Gen-Ichiro and Pampalone, Gioena and Ruta, Luana and Pey Rodríguez, Ángel Luis and Rossi, Luigia and Laurino, Paola and Magnani, Mauro and Cellini, Barbara},
}