Mosè Rossi

TL;DR: The recent advent of glycosynthases – specifically mutated glycosidases that efficiently synthesize oligosaccharides but do not hydrolyse them – represents a promising solution to these problems.

TL;DR: Three-dimensional structures of SsoPox demonstrate that promiscuous activities probably constitute a large and efficient reservoir for the creation of novel catalytic activities, and propose a mechanism for lactone hydrolysis and to refine the catalytic mechanism established for phosphotriesterases.

TL;DR: In contrast with its mesophilic E. coli counterpart that was devoid of any tested activity, the S. solfataricus enzyme was demonstrated to have a low paraoxonase activity that was dependent from metal cations with Co2+, Mg2+ and Ni2+ being the most effective and was thermophilic and thermostable.

TL;DR: A bioreactor containing the “PU-immobilized enzyme” (PU-SspCA) as shredded foam was used for experimental tests aimed to verify the CO2 capture capability in conditions close to those of a power plant application.

TL;DR: A plasmid able to transform and to be stably maintained both in Sulfolobus solfataricus and in Escherichia coli was constructed by insertion into an E. coli plasmids of the autonomously replicating sequence of the virus particle SSV1 and a suitable mutant of the hph (hygromycin phosphotransferase) gene as the transformation marker.