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Viviana De Luca

Researcher at University of Florence

Publications -  74
Citations -  2666

Viviana De Luca is an academic researcher from University of Florence. The author has contributed to research in topics: Carbonic anhydrase & Enzyme. The author has an hindex of 33, co-authored 63 publications receiving 2380 citations.

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Biomimetic CO2 capture using a highly thermostable bacterial α-carbonic anhydrase immobilized on a polyurethane foam

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.
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An α-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction.

TL;DR: The biochemical properties, thermostability and inhibition of SazCA were compared with those of the thermophilic and mesophilic counterparts, demonstrating the special features of this unique enzyme.
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Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1.

TL;DR: A new carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 was identified and characterized and showed biochemical properties never observed for the mammalian enzyme.
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X‐ray structure of the first `extremo‐α‐carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1

TL;DR: The study suggests that increased structural compactness, together with an increased number of charged residues on the protein surface and a greater number of ionic networks, seem to be the key factors involved in the higher thermostability of this enzyme with respect to its mesophilic homologues.
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DNA Cloning, Characterization, and Inhibition Studies of an α-Carbonic Anhydrase from the Pathogenic Bacterium Vibrio cholerae

TL;DR: This work cloned, purified, and characterized an α-carbonic anhydrase from the human pathogenic bacterium Vibrio cholerae, and proposes that VchCA may be a target for antibiotic development, exploiting a mechanism of action rarely considered until now.