V
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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Journal ArticleDOI
Biomimetic CO2 capture using a highly thermostable bacterial α-carbonic anhydrase immobilized on a polyurethane foam
Fortunato Migliardini,Viviana De Luca,Vincenzo Carginale,Mosè Rossi,P. Corbo,Claudiu T. Supuran,Clemente Capasso +6 more
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.
Journal ArticleDOI
An α-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction.
Viviana De Luca,Daniela Vullo,Andrea Scozzafava,Vincenzo Carginale,Mosè Rossi,Claudiu T. Supuran,Clemente Capasso +6 more
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.
Journal ArticleDOI
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.
Journal ArticleDOI
X‐ray structure of the first `extremo‐α‐carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1
Anna Di Fiore,Clemente Capasso,Viviana De Luca,Simona Maria Monti,Vincenzo Carginale,Claudiu T. Supuran,Andrea Scozzafava,Carlo Pedone,Mosè Rossi,Giuseppina De Simone +9 more
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.
Journal ArticleDOI
DNA Cloning, Characterization, and Inhibition Studies of an α-Carbonic Anhydrase from the Pathogenic Bacterium Vibrio cholerae
Sonia Del Prete,Semra Isik,Semra Isik,Daniela Vullo,Viviana De Luca,Vincenzo Carginale,Andrea Scozzafava,Claudiu T. Supuran,Clemente Capasso +8 more
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.