http://www.cnr.it/ontology/cnr/individuo/prodotto/ID197619
Biochemical properties of a novel and highly thermostable bacterial ?-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1 Read More: http://informahealthcare.com/doi/abs/10.3109/14756366.2012.703185 (Articolo in rivista)
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- Biochemical properties of a novel and highly thermostable bacterial ?-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1 Read More: http://informahealthcare.com/doi/abs/10.3109/14756366.2012.703185 (Articolo in rivista) (literal)
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- 2012-01-01T00:00:00+01:00 (literal)
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- 10.3109/14756366.2012.703185 (literal)
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Clemente Capasso1, Viviana De Luca1, Vincenzo Carginale1, Raffaele Cannio1, Mosè Rossi1,2 (2012)
Biochemical properties of a novel and highly thermostable bacterial ?-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1 Read More: http://informahealthcare.com/doi/abs/10.3109/14756366.2012.703185
in Journal of enzyme inhibition and medicinal chemistry (Print)
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- Clemente Capasso1, Viviana De Luca1, Vincenzo Carginale1, Raffaele Cannio1, Mosè Rossi1,2 (literal)
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- http://informahealthcare.com/doi/pdf/10.3109/14756366.2012.703185 (literal)
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- 1. CNR, Istituto di Biochimica delle Proteine (IBP), Napoli, Italy
2. Centro di Ricerca Interdipartimentale sui Biomateriali, Università di Napoli, \"Federico II\", Napoli, Italy (literal)
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- Biochemical properties of a novel and highly thermostable bacterial ?-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1 Read More: http://informahealthcare.com/doi/abs/10.3109/14756366.2012.703185 (literal)
- Abstract
- A new carbonic anhydrase (CA, EC 4.2.1.1) from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 was identified and characterized. The bacterial carbonic anhydrase gene was expressed in Escherichia coli yielding an active enzyme, which was purified in large amounts. The recombinant protein (SspCA) was found to belong to the ?-CA class and displays esterase activity. The kinetic parameters were determined by using CO(2) and p-nitrophenylacetate (p-NpA) as substrates. The bacterial enzyme presented specific activity comparable to that of bovine carbonic anhydrase (bCA II) but it showed biochemical properties never observed for the mammalian enzyme. The thermophilic enzyme, in fact, was endowed with high thermostability and with unaltered residual activity after prolonged exposure to heat up to 100°C. SspCA and the bovine carbonic anhydrase (bCA II) were immobilized within a polyurethane (PU) foam. The immobilized bacterial enzyme was found to be active and stable at 100°C up to 50 h. (literal)
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