Characterization and Properties of a New Thermoactive and Thermostable Carbonic Anhydrase

Autor: C. Capasso, V. De Luca, V. Carginale, P. Caramuscio, C. Cavalheiro, R. Cannio, M. Rossi
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Zdroj: Chemical Engineering Transactions, Vol 27 (2012)
Druh dokumentu: article
ISSN: 2283-9216
DOI: 10.3303/CET1227046
Popis: A new carbonic anhydrase was isolated and characterized from the thermophilic bacterium Sulfurihydrogenibium sp. YO3AOP1. The encoding gene was cloned and expressed in Escherichia coli and the recombinant protein purified to homogeneity. This enzyme (SspCA) belongs to the ?? class of the carbonic anhydrase family, is a monomer of 26.1 kDa and shows esterase activity. The kinetic parameters were determined by using CO2 and p-nitrophenylacetate (p-NpA) as substrates. Thermoactivity and thermostability studies showed that SspCA is active in the temperature range from 0 to 100 °C and retains full activity after 2 h incubation at 100 °C. SspCA was immobilized within a polyurethane foam and was found to be unalterably active and stable up to 50 h at 100 °C.
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