Abstract
The codon-optimized carbonic anhydrase gene of Persephonella marina EX-H1 (PMCA) was expressed and characterized. The gene with the signal peptide removed, PMCA(sp−), resulted in the production of approximately five times more purified protein than from the intact gene PMCA using an Escherichia coli expression system. PMCA(sp−) is formed as homo-dimer complex. PMCA(sp−) has a wide pH tolerance (optimum pH 7.5) and a high thermostability even at 100°C (88min of thermal deactivation half-life). The melting temperature for PMCA(sp−) was 84.5°C. The apparent kcat and Km values for CO2 hydration were 3.2×105s−1 and 10.8mM. The activity of the PMCA(sp−) enzyme was enhanced by Zn2+, Co2+, and Mg2+, but was strongly inhibited by Cu2+, Fe3+, Al3+, Pb2+, Ag+, and Hg2+. PMCA(sp−) readily catalyzed the hydration of CO2, precipitating CaCO3 as calcite in the presence of Ca2+.
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