Abstract
Using a metagenome library constructed from a bacterial associated with a marine sponge Hyrtios erecta, we identified a novel esterase that belongs to the SGNH hydrolase superfamily of esterases. The substrate specificity of EstHE1 was determined using p-nitrophenyl (pNP) ester (C2: acetate, C4: butylate, C6: caproate, C12: laurate, C16: palmitate). EstHE1 exhibited activity against C2 (5.6 U/mg), C4 (5.1 U/mg), and C6 (2.8 U/mg) substrates. The optimal temperature for EstHE1 esterase activity of the pNP acetate substrate was 40°C, and EstHE1 retained 60% of its enzymatic activity in the 30–50°C range. This esterase showed moderate thermostability, retaining 58% of its activity even after preincubation for 12 h at 40°C. EstHE1 also maintained activity in high concentrations of NaCl, indicating that this esterase is salt-tolerant. Thus, EstHE1 has the thermal stability and salt tolerance necessary for use as an industrial enzyme.
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This work was funded in part by the New Energy and Industrial Technology Development Organization (NEDO) as part of a research and development project of the Industrial Science and Technology Frontier Program.
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Okamura, Y., Kimura, T., Yokouchi, H. et al. Isolation and Characterization of a GDSL Esterase from the Metagenome of a Marine Sponge-associated Bacteria. Mar Biotechnol 12, 395–402 (2010). https://doi.org/10.1007/s10126-009-9226-x
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DOI: https://doi.org/10.1007/s10126-009-9226-x