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http://dx.doi.org/10.4014/mbl.1609.09007

Biochemical Characterization of a Novel Thermostable Esterase from the Metagenome of Dokdo Islets Marine Sediment  

Lee, Chang-Muk (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Seo, Sohyeon (Global R&D Center, ISU ABXIS)
Kim, Su-Yeon (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Song, Jaeeun (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Sim, Joon-Soo (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Hahn, Bum-Soo (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Kim, Dong-Hern (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Yoon, Sang-Hong (Metabolic Engineering Division, National Institute of Agricultural Sciences, Rural Development Administration)
Publication Information
Microbiology and Biotechnology Letters / v.45, no.1, 2017 , pp. 63-70 More about this Journal
Abstract
A functional screen of 60,672 fosmid metagenomic clones amplified from marine sediment obtained from the Dokdo islets in Korea identified the gene EstES1, whose product, EstES1, displayed lipolytic properties on tributyrin-supplemented media. EstES1 is a 576 amino acid protein with a predicted molecular weight of 59.4 kDa including 37 N-terminal leader amino acids. EstES1 exhibited the highest sequence similarity (44%) to a carboxylesterase found in Haliangium ochraceum DSM14365. Phylogenetic analysis indicated that EstES1 belongs to a currently uncharacterized family of lipases. Within the conserved domain, EstES1 retains the catalytic triad that consists of the consensus penta-peptide motif, GESAG. EstES1 demonstrated a broad substrate specificity toward the long acyl group of ethyl esters (C2-C12), and its optimal activity was recorded toward p-Nitrophenyl butyrate (C4) at pH 9.0 and $40^{\circ}C$ (specific activity of 255.4 U/mg). The enzyme remained stable in the ranges of $60-65^{\circ}C$ and pH 9.0-10.5 and in the presence of methanol, ethanol, isopropanol, and dimethyl sulfoxide. Therefore, EstES1 has potential for use in industrial applications involving high temperature, organic solvents, and/or alkaline conditions.
Keywords
Esterase; thermostable; Dokdo island; marine sediment; metagenome;
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