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Organic solvent-tolerant (OST) enzymes are widely applied in various industries due to their activity and stability in organic solvents, higher substrate solubility, and increased stereo-selectivity. However, the criteria for identifying OST enzymes largely remain unresolved. In this study, we compared the amino acid composition of 19 OST esterases and 19 non-OST esterases. OST esterases have increased ratio of Ala and Arg residues and decreased ratio of Asn, Ile, Tyr, and Ser residues. Based on the amino acid composition analysis, we cloned acarboxylesterase (EstSP2) from a psychrophilic bacterium, Sphingomonas glacialis PAMC 26605, and characterized its recombinant protein. EstSP2 is substrate specific to p -nitrophenyl acetate and hydrolyzed aspirin, with optimal activityat 40°C; at 4°C, the activity is approximately 50% of its maximum. As expected, EstSP2showstolerance in up to 40% concentration of polar organic solvents, including dimethyl sulfoxide, methanol, and ethanol. The results of this study suggest that selection of OST esterases based on their amino acid composition analysis could be a novel approach to identify OST esterases produced from bacterial genomes.

Organic Solvent-Tolerant Esterase from Sphingomonas glacialisBased on Amino Acid CompositionAnalysis: Cloning and Characterization of EstSP2