A New Alkaliphilic Cold-Active Esterase from the Psychrophilic Marine Bacterium Rhodococcus sp.: Functional and Structural Studies and Biotechnological Potential |
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Authors: | Concetta De Santi Pietro Tedesco Luca Ambrosino Bjørn Altermark Nils-Peder Willassen Donatella de Pascale |
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Affiliation: | 1. Institute of Protein Biochemistry, National Research Council, Via P. Castellino, 111, 80131, Naples, Italy 2. NorStruct, Department of Chemistry, Faculty of Science and Technology, University of Troms?, Troms?, Norway
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Abstract: | The special features of cold-adapted lipolytic biocatalysts have made their use possible in several industrial applications. In fact, cold-active enzymes are known to be able to catalyze reactions at low temperatures, avoiding side reactions taking place at higher temperatures and preserving the integrity of products. A lipolytic gene was isolated from the Arctic marine bacterium Rhodococcus sp. AW25M09 and expressed in Escherichia coli as inclusion bodies. The recombinant enzyme (hereafter called RhLip) showed interesting cold-active esterase activity. The refolded purified enzyme displayed optimal activity at 30 °C and was cold-active with retention of 50 % activity at 10 °C. It is worth noting that the optimal pH was 11, and the low relative activity below pH 10 revealed that RhLip was an alkaliphilic esterase. The enzyme was active toward short-chain p-nitrophenyl esters (C2–C6), displaying optimal activity with the butyrate (C4) ester. In addition, the enzyme revealed a good organic solvent and salt tolerance. These features make this an interesting enzyme for exploitation in some industrial applications. |
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