http://www.cnr.it/ontology/cnr/individuo/prodotto/ID280611
A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: Functional and structural studies and biotechnological potential (Articolo in rivista)
- Type
- Label
- A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: Functional and structural studies and biotechnological potential (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s12010-013-0713-1 (literal)
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- De Santi C.; Tedesco P.; Ambrosino L.; Altermark B.; Willassen N.-P.; De Pascale D. (literal)
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- Department of Chemistry, Faculty of Science and Technology, University of Tromsø, Tromsø, Norway; Institute of Protein Biochemistry, National Research Council, Via P. Castellino, 111, 80131 Naples, Italy (literal)
- Titolo
- A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: Functional and structural studies and biotechnological potential (literal)
- 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. © 2014 Springer Science+Business Media. (literal)
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