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)
Alternative label
  • De Santi C.; Tedesco P.; Ambrosino L.; Altermark B.; Willassen N.-P.; De Pascale D. (2014)
    A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: Functional and structural studies and biotechnological potential
    in Applied biochemistry and biotechnology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Santi C.; Tedesco P.; Ambrosino L.; Altermark B.; Willassen N.-P.; De Pascale D. (literal)
Pagina inizio
  • 3054 (literal)
Pagina fine
  • 3068 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.scopus.com/inward/record.url?eid=2-s2.0-84899483589&partnerID=q2rCbXpz (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 172 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 14 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 6 (literal)
Note
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 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)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it