De Santi_2014_Appl.Biochem.Biotechnol_172_3054

Reference

Title : A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: functional and structural studies and biotechnological potential - De Santi_2014_Appl.Biochem.Biotechnol_172_3054
Author(s) : De Santi C , Tedesco P , Ambrosino L , Altermark B , Willassen NP , de Pascale D
Ref : Appl Biochem Biotechnol , 172 :3054 , 2014
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 degrees C and was cold-active with retention of 50% activity at 10 degrees 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.
ESTHER : De Santi_2014_Appl.Biochem.Biotechnol_172_3054
PubMedSearch : De Santi_2014_Appl.Biochem.Biotechnol_172_3054
PubMedID: 24488777

Related information

Citations formats

De Santi C, Tedesco P, Ambrosino L, Altermark B, Willassen NP, de Pascale D (2014)
A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: functional and structural studies and biotechnological potential
Appl Biochem Biotechnol 172 :3054

De Santi C, Tedesco P, Ambrosino L, Altermark B, Willassen NP, de Pascale D (2014)
Appl Biochem Biotechnol 172 :3054

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    [paper] => De Santi_2014_Appl.Biochem.Biotechnol_172_3054
    [author] => De Santi C || Tedesco P || Ambrosino L || Altermark B || Willassen NP || de Pascale D
    [year] => 2014
    [title] => A new alkaliphilic cold-active esterase from the psychrophilic marine bacterium Rhodococcus sp.: functional and structural studies and biotechnological potential
    [journal] => Appl Biochem Biotechnol
    [volume] => 172
    [page] => 3054
    [medline] => 24488777
    [abstract] => De Santi_2014_Appl.Biochem.Biotechnol_172_3054
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            [content] => 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 degrees C and was cold-active with retention of 50% activity at 10 degrees 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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