| Title : The putative lipase, AF1763, from Archaeoglobus fulgidusis is a carboxylesterase with a very high pH optimum - Rusnak_2005_Biotechnol.Lett_27_743 |
| Author(s) : Rusnak M , Nieveler J , Schmid RD , Petri R |
| Ref : Biotechnol Lett , 27 :743 , 2005 |
|
Abstract :
The open reading frame AF1763, annotated as a putative lipase gene (lipA) of the hyperthermophilic archaeon, Archaeoglobus fulgidus DSM 4304, was cloned and over-expressed in E. coli. A sequence analysis of LipA and the investigation of a truncated enzyme implied a special function of the C-terminal part of LipA. The substrate spectrum of the enzyme suggested that LipA is a carboxylesterase rather than a canonical lipase. The enzyme showed optimal activity at 70 degrees C and between pH 10 and 11, which is among the most alkaline pH range detected for hydrolases. |
| PubMedSearch : Rusnak_2005_Biotechnol.Lett_27_743 |
| PubMedID: 16086253 |
Rusnak M, Nieveler J, Schmid RD, Petri R (2005)
The putative lipase, AF1763, from Archaeoglobus fulgidusis is a carboxylesterase with a very high pH optimum
Biotechnol Lett
27 :743
Rusnak M, Nieveler J, Schmid RD, Petri R (2005)
Biotechnol Lett
27 :743