| Title : Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei - Uchino_2007_J.Biosci.Bioeng_104_224 |
| Author(s) : Uchino K , Katsumata Y , Takeda T , Arai H , Shiraki M , Saito T |
| Ref : J Biosci Bioeng , 104 :224 , 2007 |
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Abstract :
An intracellular 3-hydroxybutyrate-oligomer hydrolase was purified from a poly(3-hydroxybutyrate)-degrading bacterium, Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of Ralstonia eutropha H16. |
| PubMedSearch : Uchino_2007_J.Biosci.Bioeng_104_224 |
| PubMedID: 17964488 |
Uchino K, Katsumata Y, Takeda T, Arai H, Shiraki M, Saito T (2007)
Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei
J Biosci Bioeng
104 :224
Uchino K, Katsumata Y, Takeda T, Arai H, Shiraki M, Saito T (2007)
J Biosci Bioeng
104 :224