Purification and characterization of extracellular medium-chain-length polyhydroxyalkanoate depolymerase from Pseudomomas sp. RY-1
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- Purification and characterization of extracellular medium-chain-length polyhydroxyalkanoate depolymerase from Pseudomomas sp. RY-1
- Hyun Mean Kim; Kang Eun Ryu; Kyung Sook Bae; Young Ha Rhee
- Bibliographic Citation
- Journal of Bioscience and Bioengineering, vol. 89, no. 2, pp. 196-198
- Publication Year
- A novel bacterial strain capable of growing in a medium containing a medium-chain-length polyhydroxyalkanoate (MCL-PHA) as the sole carbon source was isolated from a soil sample. The isolate, which was identified as Pseudomonas sp. RY-1, secreted MCL-PHA depolymerase into the culture fluid only when it was cultivated in a medium containing a MCL-PHA, such as polyhydroxyoctanoate (PHO) or polyhydroxynonanoate (PHN). The extracellular MCL-PHA depolymerase of this organism was purified to electrophoretic homogeneity. The enzyme was a tetramer with identical subunits and a total molecular mass of 115 kDa. The isoelectric point of this enzyme was estimated to be 5.9 by isoelectric focusing. The maximal activity was observed at pH 8.5 and 35°C. The enzyme was insensitive to phenylmethylsulfonyl fluoride and dithiothreitol, unlike other short-chain-length (SCL) PHA depolymerases. The K(m) values for PHO and PHN were 0.86 and 1.47 mg/ml, respectively. The enzyme could not hydrolyze SCL-PHAs and p-nitrophenyl esters of fatty acids.
- MCL-PHA depolymerasepolyhydroxyalkanoatePseudomonas sp. RY-I
- Soc Bioscience Bioengineering Japan
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- 1. Journal Articles > Journal Articles
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