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Title 

Characterization of an extracellular medium-chain-length poly(3-hydroxyalkanoate) depolymerase from Streptomyces sp. KJ-72

Authors 

H J KimD Y KimJ S NamKyung Sook BaeY H Rhee

Publisher 

Springer Verlag (Germany)

Issue Date 

2003

Citation 

Antonie Van Leeuwenhoek, vol. 83, no. 2, pp. 183-189

Keywords 

medium-chain-length polyhydroxyalkanoatepolyhydroxyalkanoate depolymerasestreptomyces sp. KJ-72poly(3 hydroxyalkanoate)depolymerasepolycaprolactoneculture mediumspecies differencestreptomycespolyesterssubstrate specificity

Abstract 

A bacterial strain capable of degrading medium-chain-length polyhydroxyalkanoates (MCL-PHAs) was isolated from a soil sample. This organism, which was identified as Streptomyces sp. KJ-72, secreted MCL-PHA depolymerase into the culture fluid only when it was cultivated on MCL-PHAs. The extracellular MCL-PHA depolymerase of the organism was purified to electrophoretic homogeneity by ion exchange column chromatography and gel filtration. The enzyme consisted of a monomeric subunit having a molecular mass of 27.1 kDa and isoelectric point of 4.7. The maximum activity was observed at pH 8.7 and 50 °C. The enzyme was sensitive to N-bromosuccinimide and acetic anhydride, indicating the presence of tryptophan and lysine residues in the catalytic domain. The enzyme was able to hydrolyze various chain-length p-nitrophenyl esters of fatty acids and polycaprolactone as well as various types of MCL-PHAs. However, lipase activity of the enzyme was not detected. The main hydrolysis product of poly(3-hydroxyheptanoate) was identified to be the dimer of 3-hydroxyheptanoate.

ISSN 

0003-6072

Link 

http://dx.doi.org/10.1023/A:1023395527073

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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