Open AccessIdentification of the intracellular polyhydroxyalkanoate depolymerase gene of Paracoccus denitrificans and some properties of the gene product
Author(s) -
Gao Dai,
Maehara Akira,
Yamane Tsuneo,
Ueda Shunsaku
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10558.x
Subject(s) - paracoccus denitrificans , polyhydroxyalkanoates , biochemistry , escherichia coli , intracellular , gene product , polyhydroxybutyrate , biology , bacteria , chemistry , gene , microbiology and biotechnology , gene expression , enzyme , genetics
Paracoccus denitrificans degraded poly(3‐hydroxybutyrate) (PHB) in the cells under carbon source starvation. Intracellular poly(3‐hydroxyalkanoate) (PHA) depolymerase gene ( phaZ ) was identified near the PHA synthase gene ( phaC ) of P. denitrificans . Cell extract of Escherichia coli carrying lacZ–phaZ fusion gene degraded protease‐treated PHB granules. Reaction products were thought to be mainly d (−)‐3‐hydroxybutyrate (3HB) dimer and 3HB oligomer. Diisopropylfluorophosphonate and Triton X‐100 exhibited an inhibitory effect on the degradation of PHB granules. When cell extract of the recombinant E. coli was used, Mg 2+ ion inhibited PHB degradation. However, the inhibitory effect by Mg 2+ ion was not observed using the cell extract of P. denitrificans .