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Shifting of the distribution of aromatic monomer‐units in polyhydroxyalkanoic acid to longer units by salicylic acid in Pseudomonas fluorescens BM07 grown with mixtures of fructose and 11‐phenoxyundecanoic acid
Author(s) -
Choi Mun Hwan,
Xu Ju,
Rho Jong Kook,
Shim Ji Hoon,
Yoon Sung Chul
Publication year - 2008
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22149
Subject(s) - salicylic acid , chemistry , monomer , acrylic acid , fatty acid , fructose , biochemistry , coenzyme a , pseudomonas fluorescens , stereochemistry , organic chemistry , enzyme , bacteria , biology , reductase , polymer , genetics
Medium‐chain‐length‐polyhydroxyalkanoic acids (MCL‐PHAs) formed in Pseudomonas spp. have a rather broad distribution of monomer‐units whose precursors are supplied via β‐oxidation degradation of MCL fatty acids fed as the carbon source and/or via PhaG enzyme catalyzing the acyl‐group transfer from 3‐hydroxyacyl‐ACPs derived from acetyl‐CoA to coenzyme A. It was found that salicylic acid (SA), in a concentration dependent manner, suppressed the accumulation of PHA in Pseudomonas fluorescens BM07 from fructose as well as shifted the distribution of monomer‐units derived from a MCL fatty acid co‐added as carbon source (e.g., 11‐phenoxyundecanoic acid (11‐POU)) to longer monomer‐units. Both SA and acrylic acid were found to induce high accumulations of 3‐ketohexanoic acid in BM07 wild‐type cells grown with n ‐hexanoic acid as well as to inhibit the formation of acetyl‐CoA from acetoacetyl‐CoA by BM07 cell extract, suggesting that 3‐ketoacyl‐CoA thiolase is their common β‐oxidation target. The structural motif of acrylic acid present in the molecular structure of SA may self‐explain the similar actions of the two inhibitors. A comparison of monomer modulation between BM07 wild‐type and Δ phaG mutant cells grown on the mixtures of fructose and 11‐POU revealed that both PhaG and β‐oxidation inhibitor may play a critical role in the synthesis of PHA with longer side‐chain ω‐functional substitutions. Biotechnol. Bioeng. 2009;102: 1209–1221. © 2008 Wiley Periodicals, Inc.