Abstract
Due to their diverse bioactive effects, prodigiosin and its analogues (prodiginines) have attracted a great deal of attention. In this study, a prodigiosin synthetase PigC catalyzing a condensation reaction to produce prodigiosin was cloned from Serratia marcescens jx-1 and overexpressed in Escherichia coli with a putative polypeptide of 888 amino acids. Its biochemical properties and applications in prodiginines synthesis were investigated. The purified enzyme had a specific activity of 6.96 U/mg and exhibited optimal activity at 10 °C and pH 7.5. The recombinant PigC performed good stability below 30 °C and at pH ranging from 6.0 to 8.5. This enzyme was activated by Ca2+, while inhibited by Cu2+. The kinetic analysis with 4-methoxy-2,2′-bipyrrole-5-carboxyaldehyde (MBC) and 2,4-dimethyl-3-ethylpyrrole (DMEP) as substrates yielded apparent Km of 23.4 and 4.2 μmol/L, respectively. The enzymatic catalysis using whole cells of recombinant E. coli harboring the PigC as catalyst in an aqueous organic solvent system resulted in 59.4% yield of prodigiosin analogues, which exhibited excellent antimicrobial properties against Staphylococcus aureus, Bacillus subtilis and E. coli. The results obtain here demonstrated the great potential of PigC for the biosynthesis of prodigiosin and its analogues.
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