1887

Abstract

The poly(amino acid)s -poly(-glutamic acid) (gPGA) and ϵ-poly(-lysine) (ePL) are known to be natural linear poly(amino acid)s secreted by spp. and spp., respectively. In this study, a strain producing both ePL and gPGA was identified. Mass spectrometry and other analyses revealed that the gPGA is a mixture of oligomers consisting of 10–13 -glutamic acid residues linked by isopeptide bonds. In contrast to the known gPGA, the glutamic acid oligomers have a cyclodehydrated structure in each molecule. We previously reported that the ePL molecules secreted by the same strain disperse only slightly in an agar culture plate, as though they were larger molecules. This phenomenon is explicable by the observed polyion complex formation between the glutamic acid oligomers and ePLs. The glutamic acid oligomers control the ePL's dispersion, which would also affect the spatial distribution of the ePL's antimicrobial activity. Therefore, gene clustering or common use of the gene was presumed for biosynthesis of the two poly(amino acid)s. However, no gene for biosynthesis of the glutamic acid oligomer was found in the neighbouring region of that for ePL biosynthesis, and the glutamic acid oligomer was produced by a mutant in which the ePL biosynthetic gene was inactivated by gene disruption.

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2009-09-01
2020-05-26
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