Abstract
Genome shuffling technology was used as a novel whole-genome engineering approach to rapidly improve the antimicrobial lipopeptide yield of Bacillus amyloliquefaciens. Comparative proteomic analysis of the parental ES-2-4 and genome-shuffled FMB38 strains was conducted to examine the differentially expressed proteins. The proteome was separated by 2-DE (two dimensional electrophoresis) and analyzed by MS (mass spectrum). In the shuffled strain FMB38, 51 differentially expressed protein spots with higher than two-fold spot density were detected by gel image comparison. Forty-six protein spots were detectable by silver staining and further MS analysis. The results demonstrated that among the 46 protein spots expressed particularly induced in the genome-shuffled mutant, 15 were related to metabolism, five to DNA replication, recombination and repair, six to translation and post-translational modifications, one to cell secretion and signal transduction mechanisms, three to surfactin synthesis, two to energy production and conversion, and 14 to others. All these indicated that the metabolic capability of the mutant was improved by the genome shuffling. The study will enable future detailed investigation of gene expression and function linked with surfactin synthesis. The results of proteome analysis may provide information for metabolic engineering of Bacillus amyloliquefaciens for overproduction of surfactin.
Highlights
Bacillus strains produce many types of bioactive lipopeptides that are synthesized non-ribosomally by a large multifunctional enzyme complex
Strains of B. amyloliquefaciens and found 51 protein spots that differed between the strains by more than two-fold (Figure 1)
Searching of the National Center for Biotechnology Information (NCBI) nr database with Mascot revealed that protein spots
Summary
Bacillus strains produce many types of bioactive lipopeptides that are synthesized non-ribosomally by a large multifunctional enzyme complex. The lipopeptide surfactin is well characterized at the genetic level. Surfactin is biosynthesized by three non-ribosomal peptide synthetases, SrfA–C, and by the thioesterase/acyltransferase enzyme SrfD, which initiates this process. Surfactin is a powerful biosurfactant that is known to decrease the surface tension of water [1]. It exerts a detergent-like action on biological membranes, and is distinguished by its emulsifying, foaming, antiviral and anti-mycoplasma activities. Surfactin has many potential applications in plant disease biocontrol [2] and biomedicine [3]
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