SUMMARY: Various mutants () of PAO 2302 that lacked extracellular lipase activity were isolated. They were selected on a calcium-triolein agar. The phenotypic characteristics of two of these mutants suggested that they were defective in the gene coding for lipase: both mutants produced no lipase in liquid- and on solid medium. They were non-pleiotropic with regard to various other exoproducts. None of the mutants released any putatively cell-bound lipase after treatment of cells with Triton X-100 or alginate. The electrophoretic protein- and LPS-profiles of outer membranes derived from mutants and the parental strain were identical. The locus was mapped on the chromosome of PAO 1 by FP5- and R68.45-mediated crossings and by transduction with phage G101. The locus was cotransduced with only (60%) indicating a map position at about 57 min. The lipase gene was cloned on a 3.1 kb I fragment using vector pKT248. The newly constructed plasmid was able to complement the lipase deficiency of the two mutants of


Article metrics loading...

Loading full text...

Full text loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error