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Appl Environ Microbiol. 1989 January; 55(1): 233-239

Immunoelectron microscopic demonstration of an esterase on the outer membrane of Xanthomonas maltophilia.

Laboratoire de Microbiologie, U.F.R., de Biologie, Université des Sciences et Techniques de Lille Flandres et Artois, Villeneuve D'Ascq, France.

ABSTRACT

Xanthomonas maltophilia (later synonym of Pseudomonas maltophilia), an ubiquitous species, is known to show proteolytic and lipolytic activities. A cell-bound esterase which hydrolyzes beta-naphthyl acetate during growth has been extracted from a strain isolated from soil. Because of its strongly hydrophobic character, the enzyme could be efficiently solubilized only by Triton X-100. This nonionic detergent must be added in polyacrylamide gels to permit migration. Polyclonal rabbit antibodies raised against the Triton-soluble esterase complex were used to localize the enzyme at the ultrastructural level. Electron microscopy of cell sections of this organism and immunogold labeling demonstrated that the enzyme was located on the outer membrane. Such an envelope-bound esterase may produce assimilable substrates for X. maltophilia which can grow in various environments.

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