Summary
The dependence of the production of esterase byPs. aeruginosa on the nutrient medium was studied (a) by supplying esters to nutrient broth and (b) by supplying esters and other C-sources to a mineral medium.
The presence of tributyrin in nutrient broth does not increase the capacity of the cells of splitting tributyrin. Suppression of the esterase activity of the cells was obtained by addition of substances such as oxalate, phosphate, or fluoride which are not toxic for the bacteria and can even stimulate growth. As these compounds do not inhibit directly esterase activity, but prevent lysis of the cells by binding Ca-ions, all these results can be explained by the fact that the esterases ofPs. aeruginosa are endocellular enzymes.
Lipase and ali-esterase seem to play a rather different rôle in the metabolism of bacteria. Lipase activity appears to be adaptive, since certain inducers are necessary for its production, whilePs. aeruginosa appears to be endowed with ali-esterase activity in all the media studied.
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Part I, II: Antonie van Leeuwenhoek23, 241, 273, 1957.
This work was carried out in the Laboratory of Microbiology, Municipal University of Amsterdam, Holland, during the tenure of a grant from the “Consejo Superior de Investigaciones Cientificas”, Spain, and finished during an assistantship at the Laboratory of Microbiology.
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Sierra, G. Studies on bacterial esterases. Antonie van Leeuwenhoek 23, 278–288 (1957). https://doi.org/10.1007/BF02545880
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DOI: https://doi.org/10.1007/BF02545880