Extracellular lipases from Bacillus subtilis: regulation of gene expression and enzyme activity by amino acid supply and external pH.

Thorsten Eggert, Ulf Brockmeier, Melloney J Dröge, Wim J Quax, Karl-Erich Jaeger

Index: FEMS Microbiol. Lett. 225(2) , 319-24, (2003)

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Abstract

Bacillus subtilis secretes two lipases LipA and LipB into the culture medium. Both enzyme genes were differentially expressed depending on the growth conditions as determined by activity assays and Western blotting in B. subtilis mutant strains lipA, lipB, and the corresponding lipA/lipB double mutant. In minimal medium, LipA was produced at wild-type level in a lipB mutant, however, no LipB protein was detected in a lipA mutant. Interestingly, LipA was produced and secreted at wild-type level in rich medium, but the enzyme remained enzymatically inactive, presumably being caused by a shift of the growth medium to acid pH. Furthermore, expression of the lipase genes was studied using transcriptional fusions with the lacZ reporter gene. The expression of lipA was repressed by high amino acid concentrations, whereas the lipB gene expression remained unaffected.