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Inhibition of alkaline phosphatase by surfactin, a natural chelating lipopeptide from Bacillus subtilis

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Abstract

Surfactin, an acidic lipopeptide of Bacillus subtilis, at 70 μM non-competitively inhibited alkaline phosphatase without its glycosyl-phosphatidylinositol anchor by 50%. Enzyme activity was restored by adding 50 μM ZnCl 2 and 1 mM MgCl2 confirming the chelating action of the free carboxyl groups of the Asp and Glu residues in the peptide moiety of surfactin.

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Bortolato, M., Besson, F. & Roux, B. Inhibition of alkaline phosphatase by surfactin, a natural chelating lipopeptide from Bacillus subtilis. Biotechnology Letters 19, 433–435 (1997). https://doi.org/10.1023/A:1018387909310

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  • DOI: https://doi.org/10.1023/A:1018387909310

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