Abstract
Pb2+inhibited calcium-induced flocculation in Flo1 (S646–1B) and NewFlo phenotype strains (NCYC 1190, NCYC 1195 and NCYC 1364) of Saccharomyces cerevisiae. Flocculation was restored after washing with water or EDTA, which suggests a reversible binding of Pb2+to yeast cell walls. Pb2+probably inhibited flocculation by competing with Ca2+, since Pb2+inhibition was alleviated by excess of Ca2+. Using a fluorescent avidinfluorescein isothiocyanate (Avidin-FITC) probe, active cell surface flocculation lectins, in the presence of Ca2+ions, were visualized. Conversely, Avidin-FITC was not fixed to yeast walls of flocculent cells, in the presence of Pb2+ions or in the simultaneous presence of 0.05 mM Ca2+and 0.4 mM Pb2+. These results suggest that Pb2+ions were not able to induce the correct conformation of the lectin-like component and reinforces the hypothesis that Pb2+ions compete for the same “calcium site” of flocculation zymolectins.
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