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Int J Food Microbiol. 2004 Dec 15;97(2):157-69.

Metabolism of extracellular inositol hexaphosphate (phytate) by Saccharomyces cerevisiae.

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  • 1Department of Chemistry and Bioscience/Food Science, Chalmers University of Technology Box 5401, SE-402 29 Göteborg, Sweden. ta@fsc.chalmers.se

Abstract

Iron and zinc deficiencies are global problems, frequently leading to severe illness in vulnerable human populations. Addition of phytases can improve the bioavailability of iron and zinc in food. Saccharomyces cerevisiae would be an ideal candidate as a bioavailability improving food additive if it demonstrates significant phytase activity. The purpose of the paper was to study yeast phytase activity to obtain information required to improve strains. All yeasts tested readily degraded extracellular inositol hexaphosphate (phytate; IP6) in media with IP6 as the sole phosphorous source. Phosphate (Pi) addition yielded repression consistent with the PHO system. However, repression of IP6-degrading enzymes was not only dependent on level of Pi, but also on pH and medium composition. In complex medium, containing Pi at a concentration previously suggested to yield full repression of the secretory acid phosphatases (SAPs; e.g., [Mol. Biol. Cell 11 (2000) 4309]), and at relatively high pH, repression of phytate-degrading enzymes was weak. The capacity to degrade phytate, irrespective of Pi addition or not, was highest at the pH most distant from the pH optimum of the SAPs [Microbiol. Res. 151 (1996) 291], suggesting that expression rather than enzyme activity was affected by pH. In synthetic medium, repression was strong and pH-independent (no IP6 degradation within the range tested). The distinct difference between media shows that, in addition to known regulatory role of Pi for the PHO system, additional factors may be involved. Using a deletion strain, we further demonstrate that the main secretory acid phosphatase Pho5p is not essential for intact phytate-degrading capacity and growth without Pi, neither is Pho3p. However, when constitutively overexpressing PHO5 an increased net phytase activity was obtained, in repressing and non-repressing conditions. This proves that, although redundant in a wild type, Pho5p can catalyze hydrolysis of IP6 and that at least one more enzyme is capable of effective hydrolysis of IP6 (sufficient to provide the cell with phosphorous at a rate yielding maximum growth). Finally, a bread dough experiment showed that the typical concentrations of Pi during leavening exceed levels shown to repress phytate degradation by a wild-type S. cerevisiae.

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