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Effect of the Phytase Enzyme Extracted from Saccharomyces Cerevisiae on Biofilm Formation by Pathogenic Bacteria

Year: 2025
Type: article
Abstract: Background: Phytases are a large group of enzymes that hydrolyze phytate and its complexes. This most abundant organic phosphate in the world is commonly found in plant-based foods. Objective: The study aimed to investigate the ability of S. cerevisiae. S. yeast extract to investigate the production of biofilm by bacterial isolates (E. coli and Staphylococcus aureus) and its relationship with the phytase enzyme. Methodology: Staphylococcus aureus and Escherichia coli bacteria samples were obtained by isolation and identification from diarrhea samples. Congo Red Agar media and 96-well microplate titer method were used for biofilm detection. Phytase were extracted from Saccharomyces cerevisiae that found in local markets. Biofilm Genes expression (icaA and clfA gene for S. aureus) and (fimH and bcsA for E.coli) were studied. Results: The study showed that the yeast-derived enzyme phytase has an inhibitory effect on biofilm formation in both Staphylococcus aureus and Escherichia coli. In S. aureus, phytase application resulted in a significant decrease in biofilm production and a decrease in the gene expression of both clfA and icaA. In E. coli, phytate exhibited a dose-dependent effect, with light values ​​gradually decreasing with increasing concentration, accompanied by a significant decrease in the expression of fimH and bcsA genes. These results confirm the effectiveness of phytate as a natural biofilm inhibitor in both Gram-positive and Gram-negative bacteria. Conclusion: The results showed that phytase, an enzyme extracted from yeast, has a clear ability to inhibit biofilm formation in both Staphylococcus aureus and E. coli, by reducing biofilm biomass and decreasing the expression of genes related to adhesion and extracellular matrix formation (clfA, icaA, fimH, and bcsA).
Authors: Mais Q. Mohammed, Ahmed H.M. Shugran
Language: English
Open Access status: bronze
OpenAlex ID: W4415911126
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